ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q969X2 | MACSRPPSQCEPTSLPPGPPAGRRHLPLSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRSRRPVNLKKWSITDGYVPILGNKTLPSRCHQCVIVSSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTYRVVAHSSVFRVLRRPQEFVNRTPETVFIFWGPPSKMQKPQGSLVRVIQRAGLVFPNMEAYAVSPGRMRQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPNYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWA... | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid ... |
Q92185 | MSPCGRARRQTSRGAMAVLAWKFPRTRLPMGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLQQGTAWRRNQTAARAFRKQMEDCCDPAHLFAMTKMNSPMGKSMWYDGEFLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEANFVMRCNLPPLSSEYTKDVGSKSQLVTANPSIIRQRFQNLLWSRKTFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLSDVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSVNMHEQPISHHYYDNVLPFSG... | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Can catalyze the addition of a second alpha-2,8-sialic acid to GD3 ... |
Q64687 | MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLAQRTAWRTNQTSASLFRRQMEDCCDPAHLFAMTKMNSPMGKSLWYDGELLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGY... | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Can catalyze the addition of a second alpha-2,8- sialic acid to GD3... |
Q6ZXA0 | MWGRWRGAGGRRGVAQPVIPQMKLLGGRVPLGASALGLLIVCWFYIFPGGERLPGHKEMIRQVLQFGPRWGRNRSSGDSFRKLLQDCCDPPRLFSMTKANTALGENLWYDGEFFQSLTIDNTTRSLFPQDTPIKLPLKRCSVVGNGGILKNSRCGEQIDEADFVMRCNLPPLSREYTDDVGTKTQLVTVNPSIIDKRFQNLLWSRKSFVESVSVYKQSYVYMPAFSTKRGTDPSLRVYYTLEDFGTNQTVLFANPNFLRNVGKFWKSKGVHSKRLSTGLFMVSAALSLCEEVTIYGFWPFQMDLGGRHISHHYYDNMLPL... | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Glycosphingolipids are required for convergence extension movements... |
Q6DNG6 | MKLQGSRMWLCPRTRLPVGASALGFLILCWLYVFPGYRLPGHKEMVREVLRFGPGWRKNRTEMDSFRKLLQDCCDPPHLFSLTKVNTPLGENLWFDGEFFHSLTIDNSTRSLFPQDTPFKLPLKRCSVVGNGGILKNSRCGEQIDEADFVMRCNLPPLSREYTEDVGTRTQLVTVNPSIIDKRYQNLLWSRKSFVENLRVYQQSYVYMPAFSTKRGTDPSLRVYYTLADFGTNQTVLFANPNFLRNVGKFWKSRGIHSKRLSTGLFMVSAALSLCEEVTIYGFWPFQMDLGGRYISHHYYDNTLPLSGVHAMPEEFLQLW... | Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid (By similarity). Glycosphingolipids are required for convergence exte... |
Q92186 | MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSSPAVVDRSNESIKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFGTCAIVGNSGVLLNSGCGQEIDAHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHSLNGSILWIPAFMARGGKERVEWVNELILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCKQIYLYGFWPFPL... | Function: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42430
Sequence Length:... |
Q91Y57 | MLLLLLLLLLWGIKGVEGQNPQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVSYAPKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGV... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting c... |
Q64JA4 | MLPLLLPLLWAGALALEGIFQLEVPESVTVQEGLCVFVPCTFFYPRHTFIKISLACGYWFREGDNPLRDAPVATNDPARQVREETRGRFRLLGNPREKNCSLSIRDARRRDSGSYFFRVEEAMMKYNYKDPPLSVHVTALTHRPDILIPGALKSGRPRNLVCSVPWACEQGTPPIFSWIGTSVSPLSPTTALSSVVTLIPQPQDHGSRLTCQVTLPGAGVTTTRTVRLNVSYPPQNLTLTVFQGDGTASTTLRNESSLQVLEGQSLRLVCAVDSNPPARLSWAQDNLILSPSQPNPGMLELPQMHLRNEGEFTCQARNPL... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 42525
Sequence Length: 387
Subcellular Location: Membrane
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Q08ET2 | MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQVKRQGAQVTTERTVQLNVSYAPQNLAISIFFRNGTGTALRILSNGMSVPIQEGQSLFLACTVDSNPPASLSWFREGKALNPSQTSMSGTLELPNIGAREGGEFTCR... | Function: Putative adhesion molecule. Sialic acid-binding paired receptor which may activate associated receptors.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43970
Sequence Length: 396
Subcellular Location: Cell membrane
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Q6ZMC9 | MEKSIWLLACLAWVLPTGSFVRTKIDTTENLLNTEVHSSPAQRWSMQVPPEVSAEAGDAAVLPCTFTHPHRHYDGPLTAIWRAGEPYAGPQVFRCAAARGSELCQTALSLHGRFRLLGNPRRNDLSLRVERLALADDRRYFCRVEFAGDVHDRYESRHGVRLHVTAAPRIVNISVLPSPAHAFRALCTAEGEPPPALAWSGPALGNSLAAVRSPREGHGHLVTAELPALTHDGRYTCTAANSLGRSEASVYLFRFHGASGASTVALLLGALGFKALLLLGVLAARAARRRPEHLDTPDTPPRSQAQESNYENLSQMNPRS... | Function: Binds sialylated glycoproteins.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35653
Sequence Length: 328
Subcellular Location: Membrane
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A6NMB1 | MLLLPLLLPVLGAGSLNKDPSYSLQVQRQVPVPEGLCVIVSCNLSYPRDGWDESTAAYGYWFKGRTSPKTGAPVATNNQSREVAMSTRDRFQLTGDPGKGSCSLVIRDAQREDEAWYFFRVERGSRVRHSFLSNAFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFKKCPAPSFSWTGAALSPRRTRPSTSHFSVLSFTPSPQDHDTDLTCHVDFSRKGVSAQRTVRLRVASLELQGNVIYLEVQKGQFLRLLCAADSQPPATLSWVLQDRVLSSSHPWGPRTLGLELPGVKAGDSGRYTCRAENRLGSQQRALD... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 52992
Sequence Length: 481
Subcellular Location: Membrane
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O15389 | MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMKRQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALRLLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRAQHPL... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Location Topology: Single-pass type I membrane pro... |
Q920G3 | MRWAWLLPLLWAGCLATDGYSLSVTGSVTVQEGLCVFVACQVQYPNSKGPVFGYWFREGANIFSGSPVATNDPQRSVLKEAQGRFYLMGKENSHNCSLDIRDAQKIDTGTYFFRLDGSVKYSFQKSMLSVLVIALTEVPNIQVTSTLVSGNSTKLLCSVPWACEQGTPPIFSWMSSALTSLGHRTTLSSELNLTPRPQDNGTNLTCQVNLPGTGVTVERTQQLSVIYAPQKMTIRVSWGDDTGTKVLQSGASLQIQEGESLSLVCMADSNPPAVLSWERPTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTAS... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Location Topology: Single-pass type I membrane protein
Sequence ... |
O43699 | MQGAQEASASEMLPLLLPLLWAGALAQERRFQLEGPESLTVQEGLCVLVPCRLPTTLPASYYGYGYWFLEGADVPVATNDPDEEVQEETRGRFHLLWDPRRKNCSLSIRDARRRDNAAYFFRLKSKWMKYGYTSSKLSVRVMALTHRPNISIPGTLESGHPSNLTCSVPWVCEQGTPPIFSWMSAAPTSLGPRTTQSSVLTITPRPQDHSTNLTCQVTFPGAGVTMERTIQLNVSYAPQKVAISIFQGNSAAFKILQNTSSLPVLEGQALRLLCDADGNPPAHLSWFQGFPALNATPISNTGVLELPQVGSAEEGDFTCR... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 4991... |
Q9Y286 | MLLLLLLPLLWGRERVEGQKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRAGNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDAGRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQVTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLEGQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEFTC... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recog... |
Q9NYZ4 | MLLLLLLLPLLWGTKGMEGDRQYGDGYLLQVQELVTVQEGLCVHVPCSFSYPQDGWTDSDPVHGYWFRAGDRPYQDAPVATNNPDREVQAETQGRFQLLGDIWSNDCSLSIRDARKRDKGSYFFRLERGSMKWSYKSQLNYKTKQLSVFVTALTHRPDILILGTLESGHSRNLTCSVPWACKQGTPPMISWIGASVSSPGPTTARSSVLTLTPKPQDHGTSLTCQVTLPGTGVTTTSTVRLDVSYPPWNLTMTVFQGDATASTALGNGSSLSVLEGQSLRLVCAVNSNPPARLSWTRGSLTLCPSRSSNPGLLELPRVHV... | Function: Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells . Preferentially binds to alpha-2,3-linked sialic acid. Also binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface . Recogniz... |
P03528 | MDPRLREEVVRLIIALTSDNGASLSKGLESRVSALEKTSQIHSDTILRITQGLDDANKRIIALEQSRDDLVASVSDAQLAISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTELSTLTLRVTSIQADFESRISTLERTAVTSAGAPLSIRNNRMTMGLNDGLTLSGNNLAIRLPGNTGLNIQNGGLQFRFNTDQFQIVNNNLTLKTTVFDSINSRIGATEQSYVASAVTPLRLNSSTKVLDMLIDSSTLEINSSGQLTVRSTSPNLRYPIADVSGGIGMSPNYRFRQSMW... | Function: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to ind... |
P04507 | MSDLVQLIRREILLLTGNGESANSKHEIEEIKKQIKDISADVNRISNIVDSIQGQLGGLSVRVSAIESGVSENGNRIDRLERDVSGISASVSGIDSRLSELGDRVNVAEQRIGQLDTVTDNLLERASRLETEVSAITNDLGSLNTRVTTELNDVRQTIAAIDTRLTTLETDAVTSVGQGLQKTGNSIKVIVGTGMWFDRNNVLQLFLSNQQKGLGFIDNGMVVKIDTQYFSFDSNGNITLNNNISGLPARTGSLEASRIDVVAPPLVIQSTGSTRLLRLMYEAVDFVVTNNVLTLRNRSVTPTFKFPLELNSADNSVSIH... | Function: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to ind... |
P04506 | MDASLITEIRKIVLQLSVSSNGSQSKEIEEIKKQVQVNVDDIRAANIKLDGLGRQIADISNSISTIESRLGEMDNRLVGISSQVTQLSNSVSQNTQSISSLGDRINAVEPRVDSLDTVTSNLTGRTSTLEADVGSLRTELAALTTRVTTEVTRLDGLINSGQNSIGELSTRLSNVETSMVTTAGRGLQKNGNTLNVIVGNGMWFNSSNQLQLDLSGQSKGVGFVGTGMVVKIDTNYFAYNSNGEITLVSQINELPSRVSTLESAKIDSVLPPLTVREASGVRTLSFGYDTSDFTIINSVLSLRSRLTLPTYRYPLELDTA... | Function: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to ind... |
Q8L607 | MVMMLKKTVKKGLIGGMSFAKDAGKINWFPGHMAAATRAIRNRLKLSDLVIEVRDARIPLSSANEDLQSQMSAKRRIIALNKKDLANPNVLNKWTRHFESSKQDCIAINAHSRSSVMKLLDLVELKLKEVIAREPTLLVMVVGVPNVGKSALINSIHQIAAARFPVQERLKRATVGPLPGVTQDIAGFKIAHRPSIYVLDSPGVLVPSIPDIETGLKLALSGSVKDSVVGEERIAQYFLAILNIRGTPLHWKYLVEGINEGPHADCIDKPSYNLKDLRHQRTKQPDSSALHYVGDMISEVQRSLYITLSEFDGDTEDEND... | Function: GTPase that may function in mitochondrial ribosome assembly (Probable). Involved in a variety of growth processes during vegetative development and promotes growth and cell division in the developing integuments .
Sequence Mass (Da): 42984
Sequence Length: 386
Domain: In contrast to other GTP-binding proteins... |
P93748 | MAPGGSALKEALESNSTGVDYEVKMAKVEANSKPTKSGSGSIGKFHSSNGVYELLECPVCTNLMYPPIHQCPNGHTLCSSCKLRVQNTCPTCRYELGNIRCLALEKVAESLEVPCRYQNLGCQDIFPYYSKLKHEQHCRFRSYSCPYAGSECSVTGDIPTLVDHLKDDHKVDMHDGCTFNHRYVKSNPHEVENATWMLTVFNCFGRQFCLHFEAFQLGMAPVYMAFLRFMGDENEAKKFSYSLEVGAHSRKLTWQGIPRSIRDSHRKVRDSQDGLIIPRNLALYFSGSDKEELKLRVTGRIWKEE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins . E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . It probably triggers ... |
Q9M2P4 | MAPGGSALKEVMESNSTGMDYEVKTAKVEVNNNKPTKPGSAGIGKYGIHSNNGVYELLECPVCTNLMYPPIHQCPNGHTLCSNCKLRVQNTCPTCRYELGNIRCLALEKVAESLEVPCRYQNLGCHDIFPYYSKLKHEQHCRFRPYTCPYAGSECSVTGDIPTLVVHLKDDHKVDMHDGCTFNHRYVKSNPHEVENATWMLTVFNCFGRQFCLHFEAFQLGMAPVYMAFLRFMGDENEAKKFSYSLEVGAHGRKLTWQGIPRSIRDSHRKVRDSQDGLIIPRNLALYFSGGDRQELKLRVTGRIWKEE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins . E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . It probably triggers ... |
Q9STN8 | METDSMECVSSTGNEIHQNGNGHQSYQFSSTKTHGGAAAAAVVTNIVGPTATAPATSVYELLECPVCTYSMYPPIHQCHNGHTLCSTCKVRVHNRCPTCRQELGDIRCLALEKVAESLELPCKFYNLGCPEIFPYYSKLKHESLCNFRPYSCPYAGSECGIVGDIPFLVAHLRDDHKVDMHAGSTFNHRYVKSNPREVENATWMLTVFHCFGQYFCLHFEAFQLGMGPVYMAFLRFMGDEEDARSYSYSLEVGGSGRKLTWEGTPRSIRDSHRKVRDSNDGLIIQRNMALFFSGGDRKELKLRVTGKIWKEQHSPDSGLS... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins . E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . It probably triggers ... |
Q8S3N1 | METDSIDSVIDDDEIHQKHQFSSTKSQGGATVVISPATSVYELLECPVCTNSMYPPIHQCHNGHTLCSTCKSRVHNRCPTCRQELGDIRCLALEKVAESLELPCKYYNLGCLGIFPYYSKLKHESQCNFRPYSCPYAGSECAAVGDITFLVAHLRDDHKVDMHTGCTFNHRYVKSNPREVENATWMLTVFQCFGQYFCLHFEAFQLGMAPVYMAFLRFMGDEDDARNYTYSLEVGGSGRKQTWEGTPRSVRDSHRKVRDSHDGLIIQRNMALFFSGGDKKELKLRVTGRIWKEQQNPDSGVCITSMCSS | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins . E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . Mediates the ubiquiti... |
Q8T3Y0 | MSVRNSRPQLSWPERVSPQRTIDTPTASGEMLTRRQSAPALVVPPEETTHVVVVKRQSPDAAAAGELVPSRRKDSVAVQSGIVATGPLDTTRSGARDDFLMALLECPVCFGYIMPPIMQCPRGHLICSTCRSKLTICPVCRVFMTNIRSLAMEKVASKLIFPCKHSHFGCRARLSYAEKTKHEEDCECRPYFCPYPDDKCSWQGPLRDVYQHLMSSHENVITMEGNDIIFLATNVNLEGALDWTMVQSCHGRHFLLSLEKINLGEDCQQYFTACRMIGSMKDAAEFVYNISLEAYNRTLRWQSKPRSIRENFSSFTNADF... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. The adapter phyl is required to direct the degradation of the two isoforms of the transcriptional repressor Tramtrack (Ttk). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugatin... |
P21461 | MSNKINPKRREPTAAAAGAGATGVATNTSTSTGSSSAGNTSSANTSSSSSSSLSSAGGGDAGMSADLTSLFECPVCFDYVLPPILQCSSGHLVCVSCRSKLTCCPTCRGPLANIRNLAMEKVASNVKFPCKHSGYGCTASLVYTEKTEHEETCECRPYLCPCPGASCKWQGPLDLVMQHLMMSHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYDGHQQFFAIVQLIGSRKEAENFVYRLELNGNRRRLTWEAMPRSIHEGVASAIHNSDCLVFDTSIAQLFADNGNLGINVTISLV | Function: E3 ubiquitin-protein ligase that is required for specification of R7 photoreceptor cell fate in the eye by mediating the ubiquitination and subsequent proteasomal degradation of Tramtrack (ttk) . E3 Ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then ... |
Q62231 | MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQSNMGHARSSNYSLPGLTASQPSHGLQAHQHQLQDSLLGPLTSSLVDLGS | Function: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development . Plays an important role in the development of several organs, including kidney, muscle and inner ear . Depending on context, functions as transcriptional repressor or activator . Lacks an activ... |
Q26292 | MKLLLLLIVSASMLIESLVNADGYIKRRDGCKVACLIGNEGCDKECKAYGGSYGYCWTWGLACWCEGLPDDKTWKSETNTCGGKK | Function: Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneo... |
Q5NTH4 | MEAGVGLALQSRAAGFGGSDRRRSALYGGEGRARIGSLRVAEPAVAKAAVWARGSKPVAPLRAKKSSGGHETLHNSVDEALLLKRKSEEVLFYLNGRCIYLVGMMGSGKSTVGKIMSEVLGYSFFDSDKLVEQAVGMPSVAQIFKVHSEAFFRDNESSVLRDLSSMKRLVVATGGGAVIRPVNWKYMKKGLSVWLDVPLDALARRIAKVGTASRPLLDQPSGDPYTMAFSKLSMLAEQRGDAYANADVRVSLEEIASKQGHDDVSKLTPTDIAIESFHKIENFVIEHTVDNPVGDSQADSRAQRIQTL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 33310
Sequence Length: 308
Pathway: Metabolic intermediate biosynthesi... |
O31423 | MSYDRVKDFDLPELAVHLQPHGAVMIDRKSMFYFRLSGRGAQLAFLLSKNKNLHKTARIWEIMKKEEMSADQLKEELSAHPFTEAWTEGLLDQPLHVSGSLDSYLPISCTLQLTNACNLSCSFCYASSGKPYPEELSSEQWILVMQKLAAHGVADITLTGGEAKLIKGFKELVVVASSLFTNVNVFSNGLNWRDEEVELLSHLGNVSVQISIDGMDNTHDQLRGRKGGFKESMNTIKKLSEANIPVIVAMTINESNADEVSDVVEQCANAGAFIFRAGKTLSVGRATEGFKALDIDFEEMVQIQLREARHKWGDRLNIID... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine . The other is coordinated via 3 cysteines and maybe direct contact with the SkfA precursor (Probable).
Function: Catalyzes the formation of the thioether bond required for production of the spor... |
O31425 | MNSLSLVFWSILAVVGLLLFIKFKPPTIASLLLSKDEAKEISIQFIKEFVGIDVENWDFYSVYWYDHDTVNKLHHLGILKKNRKVLYDVGLVESWRVRFVHQNQSFVVGVNANREITFFYADVPKKTLSGKFEQVSPETLKQRLMASPDGLWSRANMTGTGKKEEDFREVSTYWYIAEAGDIRLKVTVELQGGRISYIGTEQEILTDQMSKVIRDEQVESTFGVSGMLGSALAMILAILILVFMDVQTSIIFSLVLGLLIIICQSLTLKEDIQLTIVNAYDARMSVKTVSLLGILSTLLTGLLTGFVVFICSLAGNALAG... | Function: Required for production of the bacteriocin SkfA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56292
Sequence Length: 496
Subcellular Location: Membrane
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O31427 | MQLMQVQNLSKCYRNGDGVEHLSFSIQRGEIVALLGPNGAGKTTTIRCLTGLYKPDKGDILIEGSPPGDINVQKKVALIPDQPYLYPALTAAEHIQFRARGYHPGKKDVKERVYHALKEVHLEEKANQLCGQLSRGQKQRVVLAGAIVQDALLYILDEPTVGLDIPSKQWLSNWLKTKTDQGCSAFVSTHSLEFVIETADRVILIRDGKLMQDLYVPQFEEQAEWRKEVIRLLGEWSDE | Function: Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 268... |
O31428 | MPFLIMLLFVGAIGFQVSFVSRSTTWDMSIAGWVLTGVFILYTAFGLFSNRLPSQMADIIWLYGTATSFSKVVYSVLFFSVTWKALLWIISAIFGDVLIVLLSGDHINLLGRSIIFVGLFFIAEVWLMSVSCARTVKKMKRVYVLVFLLMLGIYSICLYRFFFLQHSSGIWESIARFISGVGLVFDTLSPLYVVVFIGIITVSFMTIAFTSRQVEMKESLVKEAEFWEEFQERQFGSGQIIQKPKTTWWGLQGLNGIWSFLWLELLLFKKYLFFHSIHTVMLSGVFYVVIFMYPEWFYLLFFLIVSAVMLSSYYSGIVRH... | Function: Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for the translocation of bacteriocin SkfA across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51817
Sequence Length: 447
Subcellular Location: Cell membrane
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Q753L2 | MAVDTTTVAVALAVVLPVSIAVLIALVFWCKTQRRFKREEQDDEKNRGYDDEVVTFREMRASSGTLGPDGTPPTACAEGSGSSEGSESEKDPSPTPAPAGRAARTYMPAYRRRLNRSLSRQQSRADEMTTNSSAASYDTQHAQNAQLSVFEQMVPVLQVDNSSPFANPRDAAFERGSRHSSESLMKSLKNQDFGSYPKRRPSAANTANLAVYNGSVSSFSSRVPSSTTLNCMGDESFYAYEGSVLPRTGRDLPEVKQDVYMLKNNYDVTNNEEITEEDQYENEFTNYSENKREFIDSLRPKAERMSN | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 34105
Sequence Length: 307
Subcellular Location: Cell membrane
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Q6FLL2 | MTGTVSTAVGCAVGIPVGVGVIVACLFWIRMQRRLKEEDIIDQELNRAVYDESGFVSFNNIDTLKAEPNGHPSSEDTNEVMHSSDIDDNGDDDDEDHNARRNNTYAAQDKNNGKYVPAYRRQINKHNSILQQQRKSRNLVNTMGHSIESLSMDDHSQANGKSRQVSVYDQMVPVLDDANRDSSSPFPTNDKDTSDKKSNLFQSHDVSANTSTSFFETRSNDNLIKNLNSHDFGSYYPRRPSTSNLNHSQGSLHTRNSSMLSLGKIENAENVFATPKSENILKHPHPLEHESSSISNETNNVTDNTIDGESASKSSKTYQL... | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 40439
Sequence Length: 360
Subcellular Location: Cell membrane
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C5DH21 | MTDGLGVSVGCAVGIPCGVAVLVAVIFWYYMQRKFKKEIEDDEESMSGDGTISFTNLHSMRVPDNPEKDLPVSHVVGGSTSSDNTTTAQNVATAGQMEAQQSQPSKKPKNTYMPAYRKRLNSSLSTLQHQDEQRSPTDSSSTSLDTKNQNGRAHSTVLDQMIPVLAQDDNAAAASSEFSLTHERTSSNDNLIKNLHNHDFGSYPKRRSSGNLTGMISGNVSSASVHTRTSSVHSGKKNNENVFDTPNSQKFHEAVAPSEEDAESKGMRSYYMLKNNYDVENASQIAEEDQYENEFTNYSESKREFINSLRPKKN | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 34636
Sequence Length: 314
Subcellular Location: Cell membrane
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A7TSZ6 | MVASNSVAVGCAVGIPVGVGLIIAGCFWLRLQRRFKREDEQDADLQRAVFDEDAYINFESMPTLRNNNNNDEDNNDDKRIKKIEENGNENTIPINDNKEQRKSKYFVPAYRRKINALSVRYDGQQNIEMQGFGANSSKVSLDSSNAPPKRVISVYDQMVPFVDGDKNSVIQNTELLESNDSVGNDSTRPSSQANLISNLNSNDFGSYYPRKESFSSINIPHLNTSSPSFTTRPSSVNSMIRPNSTDNIFDTPRKSNSDIVSINKDQVNRTGSPVKGTVISENMGYKLKNNYNIENSNEIAEEDQYENEFTNYSQNKKEFI... | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 36744
Sequence Length: 326
Subcellular Location: Cell membrane
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B3LRH5 | MTASTSVAVGCAVGIPVGVGIIIAVCFWFNLQKRYKREEQDDRELERAIYDESGFVSFDNFGPLRDSKDEAALASSELKNPDHTSGSSEGSAHPEEKDGKSRDQEKPLGKKNSKYYVPAYRRKINLLQVRNNNYGNNARQKSVVDLPSINNSSNVSLSSSQRHITKRQISVYDQMVPVISDEGPKFFADPSSDTNTSNDQNKASMIELKHNTRQSSNENLIRKLQNQDFGSYYPRRASSSFLNGNISNASFHTRNSSITSVNKRDALEDVFATPKSAAQSQLPNTFDKDNEGIDADHSVKDSRSAITDKDKNIYKLQNNY... | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 39839
Sequence Length: 355
Subcellular Location: Cell membrane
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C5DSG3 | MGDVSIAVGCAVGLPVGLSFLLAIVFWIRMQRRYKKEDARDCELENIIRDESGFISFDNLGTWQETQQEKKDVYVNDESVESSGIQGSSSSEQLQQPNETHQNKHQSKHYMPAYRRNLNAYRIRQLPTGINVDNNGSNLSLDSTQNMRKRPNLHQETVYDQMIPVLANTEPKLFSEDNNEQDTAATIQQNQQNNEKVIMKNLRNNDFGSYPRGTQSATSLSRSNSNSNTNTNTNVSRSSLHTRSSSVMSAVKGTTSYDNVFDTPKSATAASLVDVKVSNNNNNNNKQPVYSLKNNYDIKNTSEIQEEDQYENEFTNYSES... | Function: Plays a role in cell wall integrity. Affects the cell wall polymer composition in the growing region of the cell (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 37761
Sequence Length: 334
Subcellular Location: Cell membrane
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P32900 | MYHTHMHESLISVTSTVSVSDASYAYARLTRRDDSDSSSSSASSTKNSKSAECTGSKQQCQLPTDSSHSTSVTVGVAVAVPVGVIIIVLAVILCIVYRRSKKEAEEDNDPDFEGDSEFLPTMKDYSPGINHLYSSDSQQDFMEKTLQQPPSDPFVGSMHSSKYNVRSATPPAIGRSWYVDPFQLPQESNDSNSLRDFAMRVQEDGLGGYKVAAESRNASQTSLHPDNFSNCTPIRASSRFQESESFRSHGSPIHNNQLSRGSATEGANKQFTFPNEDNDSSSVSEEAEVLNESNESASNDAFEFELDNSSEKTHERNLRF... | Function: May be involved in the polarity establishment process. Suppresses the lethality of KEX2-GAS1 double null mutant when overexpressed.
PTM: Phosphorylated by CDC28.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 81849
Sequence Length: 734
Subcellular Location: Membrane
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J9VSG5 | MATTNAQIYQQSQMPIPMPTPSLNPNINSAPTPGPNAMSVYEDCQSPLDTSVSGMYPGDRGSRVVSQPAPLLDQSHLRPGNQANLLSHDRTIELYRENAKKTNDPELIFEFSAFMIDAAKAMIPPEQEKDTNPSPALIKQMEKREEIIKEATSLLKRLADRGFPDAQYFLADCYANGIGTARGKQDFDRAFPLFILAAKHGHPDACYRAGTCCEHGWGCRRDSAKAVSFYKKAAVGLHPGAMYRLGTAELNGALGFPRRPKEGVKWLKRSAEHATEEFPHALHELALLHERGIENVVFVDNDYAAELLAQSAELGYAPSA... | Function: Activator of the chitin synthase CHS3 which polymerizes chitin, a structural polymer of the fungal cell wall . Chitin produced by CHS3 is deacetylated to chitosan, which helps to maintain cell wall integrity, anchor melanin, and offers an advantage during infection, as chitosan is less readily detected by hos... |
P34226 | MASSPQVHPYKKHLMQSQHINFDNRGLQFQNSSLKVGQDFSDNKENRENRDNEDFSTADLPKRSANQPLINEHLRAASVPLLSNDIGNSQEEDFVPVPPPQLHLNNSNNTSLSSLGSTPTNSPSPGALRQTNSSTSLTKEQIKKRTRSVDLSHMYLLNGSSDTQLTATNESVADLSHQMISRYLGGKNNTSLVPRLKTIEMYRQNVKKSKDPEVLFQYAQYMLQTALTIESSNALVQDSDKEGNVSQSDLKLQFLKEAQSYLKKLSIKGYSDAQYLLADGYSSGAFGKIENKEAFVLFQAAAKHGHIESAYRASHCLEEG... | Function: Activator of the chitin synthase CHS3 which polymerizes chitin, a structural polymer of the fungal cell wall.
PTM: Farnesylation is required for chitin synthase CHS3 activity but is not required for SKT5 membrane association.
Location Topology: Lipid-anchor
Sequence Mass (Da): 77066
Sequence Length: 696
Subce... |
Q9SU40 | MDLFKILLLVFFVNISFCFAADPYSFYNFEVSYITASPLGVPQQVIAINGKFPGPTINVTTNENLVVNVRNKLDEGLLLHWNGIQQRRVSWQDGVLGTNCPIPPKWNWTYEFQVKDQIGSFFYFPSLHFQRASGGFGSFVVNPRAIIPVPFSTPDGDITVTIGDWYIRNHTALRKALDDGKDLGMPDGVLINGKGPYRYNDTLVADGIDFETITVHPGKTYRLRVSNVGISTSLNFRIQGHNLVLAESEGSYTVQQNYTSLDIHVGQSYSFLVTMDQNASSDYYIVASARVVNETIWRRVTGVGILKYTNSKGKAKGQLP... | Function: May be a monocopper oxidase of unknown specificity. Involved in directional growth processes, possibly by participating in cell wall expansion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 65638
Sequence Length: 587
Subcellular Location: Secreted
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Q03656 | MGSSINYPGFVTKSAHLADTSTDASISCEEATSSQEAKKNFFQRDYNMMKKAPAPTKSKLSLALQTSKSSSSANGTVQEDTSSKTEDFSTKSIKKKPDSGVESHVSIQSDSGPQSDSDLDSDSSISSCDERNEESLKDYRPGGYHPAFKGEPYKDARYILVRKLGWGHFSTVWLAKDMVNNTHVAMKIVRGDKVYTEAAEDEIKLLQRVNDADNTKEDSMGANHILKLLDHFNHKGPNGVHVVMVFEVLGENLLALIKKYEHRGIPLIYVKQISKQLLLGLDYMHRRCGIIHTDIKPENVLMEIGDVEGIVQMVEALDKQ... | Function: Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 83238
Sequence Length: 742
EC: 2.7.11.1... |
Q9VIH7 | MPYHRGGDASSQADKLSGIVEESDLYEGFAPHVETSEIKTLDFYNLPKQTGKEPALRSYTEIQQLLQQGKKRDVKNILRENSWPINSPIRAQLWPMLCGQHQTKQQMLDGFYWEMVHQVFGTTELSEKPIMLPAFVDATHCLPYHLTSTGRAVADRIVNVLGYDCPDITYSPVLYPITSILLHFMSEEEAYICLAGLVGSKEKVFINQTKLQHEVTWKTVMQIAKKHTKSATSYFQRICPGLKLERIFMDWCWWILAGLPFQHLVRIMDCYFHEGIKVLYRVALVILNLFHKECQSNNEWSPDNIKNDIGNALIKFCKKI... | Function: GTPase-activating protein (GAP) for Rab35 which regulates synaptic vesicle (SV) protein recycling and turnover at the neuromuscular junction boutons and possibly ventral nerve cord via endosomal trafficking . Inhibits Rab35-mediated endosomal sorting which traffics old or dysfunctional SV proteins through a d... |
Q00497 | MEARVSQSLQLSSWINSDKVVRKPSGLLRFSEKWNEKPRHRVVVSCHLQPRKAAHSDRRVQLKVSCSPQNVQASVLESGCFSASIDEIETLKNKAEEVEEYLDGRCVYLVGMMGCGKTTVGRILAETLGYSFFDCDRLIEQAVGGITVAEIFELRGESFFRDNETEVLHKLSLMHRLVVSTGGGAVVRPINWRHMHKGISVWLDVPLEALAKRITTEGTKSRPLLHEESGDVYDTTLKRLTTLMETRGENYANASARVSLENIALKREKDVCHITPAEITLEVLIQIENFLKTQKSVVVL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 33720
Sequence Length: 300
Pathway: Metabolic intermediate biosynthesi... |
A2ZLU6 | MAGDRAEEEEGEAPPPEARAAAAVERVAAAVEAVAAGAGAGAGEYRNAYRRQLLALSRRIRLLGPFVEELRERRRGEGEGEEEERALAPLADALEAALALLRLGREGSRISLVLERDSVMKKFQGVILQLEQALCDIPYNELDISDEVREQVELVHAQLKRAKERIDMPDDEFYNDLLSVYDKNYDPSAELAILGRLSEKLHLMTITDLTQESLALHEMVASGGGQDPGEHIERMSMLLKKIKDFVQTQNPDMGPPMASRVLDSNGDSRPITIPDEFRCPISLELMKDPVIVSTGQTYERACIEKWIASGHHTCPTTQQK... | Function: Defense related protein that negatively regulates programmed cell death. In vitro, possesses E3 ubiquitin ligase activity.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor pr... |
P35829 | MKKNLRIVSAAAAALLAVAPVAASAVSTVSAATTINASSSAINTNTNAKYDVDVTPSVSAVAANTANNTPAIAGNLTGTISASYNGKTYTANLKADTENATITAAGSTTAVKPAELAAGVAYTVTVNDVSFNFGSENAGKTVTLGSANSNVKFTGTNSDNQTETNVSTLKVKLDQNGVASLTNVSIANVYAINTTDNSNVNFYDVTSGATVTNGAVSVNADNQGQVNVANVVAAINSKYFAAQYADKKLNTRTANTEDAIKAALKDQKIDVNSVGYFKAPHTFTVNVKATSNTNGKSATLPVVVTVPNVAEPTVASVSKR... | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
PTM: Glycosylated.
Sequence Mass (Da): 46570
Sequence Length: 444
Subcellular Location: Secreted
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P38059 | MKKNLRIVSAAAAALLAVAPIAATAMPVNAATTINADSAINANTNAKYDVDVTPSISAIAAVAKSDTMPAIPGSLTGSISASYNGKSYTANLPKDSGNATITDSNNNTVKPAELEADKAYTVTVPDVSFNFGSENAGKEITIGSANPNVTFTEKTGDQPASTVKVTLDQDGVAKLSSVQIKNVYAIDTTYNSNVNFYDVTTGATVTTGAVSIDADNQGQLNITSVVAAINSKYFAAQYDKKQLTNVTFDTETAVKDALKAQKIEVSSVGYFKAPHTFTVNVKATSNKNGKSATLPVTVTVPNVADPVVPSQSKTIMHNAY... | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
PTM: Glycosylated.
Sequence Mass (Da): 46688
Sequence Length: 439
Subcellular Location: Secreted
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Q05044 | MQSSLKKSLYLGLAALSFAGVAAVSTTASAKSYATAGAYSTLKTDAATRNVEATGTNALYTKPGTVKGAKVVASKATMAKLASSKKSADYFRAYGVKTTNRGSVYYRVVTMDGKYRGYVYGGKSDTAFAGGIKSAETTTKADMPARTTGFYLTDTSKNTLWTAPKYTQYKASKVSLYGVAKDTKFTVDQAATKTREGSLYYHVTATNGSGISGWIYAGKGFSTTATGTQVLGGLSTDKSVTATNDNSVKIVYRTTDGTQVGSNTWVTSTDGTKAGSKVSDKAADQTALEAYINANKPSGYTVTNPNAADATYGNTVYATV... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria.
PTM: Glycosylated.
Sequence Mass (Da): 48159
Sequence Length: 465
Subcellular Location: Secreted
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P22258 | MKNLKKLIAVVSTFALVFSAMAVGFAATTPFTDVKDDAPYASAVARLYALNITNGVGDPKFGVDQPVTRAQMITFVNRMLGYEDLAEMAKSEKSAFKDVPQNHWAVGQINLAYKLGLAQGVGNGKFDPNSELRYAQALAFVLRALGFKDLDWPYGYLAKAQDLGLVHGLNLAYNGVIKRGDLALILDRALEVPMVKYVDGKEVLGEPLISKVATKAEYTVIATNAQDRSVEEGKVAVLDKDGKLTTINAGLVDFSEYLGKKVIVYSERFGDPVYVAEGDNDVVSFTEGQDSVGTTVYKNDDNKTAIKVDDNAYVLYNGYL... | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
PTM: Glycosylated; contains 8% carbohydrates, which correspond to about 40 to 50 sugar molecules per monomer. O-linked glycans consist of Glc, GalNAc and GlcNAc.
Sequence Mass (Da): 82785
Sequence Length: 76... |
O14216 | MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQ... | Function: Has a role in the initiation of DNA replication. Required at S-phase checkpoint.
PTM: Phosphorylated by cdc2 at the onset of S-phase.
Sequence Mass (Da): 38685
Sequence Length: 337
Subcellular Location: Cytoplasm
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P34252 | MYSFELDKLKIELKTWEHDFIDKNKREPTRDDIKSLRTVRQMYKQYSTLKKKQSLQRQKVDTQESVELPAHKKDHDEVVEIGPTPQVYGKAISIFDMNLSPIKPIYMTFTNNIDVNNDNSKTISNESSPRKTILLKSSPADRTLVAEPISSVKRQLNFQMLNASSTRTPTSSPCKNRNGKLVEIKKCSPTINPPLESGKPSGYYGPNSPLKLDEENIHLNISLNSSTKRRLQIAYPSLQKTPSKDQADISTSFSPSPLIRRPLTKSLIELAREHTEIVKEFGVLQEEDIEEEEEGEEGENGYDEKNHEDDFGLEDELIRP... | Function: Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks.
PTM: Phosphorylated by CDC28 at the onset of S-phase. This phosphorylation, specifically phosphorylation of Thr-84 promotes intera... |
Q09761 | MNNDHASKKSFCIKAPSNWEKSYLEVWPLVTVPRQCICLRWCISKEYHEFTCSSLQFIVIRPAGTSVLLGRVKSSKANQLVGIEHVEGSRYALIFLSEKLDFKSLKVIANHQLTKSSKSLSNVSNKPLGDQLFRSNSLMSPSLLKKELHRIQSDASQANERESQAPHSFVTHDLISSSKDGNSLTHEFANDSVTEMVQDYTPSCSRDVKSLLDHLYNSYFYQLLMTKTPVVFYVKQMVGKTRQLAVEVHNHVEEKALVDELLKFLDNLKSVDDRKSRLLQCFESHLNYKAWHLEFENEAHQYEIKGYRLWLQNILNRENC... | Function: Required for loading and maintenance of stable association of cdc45 with chromatin during initiation and elongation of DNA replication. Also involved in temporal regulation of origin firing. Plays a role in meiosis.
PTM: Phosphorylated.
Sequence Mass (Da): 79815
Sequence Length: 699
Subcellular Location: Nucl... |
A6XIG6 | MSEQAVEVSPKCLGPQHHINPLRFVMPPGSWDTHFHVFGPTTKYPYSETRKYTPPDSPFEEYVKLMLALGIERGVCVHPNIHGPDNSVTLDAVERSEGRFLAIVKIAPDVTLPQLKEMKKKGACGVRFAFNPEHGSGELDTALFDRVVQWCGELDWCVNLHFASNAIHSLAERLSQLTIPTLIDHFGRVHPTKGVDQPDFKTLVDLMRLPHMWVKLTGADRISRNSPSYQDVVPLARTLVDVAPDRVIWGTDWPHSGYFDVKRMPNDGDLTNLLLDFAPSEEQRRRILVDNPSRLFGQVAKGA | Function: Involved in the degradation of 4-sulfocatechol which is a central intermediate in the degradation of substituted sulfonated benzenes. Catalyzes the hydrolytical desulfonation of 4-sulfomuconolactone to yield maleylacetate.
Catalytic Activity: 4-sulfomuconolactone + H2O = 2 H(+) + maleylacetate + sulfite
Seque... |
Q8IYM2 | MNISVDLETNYAELVLDVGRVTLGENSRKKMKDCKLRKKQNESVSRAMCALLNSGGGVIKAEIENEDYSYTKDGIGLDLENSFSNILLFVPEYLDFMQNGNYFLIFVKSWSLNTSGLRITTLSSNLYKRDITSAKVMNATAALEFLKDMKKTRGRLYLRPELLAKRPCVDIQEENNMKALAGVFFDRTELDRKEKLTFTESTHVEIKNFSTEKLLQRIKEILPQYVSAFANTDGGYLFIGLNEDKEIIGFKAEMSDLDDLEREIEKSIRKMPVHHFCMEKKKINYSCKFLGVYDKGSLCGYVCALRVERFCCAVFAKEPD... | Function: Ribonuclease which is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in ... |
Q5U311 | MEIHPSLVVEPSYPDLIIHAGEVTLGEKDRNKMDSKKKRLEKARITEAACALLNSGGGVIVMQMSNKSEHPVEMGLDLETSLRELIPSSDLQAFIETKQQGDLFYIFVKSWSCSPKDGSTKPRICSLSSSLYCRSLTSKLPLDSKETFEFLERKKTCVKGSLTDGKGPPAKIPRLMYQNDLESNPAFEIFQSERLEYGQRLPFSESASIEFKQFSTRRAHEYIKSVIPEYISAFANTQGGYLLFGVDDESKRVLGCPKDNVDRDSLKAVVNEAISKLPVFHFCSSKEKVSYKTRVIDVFKEGNLYGYLCVIKVERFCCAV... | Cofactor: Can also use Mn(2+).
Function: Endoribonuclease that cleaves tRNAs and rRNAs . Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem . Does not act on tRNA(Sec) .
Sequence Mass (Da): 103655
Sequence Length: 907
Domain: Shows a pseudo-dimeric U-pillow-shaped architecture of the SLFN13 N'-domai... |
P0C7P3 | MESLKTDTEMPYPEVIVDVGRVIFGEENRKKMTNSCLKRSENSRIIRAICALLNSGGGVIKAEIDDKTYSYQCHGLGQDLETSFQKLLPSGSQKYLDYMQQGHNLLIFVKSWSPDVFSLPLRICSLRSNLYRRDVTSAINLSASSALELLREKGFRAQRGRPRVKKLHPQQVLNRCIQEEEDMRILASEFFKKDKLMYKEKLNFTESTHVEFKRFTTKKVIPRIKEMLPHYVSAFANTQGGYVLIGVDDKSKEVVGCKWEKVNPDLLKKEIENCIEKLPTFHFCCEKPKVNFTTKILNVYQKDVLDGYVCVIQVEPFCCV... | Cofactor: C-terminally truncated SLFN14 endoribonuclease requires manganese and magnesium for its endoribonuclease activity.
Function: Shows no ribosome-associated and endoribonuclease activities.
Sequence Mass (Da): 103907
Sequence Length: 912
Subcellular Location: Nucleus
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Q8W127 | MKREYQDGGGSGGGGDEMGSSRDKMMVSSSEAGEGEEVDELLAALGYKVRASDMADVAQKLEQLEMAMGMGGPAPDDGFATHLATDTVHYNPTDLSSWVESMLSELNAPPPPLPPAPPQLNASTSSTVTGGGGYFDLPPSVDSSSSTYALRPIISPPVAPADLSADSVRDPKRMRTGGSSTSSSSSSSSSLGGGAARSSVVEAAPPVAAAAAAPALPVVVVDTQEAGIRLVHALLACAEAVQQENLSAAEALVKQIPLLAASQGGAMRKVAAYFGEALARRVFRFRPQPDSSLLDAAFADLLHAHFYESCPYLKFAHFTA... | Function: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Acts... |
Q0V640 | MPASPLPALSPPASPRRNTSGASALGSRKADIPPDAIRGFATVGSLVRSEHFAQHFDDDIAGKDQEQSRKKSPEDVGNIAATKKKPGKRAATTSTADGEAKPKPKPRARKPKAADEEAVIIDPELRLPAAKVSPFFAAEGAPAAIEPSDEPVVDVPKLTKAGKPRKPRAKKENVGGEEAVPKPKRTRVTKPKAAKAKAGGKSQEEACVESAHFRKSEDTGDETVAGVLATRKSATTENVGSGEASIWDVPQSPKPKKKRAPKKPPPDPVINNLELDEAVSRRRDWTPPRDTAIPSPFTDSVGKENKQIEPDADNGGFTHM... | Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
A5DIU9 | MSNDVYFESIHMQSNYEEFETQAQERENISKISTSLSKFRKMSPKSTRSFKVKSAPLTNRKARNRIKSINAHVSAQYKVSNGQQNDDILDFFLKRKHNISSILEGVEDLENRNIVSNDTPQPSDNTGNYSSQLFTQEEWFQILRRIKLRFPKLSARTRKSLKYVTTKLEHLKNINSDDDSPQLWTQAASLPEEGLVNEDMKWLYELDDEQMDIGSSFCNVDEDSDQKLFVLTLSQAMGEREKSEPDVEIISDSSPEPTQLLNDGIIEEEHEVDEEEEDNENEEKSEKQLASSPTQISSDDTQEQLTNRAEISSYEASSLF... | Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
A3GGG8 | MVDSESQNDFANDGDNDSYFVSTQFESKQEEIMEKELQKLQTGQTVSQLLRFRSGISGLTSVTPKPVKVSRPGLRKTGSRKSKKNQSMSAMVKERFKTDKYAYFSGDQRKIDEFLRRLEGSEDIENMAMSTSGKDGSCLFTRDEWICIVQSIKLRFPELSTTKKKSLSAITRQINKQEKENEDENSIWSQARSLPSLELTDEDLKWLYDLDDEQMANRTITSSMTEVDGNDDHSPFVMTLSQTTPSQLSHIKESDSLYSQETNVQTTEPADHQSGHMQRCHSQTAEGKTQSKILEIEIVSDSEEEIESLIRNTEPDSSED... | Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
Q9P6M0 | MSAEEYIEVSSSPDIFTDDDDMITIEPELNKNPKDCNSKRKRSVTECCEIRLITSKCDFESTQQLVHHNCTGHKVHEHNLNAVDEEDFDTENLPLLFSSFSDNESDILEPDLNTRVAEDNDVLLSRYSKIKNSASCRNTFEHSAYHSNREEISSSGFYYHRKPQLFEKSLEKLGNKSIEANRSPLIKELCESANSTENVCFSVSTVDEIQQRHPSAGHSIDSTCQSNSFLEGDSATHKKKKTDNIKEFTSCEFNDRSRTLLNYAGYMDTNKNADNEAKSLKEKLENFPVEKLRAIAESYGFKSSDSKATLIKIVESCLDA... | Function: Regulatory subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for... |
A7F2D1 | MATTDVFIISSSPPRRLVSHIASSPPLPSLDKMVNGKKASNLRQGSSVAPIPTGATIFASASTLLRESSSGSLQGFDNARSFVTSAVQDENDLKKSAKPKAPRKTAPKKEDGTVEKVAKASRKTVKKKDKDVSGDFVDELVGEAAEIIAEKKPRKPRAKKGDNAEGKSGSVAEATVEKKPRKSRAKKAVDATGEDLKEKVPRKSRAKKTDVEAGIETVPKEKAVRKPRAKNSDLDSNLQSKMVKGRVTKSAVNASNTHKVETSKADTGNKHFAPNPIVEDIVADEGFGLVEAIRRRTNWTPPKSTKVPIDLEDSPEAQES... | Function: Regulatory subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
B8MED8 | MTSRLDHTIVIPSSPEQNWARSVSPCTPTRLFGLPPMSISPPSLPSPSRLFEEIGLGQQKNPPSPKSPFSSAAGKTATSKAITENPSRNESSSKRGRPGSSEAKTAGSRKNSKSQETRNKILTGRVAKPTTVSKAKATAASKSKDTSVVKAKAGTKKSKPASQNKKDKLAEEAEAEAKEVADAEGLNLEEALKRRSDWTPPKALSLVSIDEDTPSQGSGTKLSFGDVLRDYHYNRENSSCEPAQPSKEGNPTKRRRLELVEFEVLQERKPIQQKQIKDAVKTRKTKSKPKKQLNTITARVTARYEQIGELEDLFVYNEES... | Function: Regulatory subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
C4JJE8 | MSFLNSSRRRTRSPSPGQIFAPSATPIVIDSSPSVPSASSILDSLLGEFSEARDPYTVEAGPTGRSSDHLFSSPGVLTQSPGRENVPPRPSERTKDAHGKDRFLVSTERNGRSPFRGNPYRSAEIHSPKGRLKAPTKEGGTRKTKKFSSSNRTLTGRSTKFLAKTASKPTQSSKVPSEIPAAKLDSLQWEDGELRLELATTRRGSWTPIKDTSIDIVDPTRNLSPSNVSAAGSQKFSSMLSDYGFTKGSTLTMENELRREVPTTKRRLELLQGTANDIFSEGDFSRPPEKSVVNPNGTHSRRSRKTTSTTITSLSTAQYG... | Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
A7TEM0 | MDFRQAQRNLELIEEVAKNSQDSDEPIIDEDDLKEGKVEEEGEGTQIPSMPFSDDDDSDNNSKDTFKETPLELVDKEEAIEDKAPNDDEPVVSVEEKIATQEPEPEEQIFMNTQIQGQLDDIEQEDNLRSKLSNFKYASEESSSVQVIKRSNERKLKSKKITKPKLTKTSKRTKTNSNPSTQQTLDEIKISRSENILKLLSGKHGKVKDMINHQRNVEKKVKLVKNKNSNIITYDTYNSEEWLRIMKLILEKFPSANDMEVKQVYHYIYGEEQEQEYDNLWEASQIPLASMREEAYNEDNQIDRKIPNIPNSTQTRVEVM... | Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
PTM: Phosphorylated ... |
B3LT96 | MELQRAQRNLKFLQNEDYVNVTDQTNLNGESQNAYSLGMETQVPEMQFSLSSDDDSIGTQVKSVTAQKSPMTQETTKNDTERNKDVDKSCNPVSTSHPDLGGSNIEENIFINTQIQSRLDDAEEETNLKLKLEKFKYSFKSSNADDTHSNANVTAKRRPAIRKANSKLKTKPKTKRDPKIIKNITDFNINNYERSRTASLLKQLSGKHKKVLDIIKTQNEGNSDKPPRARNNKGEKATFDTYSEQEWKDIMKLLLQKFPQSEETDLNEVQKFLYGSEKSSNSLDNQESSQQRLWTASQLPPELPDEAIQPEQEERIRDTQ... | Function: Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA seco... |
C5DY61 | MDFHRANRNLQLVESGVSDGRNPESFSLDETQVPVSSGFSSDSDKDQQEQIFINTQVQGRLDEAEEADKVRANLGQFRYDSQDSAISPKHKSAIQRPSARTTKRSSSSQRRKAPTKAQSLLKQLSGKHAKVQDMIKYQQKLDSLAGSQQRAKSKGKTTKTKKQQEKRYDTYNANEWQHIYNLLLEKFPHTRPSEVEDVYQYLYGDESEDQPLWNESQRPIEPESQDLGFLPPPPADKQRVSVLSLSQVMDDKHSREPDEDIIVPDSTDEEYIVIPIPSSPQPLRPPLATKPPLLTKPPLKKVESDAGTPKTAHSPSDGVI... | Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA (By similarity).
PTM:... |
P32828 | MHSDTNGRTKSNNSPSDNNPNETVILIDSDKEEDASIREANLPVRLYPDRRVGRRRDALNRFVRSDSRSRNSQRTHITASSERPDFQANNDDITIIREVGRFFGDDGPIDPSAHYVDLDQEPGSETLETPRTIQVDNTNGYLNDNGNNNESDDGLTIVEERTTRPRVTLNLPGGERLEVTATTTDIPIRRSFEFQEDLGASRRQLLRRSATRARNLFVDRSDENDEDWTDDTHNLPEAIQRARRESRMRMSRRIAERQRRVQQQRVSSDENISTSIRLQSIRERIQSYTPDIRSAFHRAESLHEFRSILQNVAPITLQEC... | Function: Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation . The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC... |
P87176 | MPPAHKRDTNVRNLSAPYNIPSQSARVAAGNAAINRRRSSPVENSPGNGFPVSEDATDYPSGTTSENESLPLNRAPRSLREVASELAQEETLPVETSDLNIDVESEVFDLEDINFQNDADDINQRFTYNNHPASVENSLTNVNSIHAQPTTISDMIDLTDETSYDPRKQKFEQGKNPSTTNAEIEKEEPSKKQVVPSSQRLADYKCVICLDSPENLSCTPCGHIFCNFCILSALGTTAATQKCPVCRRKVHPNKVICLEMMLGSQKKKS | Function: Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Acts as a critical suppressor of gross chromosomal rearrangements (GCRs) during normal cell cycle progression. Involved in stabilizing, restarting or resolving transiently stalled... |
P40072 | MARRPDNQNPEGENLRIKRVRLESVRQNDEEEENEVSRTQNIVTDNRHDSPEAVVEIIGERALENTSEEDGDDDLSLFRALEEDPGSDHNTSNNDSGNHDRETMHTEEPEASSGNNITLTNNVEELHTMDVLSQTANTPSASPMLDAAPPTTKPGTNSKEQTVDLTADAIDLDAEEQQVLQISDDDFQEETKEAPKEYGAAKDYRCPICFEPPETALMTLCGHVFCCPCLFQMVNSSRTCRQFGHCALCRSKVYLKDVRLIILRKKQVKKKVKS | Function: Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation . The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC... |
Q9UHJ3 | MNGEQQLDADAGSGMEEVELSWEDYLEETGSTAVPYGSFKHVDTRLQNGFAPGMKLEVAVRTDPETYWVATVITTCEQLLLLRYDGYGEDRRADFWCDIRKADLYPIGWCEQNKKTLEAPEGIRDKVSDWDEFLRQTLIGACSPPVPLLEGLRNGRNPLDLIAPGSRLECQAFQDSLSTWIVTVVENIGGRLKLRYEGLESSDNYEHWLYYLDPFLHHVGWAAQQGYELQPPSAIRHLKNEAEWQEILAKVKEEEEEPLPSYLFKDKQVIGIHTFSVNMKLEAVDPWSPFGISPATVVKVFDEKYFLVEMDDLRPENHAR... | Function: Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic prog... |
Q9MA17 | MEIGSSSTVAGGGQLSVPPGFRFHPTEEELLYYYLKKKVSYEPIDLDVIREVDLNKLEPWELKEKCRIGSGPQNEWYFFSHKDKKYPTGTRTNRATAAGFWKATGRDKSIHLNSSKKIGLRKTLVFYTGRAPHGQKTEWIMHEYRLDDSENEIQEDGWVVCRVFKKKNHFRGFHQEQEQDHHHHHQYISTNNDHDHHHHIDSNSNNHSPLILHPLDHHHHHHHIGRQIHMPLHEFANTLSHGSMHLPQLFSPDSAAAAAAAAASAQPFVSPINTTDIECSQNLLRLTSNNNYGGDWSFLDKLLTTGNMNQQQQQQVQNHQ... | Function: Transcription regulator. Together with BRN1 and BRN2, regulates cellular maturation of root cap. Represses stem cell-like divisions in the root cap daughter cells, and thus promotes daughter cell fate. Inhibits expression of its positive regulator FEZ in a feedback loop for controlled switches in cell divisio... |
C0NUU1 | MTPLLRTICAILCILIAVPLTFACPTKAGVSKQANKRPTYAIAHMVLDRKGLKDAIKNGANSVEIDIAAYKEGWWADHDIRGRSWGDSLEDMFKAVAKESKNIAFVWLDLKTPDMCSGATCNKDVLDPSKCKPKDKCSMNSLQELAQKILNPAGVRILYGFFGAGATDSAGFNYIQGNLKAGEAVCLSGEVENVLNVYKKKGRGVKPQQRVMDYGYTQLETGFGNCKEKGYNTCAGLRNGAKARDKGDVKRVFGWTSRVGDGERVGQLLDKAHVDGIIYGFAITRYYDHEDSRAAARDITQRVQKSDDRYMATGADKPW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane d... |
D4AZV8 | MVSLLRLCSFLLAAGSILVQGSPIIAPSIPPCEPPSNFTGPSNFTSRPGNGASPFWLIAHRVLTKDGVKAALGHGANALEMDITGWWSGWFGDHDGLLTSAGDTVSDLFDEIASRRTQGDPVSFVWLDLKNPDFNKNGVNIVSLMILCREKLEKVGVRVLYGFYSSQTNGPSFKFVKQVMNENEAIGIDGKFETVEKDFEEKGIPLQKRVFSSGLFNPDFNFGNCEVHSSGVCAQLREGKESHEFSKVFGWTVSSYTRKDHVYKMMEVGVDGLIYGFVASHYYDHADIRHTLSTIRGWLEEHKDTHRLATVDDNPWSSMS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane d... |
B8NQ51 | MQSISVLICVLLALSILNFTVASLTQRPIYAIAHRVLRNEAVTAALSHGANALEVDLTAWYFGWWADHDGKLFSAGSTARDLFKFIAQKQWTKDYNISFVWLDIKNPDFCRKGRPCSIEALRDLAREILEPAGIRVLYGFFETAESRGFKVIRDGLNSNEAVVLSGETSTILHLYNISGAGIPVKQMVMDFGDSWLRKGVDIYPELRYGSWKRDHGKLGKVFSWTSAQGDTEMVRYLLREAGIDGLIYGYQTDEYNDKSGPKSALKDIVDFVEAHSDTHRMATEDDAPW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane d... |
J3K844 | MVSLSLLLCSALAGLLHVASCIDVPDQAPLTVDECKCKPTSPKPVYAIAHRVLTEEGIQAAIAHGANAIEIDMTAWKSGWWADHDGLPTSGNVTAKAMFREVARLREDGAHLSFVWLDIKNPDWAISGRSSVAYLRKLAREYLEPAGVRVLYGFSNPRNSWGFKEIRNFLNANESVSVWMDSGDAKKIYAGVGRSIPVAQRVVDNGLFSLFWKPYIFDDLRRSSEARDCCTVGKAFGWTILAGQDRYVDKLLGYSGVDGLIYGTMASAYEDSEDTRAAAALISNWIKNHPDTHRVPTQDDKPW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane d... |
C4JUE5 | MLLSSLISLALLSSQVVADPAWAPPDKGLKPEVARLLPPFLRYRRPIYAIAHRVVTVGGIKDAISHGANAFEVDMCADSIGEGWWANHDCTNGRKAGDSARKIFETFAAERKRGKTVTFVWLDFKNPDACVKNQGCSIEAIQQLCRDILEKQGIRVLYGFYKAEDSRAFKTIRNNLNDREAISLNGATTKVLKLFEGTAPKVSKHQRVMDYGDTYLDKGFGDCTEKDWYTCTELRQGADLRRKGKLGKVFAWTSTVNQGRLVDQLLGKAHVDGIIYGFKLTDYYDHADSRAAANDIISWVKRRRALYYMATNDNNPWIDI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases D are produced by some spider in their venoms, but also by arthropods such as ticks, or pathogenic bacteria and fungi. They might play a role in pathogenicity through different mechanisms, such as membrane d... |
P38925 | MVNVGPSHAAVAVDASEARKRNISEEVFELRDKKDSTVVIEGEAPVRTFTSSSSNHEREDTYVSKRQVMRDIFAKYLKFIGPGLMVSVAYIDPGNYSTAVDAGASNQFSLLCIILLSNFIAIFLQCLCIKLGSVTGLDLSRACREYLPRWLNWTLYFFAECAVIATDIAEVIGTAIALNILIKVPLPAGVAITVVDVFLIMFTYKPGASSIRFIRIFECFVAVLVVGVCICFAIELAYIPKSTSVKQVFRGFVPSAQMFDHNGIYTAISILGATVMPHSLFLGSALVQPRLLDYDVKHGNYTVSEEQDKVKKSKSTEEIM... | Function: High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Contributes also to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63264
Sequence Length... |
P38778 | MTSQEYEPIQWSDESQTNNDSVNDAYADVNTTHESRRRTTLQPNSTSQSMIGTLRKYARFIGPGLMVSVSYMDPGNYSTAVAAGSAHRYKLLFSVLVSNFMAAFWQYLCARLGAVTGLDLAQNCKKHLPFGLNITLYILAEMAIIATDLAEVVGTAISLNILFHIPLALGVILTVVDVLIVLLAYKPNGSMKGIRIFEAFVSLLVVLTVVCFTVELFYAKLGPAKEIFSGFLPSKAVFEGDGLYLSLAILGATVMPHSLYLGSGVVQPRLREYDIKNGHYLPDANDMDNNHDNYRPSYEAISETLHFTITELLISLFTVA... | Function: High-affinity manganese transporter involved in mobilizing manganese from vesicular stores iin conditions of low manganese ion concentrations.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59768
Sequence Length: 549
Subcellular Location: Vacuole membrane
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Q12078 | MRSYMQILQKFAKFIGPGILVSVAYMDPGNYATSVSGGAQYKYTLLFSIFISNIFAVLLQCLCVKLGTITGYDLAENCRHNLPKKLNYTLYLFAEVAIIATDLAEVVGTAIALQILFKIPLTWGVLLTVLDVLVILMFYTPNGQSLKKVRVFEFGVGILVIGTCICFVLELFKVSIPDKAELFKGFLPSNIIFKEQQALYISLGILGATVMPHSLYLGSSIVKPRLHDYDLKKYGKVNARPSLSAIKYTLNYAYAELIISLFLIATFVNSAILIVAGATLSGQPEAEDADLLSIYKLLVHYISPAAGLIFALAMLCSGQS... | Function: Has a role in controlling the cellular iron ion levels. Mobilizes vacuolar stores of iron in conditions of low iron levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51775
Sequence Length: 473
Subcellular Location: Vacuole membrane
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B0R061 | MSFFNLDRFRFQRDNAVGIHRKSPDGSNSDKENKQAHQRKADGQFPSGKTSRQVLEDVSSDDEVVRMGKDSASDLQQHINKDMEDKIIKLLEIFPQKSKKDLLEVIENTSTLDGAVAHCLMIYGDEDSGGRKDKGGRSDDDDQPKKKRKIQRSDSSESEDEDSEDEESEEPSREKQEALLKKLKRKLPDIEKEVLRDILKEHDWDYENALGSLLVFSSTDTSSPENQKSKQKSKSSHSKEKTDKITQRPSGSSSLSRWLTAASSHVPEVSSMSALKTQKSALSKSTSKNSSFKRKRGDEMPLNDVSASEDEDEIDSDVDS... | Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking D... |
Q9U3D4 | MSVTVEVADEETHDVPLVEQVRTTPDQNVDVKVQENNVVTTKIGPKLETIPAAKMQDDNGDEEKAENSEGAAAEKVEKQHDDDGVVVHEETDGVASSRSSHHDKQKPGETKKSGDGKMDDDDIITTARSSSRRICGSAASSSDSETADDAPLLPDEGPSHAVRLEMPGDKPASPHDRFPKTPLKTLVAFLMLVVAAAGNTITLSWIHERYPLTPPLPDIVFELIPKIPWGLRLCENLMIGSFVSLLVLILFHRHRWIVLRRLCFIGSILYGMRCITMMVTPVPKADEDFECSPRFGENATFSLIVMRGVWSMFGLGLNLF... | Function: Sphingomyelin synthases (SM synthase or SMS) synthesize the sphingolipid sphingomyelin (SM) through transfer of the phosphatidyl head group of 1,2-diacyl-sn-glycero-3-phosphocholine (phosphatidylcholine, PC) on to the primary hydroxyl of ceramide (N-acylsphingoid base), yielding 1,2-diacyl-sn-glycerol (diacyl... |
Q7T3T4 | MSGRMKEVVSWSPEEVTNWLMENAVPEYCEPLKSFTGQDLINLTEEDFKKTPLSRVSSDSGQQLLHMIETLKMAHHIEAHKNGHVNGHIHVSVNNTAHENGFSSKTKLNGVPNGYKKEMIKIPMPEPERLQYPMEWGKTFLAFIYALFCFIFTTVTISVVHERVPPKEVQPPLPDAFFDRFDRVQWAFSICEINGMILVGLWLVQWLLLKYKSIISRRFFCIVCTLYLYRCITMYVTTLPVPGMHFKCSPKLFGDWESHLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVILTLTYLFIKEYSPRRLWWYHWLCWTLSM... | Function: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Golgi apparatus SMS1 directly and... |
Q86VZ5 | MKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSSDNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKEMIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFFDHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTTLPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIF... | Function: Major sphingomyelin synthase at the Golgi apparatus . Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and d... |
Q20735 | MTNSSEFTDVLQSRDPCVSNGIVINIDPIDPEPTPIRKEFTCEDTFHHEHHGNSEGFKTLTAFLCLMLSAFLNFFLLTVIHDVVPRQPLPDLTFMIIPQQRWAWSVGDVLSTVSSVVAFTIIFLHHQRWIVLRRTFLLGAIMYGLRAVILGVTFLPPSFHNRDEICQPQVNRTAMYGMEIATRFLTYVITLGLTSGQDKILCGDLMFSGHTVVLTIMYFVQLQYTPRGLVILRYIAAPITFLGIAALVVSGGHYTMDVLIAYWLTSHVFWSYHQIFEMRKDDRPQAPLSRLWWFWLCYWFESDVADGKLVNKWNWPLEGP... | Function: Sphingomyelin synthases (SM synthase or SMS) synthesize the sphingolipid sphingomyelin (SM) through transfer of the phosphatidyl head group of 1,2-diacyl-sn-glycero-3-phosphocholine (phosphatidylcholine, PC) on to the primary hydroxyl of ceramide (N-acylsphingoid base), yielding 1,2-diacyl-sn-glycerol (diacyl... |
Q7ZXV5 | MGQPEGLERFDSPGKGRGLKATRSFALGELLFTCPAYTYVLTDTERGNHCDFCFARKEGLSKCGKCKQAFYCNVDCQKGDWPMHKLECSAMCSYGQNWCPSETVRLTARILAKQKTQTERTPSETFLSVKEFESHLSKLDNEKKELIESDIAALHRFYSKNLHYTDNAALVFLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNIIVTFKGTVAEIRAVQEIHAGDEVFTSYIDLLYPTEDRNDRLMDSYFFTCDCRECSTKQKDPAKLEIRKLSDPPSHQTVKDMIKYARNIVEEFRRAKHYKTPSELLEMCE... | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'L... |
Q5RGL7 | MMKAEGIPGIEQFASPGKGRGLRVSRAYGVGELLFSCPAYSYVLSVGERGLICEQCFTRKKGLAKCGKCKKAFYCNANCQKKNWPMHKLECQAMCAFGENWRPSETVRLVARIIARLKAQKERSPSEILLLLGEMEAHLEDMDNEKREMTEAHIAGLHQFYSKHLDFPDHQALLTLFSQVHCNGFTVEDEELSNLGLAIFPDIALLNHSCSPNVIVTYRGINAEVRAVKDISPGQEIYTSYIDLLYPTADRLERLRDMYYFSCDCKECTTKSMDVVKMSVRKRSDEIGEKEIKDMVRYARNSMENFRRAKQDKSPTELLE... | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'L... |
Q8NB12 | MTIGRMENVEVFTAEGKGRGLKATKEFWAADIIFAERAYSAVVFDSLVNFVCHTCFKRQEKLHRCGQCKFAHYCDRTCQKDAWLNHKNECSAIKRYGKVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKDLRVDVDTFLQYWPPQSQQFSMQYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGNHEAVKSMFHTQMRIELRALGKISEGEELTVSYIDFLNVSEERKRQLKKQYYFDCTCEHCQKKLKDDLFLGVKDNPKPSQEVVKEMIQFSKDTLEKIDKAR... | Function: Methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-tr... |
E1C5V0 | MRSEAVPQPGGLERFASPGKGRGLRALRRYAVGELLFSCPAYTAVLTVSERGSHCDGCFARKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECAAMCAFGQNWNPSETVRLTARILAKQKIHPERTQSEKLLAVKEFESHLDKLDNEKRELIQNDIAALHHFYSKHMEYPDNAALVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVKEIEPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCDCRECTMKEKDKEKLKIRKLNDPPSAEAVRDMIKYARNVIEEFRRAKHYKPPSEL... | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'L... |
Q9NRG4 | MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI... | Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'L... |
Q9H7B4 | MEPLKVEKFATAKRGNGLRAVTPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEKLMRCSQCRVAKYCSAKCQKKAWPDHKRECKCLKSCKPRYPPDSVRLLGRVVFKLMDGAPSESEKLYSFYDLESNINKLTEDKKEGLRQLVMTFQHFMREEIQDASQLPPAFDLFEAFAKVICNSFTICNAEMQEVGVGLYPSISLLNHSCDPNCSIVFNGPHLLLRAVRDIEVGEELTICYLDMLMTSEERRKQLRDQYCFECDCFRCQTQDKDADMLTGDEQVWKEVQESLKKIEELKAHWKWEQVLAMCQAIISSNSERL... | Function: Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation . Also methylates 'Lys-5' of histone H4 . Plays an important role in transcriptional activation as a member of an RNA polymerase complex . Binds DNA containing 5'-CCCTCC-3' or 5'... |
Q5F3V0 | MALPVEEWRRSAARCWAALEPALRERLAAAPLGEALRMGCGLFGPEEAALQRLCRRARTGKEPAAARFYREEGNRQFGRCCYRDAVRLYSQAAAHEPPRSPEVALCFANRSAALFHLGHFEVCLEDIARAESHGYPDRLLPKVLLRKAECLLRLGRLQDATDTLTAVENKMAVDGIMTSPIHRMLLKKLSQLKTEIHEGSCPEPAREADGDVQRESEIWEENGSISGASSSLSLNFSTERGRHLVASQDILPGQNLLKEKAFVSVLCPGEGDSLLLQDSSETVWDTRVTNADLYCHHCLKQLLASIPCCGCSYAKYCSQN... | Function: Plays a critical role in cardiac development. Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1.
Sequence Mass (Da): 82027
Sequence Length: 742
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q08C84 | MDLPCQDWVCHVEQKWAELRSEETERFSLLTDIDAIFNYGLSLICPEDLNILSRISEKFSVKKSPETASEFRQQGNLSFKVKDYPAAVLHYSKGVCHADKNTDELSLCYANRSAALFYQGLYQACLEDIRRSLEAGYPSHLQDKLQTRQTACQNQLRKAEKPNIPHTDHQLSPCQKTVNSTGHLSDGVSVYFSSDKGRHMLVMENKPAGEVVLEDEAYCSVLIPANIFNTGTNKAVETFGTEDRHCHHCLSQSLSFVPCPKCSYARYCGESCQKDAWDQWHQWECPVGADLLAIGVLGHLALRVVLKAGQTEVQMGIKNT... | Function: Plays a critical role in cardiac development . Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1 .
Sequence Mass (Da): 83677
Sequence Length: 753
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8IYR2 | MDLPVDEWKSYLLQKWASLPTSVQVTISTAETLRDIFLHSSSLLQPEDELFLKRLSKGYLVGKDSDAPLFYREEGNKKFQEKDYTGAAVLYSKGVSHSRPNTEDMSLCHANRSAALFHLGQYETCLKDINRAQTHGYPERLQPKIMLRKAECLVALGRLQEASQTISDLERNFTATPALADVLPQTLQRNLHRLKMKMQEKDSLTESFPAALAKTLEDAALREENEQLSNASSSIGLCVDPLKGRCLVATKDILPGELLVQEDAFVSVLNPGELPPPHHGLDSKWDTRVTNGDLYCHRCLKHTLATVPCDGCSYAKYCSQ... | Function: Plays a critical role in cardiac development . Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1 (By similarity).
Sequence Mass (Da): 89225
Sequence Length: 804
Subcellular Location: Nucleus
EC: 2.1.1... |
Q12483 | MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEFRSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELEKVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILGYSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL | Function: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II... |
O43759 | MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPTGPDPAGMGGTYQQPANTFDTEPQGYQSQGY | Function: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (By simi... |
P46950 | MTKSVGDEESQYIEDPSFAAAAAFTGGRDGVSYSNQRFAEGSGHSSDLAKSLEDYRPPDEKPSSLSSVGEGGANEEEKGGNDGGPLARIQTGLFSPRLRNHRKKILSKFVLNNFFIACVCVSLISIYWGACYGTDRYFFKVKNIVVLQDAPSNTSVQSISAIIPSLLASVPGTWHIYNATSFHRKFGTTNSTEIDRKIVDLIYDERYWLALNVKPNATDTLYNSLISQDANSEFNSSIFFESVFESGRDPSSVKSTILPLMQQLEVRLQKYYVKEYLPSLMSNITSNDRDLNINMENWAIAGQLLFTYNDYRPFADRILM... | Function: May function as a N-methyl-N'nitro-N-nitrosoguanidine (MNNG) export permease.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61293
Sequence Length: 547
Subcellular Location: Membrane
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O43760 | MESGAYGAAKAGGSFDLRRFLTQPQVVARAVCLVFALIVFSCIYGEGYSNAHESKQMYCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAYFPQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAVTNPKDVLVGADSVRAAITFSFFSIFSWGVLASLAYQRYKAGVDDFIQNYVDPTPDPNTAYASYPGASVDNYQQPPFTQNAETTEGYQPPPVY | Function: May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane.
PTM: M... |
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