ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P40316 | MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKDADLPQLQNTLSIRKNDQLRKLSQISRSRSRANHNDLLSNSRKLQKYGSVLGYNALPKMKSLVLKDLADSGKNEESSDDDEGNEDSESKLGKKLQSALLKQDSSDGENELNGGLGLFNEQGGLQQLIKNSTKNEQKTKNDKSDKTDDYDIEIAPQRQEPLPYVPEGYSPFQQDDIEKLKTFNSPYKLDLEDEDDTPDKVDLLPLEQIDEEG... | Function: Regulatory protein, which plays a central role in chromosome stability. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESP1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it ... |
F6CD01 | MFSTLKNAFKDKEIRNKIYFTLFILLLYRIGANITVPGINVKAITQVAQTGLVPMLDTVSGGGLDNYSIFSLGVSPYITAQIVIQLLQMDIVPTLVEWGKQGEVGRRKTNQVTRYLTLVVAFVQSIGITLGFNALTQMGLVKNQTPQTYVEIAIIMTAGTMLLTWLGDEITDKGLGNGVSVIIFAGIIARLPSGLYQIYKEEIINNSASDRWQGILFFIAVIVAILIVTQLVTWVEQADRRIPIQYTRRATISGSESFLPLKVNVSGVIPVIFASSFIVTPATILMAFQRTQGDQQWFKVMNQIFSLQTTPGVIIYTLLI... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
Q74L41 | MEKKNLLNVIKKVSFSLFIVIIYVMGLYIPLPFAEGTKQYMEAVKNTPISILGAFSGANFTRISIFSIGLNPLMFSMLIIQLLSFTHSFGFDALSPKQVQYLMQFLTMIITIIQAALLVFAFTNRRNGLEDFEMILILSAGSCLVVWLCYRNMKYGVGASAPVILTSILNGAIPNIISNVKLLLTMKYAWIWLAALAIFILLLIKFWLAFTKAYYPLKVVNPSLPASSNLMTVPLGLNMAAMMMYMVGMAILTLPLMVGRYFSSSSLINNWVFQASFSAVMGILIFYFFTFVNFDPKEQAKSFRNNHYYIPNIAPGRPTQ... | Function: Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44559
Sequence Length: 395
Subcellular Location: Cell membrane
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F6CFW7 | MILIIYRALFFVTIPGVNSAALAKLSNNSSLTMLSMFSGGGFENFSIMSLGVTAYITAQIIVQLLQADVIPTFTQWSKEGQTGRKKLDQVTRSLTLVLGLVQATGITLGINTLTNGKFMIENNPFTIIVIAVSMTAGSFIAMWLGDLITENGLGNGISVIITAGILVRFPSMINDVIKGVTFGTKVNWIRFSELMIGAAILILLIVWFTRSELRIPIQYARRAQLTGKDSYLPLKIIVPGVIPVIFASTIMTIPQTILMFFNAGQNSSWYRVVQTFFTLSTTSGVIIYGLMIIFFEYLYSIVQIEPDKFADNLEKQEAYI... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
D8MEB8 | MKGENINNIHLVLKKMLWTSLIVFIFLIGRNILIPGVDAKQLARFLNNQYLLQIVNGTTGGDLSRMSLFALGLGPWMSATILWRVLTLIKRFDLKKIPIERTFLFKIAIAIIIGFIQSIAIISNIDINPKISIFAQTQFGAMATISLIMVSGAVFLVWLSNMNEILGIGGPTVLILASMIINWPTNVSLYILENVRSSLDINSVILMLVIMISIVFLVLLTVVVQRAQRQIPIRRILVNNNFYQQSYLPIQINPAGGMPLMYSMTLLVLPQYILQAVHYWLPNNVLVENGLDNIAITKPLGVTAYIIILFALSIGFAFIN... | Function: Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47180
Sequence Length: 421
Subcellular Location: Cell membrane
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Q2FUW2 | MLKLLQQYEYKIIYKRMLYTCFILFIYILGTNISIVSYNDMQVKHESFFKIAISNMGGDVNTLNIFTLGLGPWLTSMIILMLISYRNMDKYMKQTSLEKHYKERILTLILSVIQSYFVIHEYVSKERVHQDNIYLTILILVTGTMLLVWLADKNSRYGIAGPMPIVMVSIIKSMMHQKMEYIDASHIVIALLIILVIITLFILLFIELVEVRIPYIDLMNVSATNMKSYLSWKVNPAGSITLMMSISAFVFLKSGIHFILSMFNKSISDDMPMLTFDSPVGISVYLVIQMLLGYFLSRFLINTKQKSKDFLKSGNYFSGV... | Function: The central subunit of a protein translocation channel (Potential). Part of the accessory SecA2/SecY2 system specifically required to export SraP, a serine-rich repeat cell wall protein encoded upstream in the same operon.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46885
Sequence Lengt... |
G5EDF7 | MERKGRERKLPGMKIVMPTPVETPTMNLEDRCLIKLTNESEEIEIAATDLVVLEELGKGGYGIVEKMQHRQSGIIMAVKRIKSSINDQSQKQMLNELDACRRSDCCPQMVRFYGAMFREGDVWICMEVMDTSLDKFYRHAYKIGKHIPEPFIGKMALSVIEGLNFMKEQLNLIHRDVKPSNILLNRHGQVKICDFGISGHLTNSMAKTVQAGCKPYMPPERIDGETKSAYDVRADVWSLGITIIEIAVGTHPYANWKTPFEQLKQVVKEPPPKLPMESGFSVDCQYFVKRCLEKDYNERPKYPELLAMPFMEQARNEKQF... | Function: Dual specificity protein kinase which acts as an essential component of the p38 signal transduction pathway which is also composed of upstream effector nsy-1 and downstream effector pmk-1 . May phosphorylate pmk-1 . Downstream of CaMKII unc-43 and adapter protein tir-1, plays a role in determining asymmetric ... |
O13858 | MSHASKNYNAQLTAAAASTALHGTKKIYNSNENDRAVNSFLGNRTSYGEAVNGSPQYDYMRSRMSTLGSANQPMAPPSLRNRSSVYLPTPAGPPQIPVNTGKRYTLTSSSANYMTKSERQMRPPKSYDFPPSQQVRPSTSRSPSYASYNSEEVNFQSYQDPRLLPRTSQMYMPDNNYSPAVKSPAAQRRSSSYMVPANSRGSPANYNTPYYPTAIPPPIEEYSPSVSLPTSPVAEESYNNVQRSSTVRNNTTQKSVLKKPSRKMSPAYTSSYRQNSPSSQVPPVSKKHVIIYENKEGSSSSESVYEDVFEDFDPSGSNQA... | Function: Important for the biogenesis of filamentous eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on the plasma membrane to cluster specific proteins at sites of membrane invaginations.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69794
Sequence Length: 636... |
A6TQL2 | MNKGRILSQLPSVDELIKNLEHDKLEKMIPRSVVVEQTRITVDTYRKAILTMDEGSLRDYQIDITSMHDEIKQACESFCSMNLREVINGTGVILHTNLGRSLLSEEIKGQIWEVASGYSTLEIDVTTGKRGSRYNHVVDVLKHLTGAEDALVVNNNAAAVMLVLGTIAKGKEVIVSRGELVEIGGSFRVPDVMEQSGGKLREVGTTNKTHLWDYEGAISDETAALLKVHTSNYRIMGFTESVGLEEIVELGNRYHIPTIEDIGSGVLIDLQKYGLAHEPTVQESVKAGVDIVTFSGDKLLGGPQAGIIVGKRKWIEKMKK... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 52130
Sequence Length: 467
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
O67140 | MKSLLRQIPQISKVVEIFKKKYPEIYVVKAAREVAEKYRKEIIEGKRKDLNGFLEDVERKIKSLMKPNIKRVINATGVVINTNLGRAPLSKDVINFISEIANGYSNLEYNLEEGKRGSRIAHIEKYLNELTGAESSFVVNNNAGAVFLVLNTLAEGKEVIISRGELVEIGGSFRIPDIMKKSGAILREVGTTNKTKVSDYEGAINQNTALLMKVHKSNFYMEGFVEEVKLEDLVKLGHKYGIPTYYDAGSGLLINLKEFGISVDEPNFRDCISLGIDLVSGSGDKLLGGPQAGIIVGKKNLIEKIKKNPIARALRIDKLT... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 50848
Sequence Length: 452
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
Q8R8W4 | MEDLYRKLPSVDEILREEKINEVLKFNKREVVKNCIREVLERYREKIRRGEVKKIDIEKILEDVVSQIEEKKKMSLRRVVNGTGIILHTNLGRALFPPQVKEHLLDIAFCYSTLEYDVEKGERGSRYSHVEKLLCELLDVEAALVVNNNAAAVLLALNTLAKGKEVIVSRGQLIEIGGSFRIPDVMLQSGAILKEVGTTNKTYDFDYINAITENTALLLKVHTSNYRIVGFTHDIATEELVQIGRKYDIPTMEDLGSGVMVDLREYGLPHEPTVQEVVKAGVDIVTFSGDKLLGGPQAGIIVGKKKYIDLMKKNPLTRAL... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 51668
Sequence Length: 461
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
A0RR46 | MRKAMNKLPKIDKIPNLKEFQNYFKPALLDISKSVLEEIRSKNQNETISEQDVINLIKNAYAKFQNIEPKPLINATGVIIHTNLGRSPISEDLIKQATHLMTSYSNLEYGLSSGKRGDRYAYTSYLLKLLFGCEDALIVNNNAAAVFLILNSFADEKEVLVSRGELVEIGGSFRVPEVMKNSGAILKEIGTTNKTHLSDYENSINENTAMILKVHKSNYDIVGFSSEVSINDIAKLTQKRGILNYYDLGSGYVNTLPYSLSKDEPNVKKLIQSGVDIISFSGDKLFGSVQCGIILGKKELINKLKNNQILRMLRVDKMVL... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 49780
Sequence Length: 442
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
Q9PMS2 | MNKFRTFPQINTLIEDESLKSYPFYIKAFFCKKVVAKLKENFFQDEISKDKLLLEIKKEIKTFYRKDLQSVINASGVVIHTNLGRSVIHEELYEACKDIICNYSNVEFDLENGKRGSRYALVLEKLKMLFECEDALVVNNNAAAVFLVLNSLCYDKEVISSRGELVEIGGSFRVPEVIKAAGVKLCEVGTSNKTHLKDYEQAINENTALILKTHKSNFALMGFHSEVNIKDLHELAKEKELLSYYDLGSGWCENLNEKLIKNEPKIRKLVQECDILSFSGDKLFGSVQAGIILGKKELIEKLKQNQLLRMLRVDKLTLSF... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 50612
Sequence Length: 440
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
Q21VU1 | MTVATQNLTALDVGLAWRNSFAQLGKSFYTPLAPWPLPAPYWVGRSTSTARELGLSESWLDSPELLQVLTGNQPMAGTQPLASVYSGHQFGQWAGQLGDGRAILLGETGGLEVQLKGSGLTPYSRMGDGRAVLRSSIREFLCSEAMQGLGIATSRALCVVGSDAPIRRETVETAAVVTRVAPSFIRFGHFEHFSHHDQHAQLKVLADYVIDRFYPECRASDKFAGNPYAALLEAVSERTAALVAQWQAVGFCHGVLNTDNMSILGLTIDYGPFQFLDAFNPGHVCNHSDQEGRYAFDKQPNIAYWNLFCLGQALLPLIGE... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 54736
Sequence Length: 496
EC: 2.7.7.108
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Q5E3Y2 | MSFWNSLSITTRYSRLPRCFFTYVQPTPLDNSRWLIWNSELAKQFDLPENVHNHSELLDAFSGETVPSVFSPLAMKYAGHQFGCYNPDLGDGRGLLLAEIKDKKGNSFDLHLKGAGLTPYSRSGDGRAVLRSTIREYLCSEAMAGLGIPTTRALGMMTSDTPVFREGYETGALLIRMAETHIRFGHFEHLFYSNLLEELKLLSDKVIEWHFPCCLGEDKPYLAMFNNIVDRTAYMIAQWQAVGFAHGVMNTDNMSIIGQTFDYGPFGFLDDYEPGYICNHSDYQGRYAFNQQPRIGLWNLSALAHSLSPLIDKSDLEKAL... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 55614
Sequence Length: 485
EC: 2.7.7.108
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Q5NYD9 | MKNLVLDNRFVHELPGDPNPSPDVRQVHGACYSRVMPTPVSAPHLIAWSPEVAALLGFDESDVRSPEFAAVFAGNALMPGMEPYAACYGGHQFGNWAGQLGDGRAITLGEAVTTRGDGHTGRWELQLKGAGPTPYSRHADGRAVLRSSIREFLCSEAMHHLGVPTTRALCLVGTGEKVVRDMFYDGRPKAEPGAVVCRVAPSFIRFGNFEIFTSRGDEALLTRLVDFTIARDFPELGGEPATRRAEWFCKVCERTARMIAQWMRVGFVHGVMNTDNMSILGLTIDYGPYGWIDNFDPGWTPNTTDAGGKRYRFGNQPHIA... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 58132
Sequence Length: 523
EC: 2.7.7.108
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B7JH71 | MTKNNEAGWNLDHSYTTLPQSFYTEIPPTPVSSPELVKLNHSLAISLGFNPEELKKEAEIAIFAGNALPEGAHPLAQAYAGHQFGHFNMLGDGRALLIGEQMTPSGKRFDIQLKGSGPTPYSRRGDGRAALGPMLREYIISEAMYALDIPTTRSLAVVTTGEPTYRETKLPGAILTRVASSHIRVGTFQYAAARGSIEDLQSLADYTIKRHYPEIEAHENRYTALLQEVIKKQASLIAKWQLVGFIHGVMNTDNITISGETIDYGPCAFMDNYDQGTVFSSIDTQGRYAYGNQPYMAAWDLARLAESLIPILHEDEEEAL... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 55085
Sequence Length: 488
EC: 2.7.7.108
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Q87VB1 | MKALDELVFDNRFARLGDAFSTHVLPEPIDAPRLVVASESALALLDLAPEQSELPLFAEIFSGHKLWAEAEPRAMVYSGHQFGSYNPRLGDGRGLLLGEVYNDAGEHWDLHLKGAGRTPYSRMGDGRAVLRSSIREFLASEALHALGIPSSRAACVVSSNTPVWREKQEYAAMVLRLAQSHVRFGSLEYLFYTKQPEHLKTLAEHVLTMHYPHCQEQPEPYLAMFREIVERNAELIAKWQAYGFCHGVMNTDNMSILGITFDFGPFAFLDDFDEHFICNHSDHEGRYSFSNQVPIAQWNLSALGQALTPFVSVEALRETI... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 55208
Sequence Length: 487
EC: 2.7.7.108
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Q3IJ32 | MNLMPRYRQVADNFAIEDRPSKVAAPQLLLWNDSLAKAFNINVVPELRASTFSGNEQQAIAAVALGYSGHQFGHFSPRLGDGRAHLLGAVEDAQNQLWDIQLKGSGATPYSRGGDGRCALGPAIREYIMSEAMQALGIKTTRCLAVVGSGETVYRNPPQPGAIVTRLASSHIRVGSFQYLATQGDVAGLKNLADLAIERHYPKIQATGPERYLAFLAAVIKNQVELVVSWMRVGFIHGVMNTDNTLVSGETIDYGPCAMMNSFDFDTVFSSIDKQGRYAFGNQPNIANWNCARLAESLIPLVNDDDEQAVALMTPIIDGF... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 51774
Sequence Length: 469
EC: 2.7.7.108
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Q2KAV8 | MTSALEKNRPGAAFAFDNSYAGLPQRFFAPQAPTPVAEPWLIKLNEPLAEELGLDVEVLRRDGAAIFSGNLVPEGALPLAMAYAGHQFGGFSPVLGDGRAILLGEVVGRNGKRYDIQLKGAGQTPFSRRGDGRAALGPVLREYIISEAMFALGIPATRALAAVTTGEPVYREEVLPGAVFTRVAASHIRVGTFQFFAARGDAEGVRALADYVIDRHYPELKEAENPYAALFEAVSERQAALIARWLHIGFIHGVMNTDNMTVSGETIDFGPCAFMDIYNPSTVFSSIDHHGRYAYANQPAIGQWNLARLGETLLPLIDAD... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 54443
Sequence Length: 500
EC: 2.7.7.108
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Q7UKT5 | MTFDLTFDNRFTRDLPADTEPRNFTRQVHQAGFSRVKPTPVSAPKWVAGSKEVAELIGLDPKWLGSAELTEVLAGNALADGMDPFAMCYGGHQFGNWAGQLGDGRAINLGEVVTADEKHWTLQLKGAGLTPYSRTADGLAVLRSSVREFLCSEAMHHLGVPTTRALSLVLTGEKVLRDMFYDGHPEHELGAIVCRVAPSFIRFGNFEIFASREDTETLQTLVEHTIRSEFSHLLSEPDAEIGPDVIAAMFEEVCRTTAEMVVHWMRVGFVHGVMNTDNMSILGLTIDYGPYGWLEDYDPDWTPNTTDAQGRRYRYAHQPQ... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 60797
Sequence Length: 540
EC: 2.7.7.108
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Q0SJ74 | MRGGPCGGYPRRMTAIPDSTVGTNTAVAGLESTFADELGALTVPWQGAHAPDPTLLVLNEQLAASLRLDVQTLRSEDGVGVLSGSTAPAGAKPVAMAYAGHQFGGYAPLLGDGRALLLGELTSSDGQRVDLHLKGSGPTPFSRGGDGFAVIGPMLREYLVSEAMYALGIPTTRALSVVATGQNVHRYGAEPGAVLARVAASHLRVGTFEYAVRQGEVLQPLADYAIARHYPELTELPPGRDGNRYLSFFEAVVEAQASLVAKWMLTGFVHGVMNTDNTTISGETIDYGPCAFLDAFDPAAVFSSIDHGGRYAFGNQPVVL... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 54961
Sequence Length: 514
EC: 2.7.7.108
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Q24322 | MLNSHNTNHNNNSASNSNYNKGHKMHLKSATAKATIMKHKLSKFYGYGWMQVFLLLTVLVIGNQSAWQENIRPKLYVELGPEDVLKFVGNESVVDHFKLVTKDGNSLLIGARNTVFNLSIHDLVEQQRLVWTSPEDDTKMCLVKGKDEEACQNYIRIMVVPSPGRLFVCGTNSFRPMCNTYIISDSNYTLEATKNGQAVCPYDPRHNSTSVLADNELYSGTVADFSGSDPIIYREPLQTEQYDSLSLNAPNFVSSFTQGDFVYFFFRETAVEFINCGKAIYSRVARVCKWDKGGPHRFRNRWTSFLKSRLNCSIPGDYPF... | Function: Involved in growth cone guidance through its role in axonal repulsion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101057
Sequence Length: 899
Subcellular Location: Cell membrane
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Q26473 | MRAALVAVAALLWVALHAAAWVNDVSPKMYVQFGEERVQRFLGNESHKDHFKLLEKDHNSLLVGARNIVYNISLRDLTEFTEQRIEWHSSGAHRELCYLKGKSEDDCQNYIRVLAKIDDDRVLICGTNAYKPLCRHYALKDGDYVVEKEYEGRGLCPFDPDHNSTAIYSEGQLYSATVADFSGTDPLIYRGPLRTERSDLKQLNAPNFVNTMEYNDFIFFFFRETAVEYINCGKAIYSRVARVCKHDKGGPHQFGDRWTSFLKSRLNCSVPGDYPFYFNEIQSTSDIIEGNYGGQVEKLIYGVFTTPVNSIGGSAVCAFS... | Function: Plays a role in growth cones guidance.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 81215
Sequence Length: 730
Subcellular Location: Membrane
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Q26972 | MVVKILVWSICLIALCHAWMPDSSSKLINHFKSVESKSFTGNATFPDHFIVLNQDETSILVGGRNRVYNLSIFDLSERKGGRIDWPSSDAHGQLCILKGKTDDDCQNYIRILYSSEPGKLVICGTNSYKPLCRTYAFKEGKYLVEKEVEGIGLCPYNPEHNSTSVSYNGQLFSATVADFSGGDPLIYREPQRTELSDLKQLNAPNFVNSVAYGDYIFFFYRETAVEYMNCGKVIYSRVARVCKDDKGGPHQSRDRWTSFLKARLNCSIPGEYPFYFDEIQSTSDIVEGRYNSDDSKKIIYGILTTPVNAIGGSAICAYQM... | Function: Plays a role in growth cones guidance.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 79752
Sequence Length: 712
Subcellular Location: Membrane
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O14140 | MSRAALPSLENLEDDDEFEDFATENWPMKDTELDTGDDTLWENNWDDEDIGDDDFSVQLQAELKKKGVAAN | Function: Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis . Acts as a ubiquitin receptor of the 26S proteasome, by interacting with ubiquitin chains linked by 'Lys-63' and 'Lys-48' . Invol... |
Q14563 | MGWLTRIVCLFWGVLLTARANYQNGKNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFDLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLKAYNQTHLYACGTGAFHPICTYIEIGHHPEDNIFKLENSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPKFISAHLISESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNFKDPK... | Function: Involved in the development of the olfactory system and in neuronal control of puberty. Induces the collapse and paralysis of neuronal growth cones. Could serve as a ligand that guides specific growth cones by a motility-inhibiting mechanism. Binds to the complex neuropilin-1/plexin-1.
Sequence Mass (Da): 888... |
O08665 | MGWFTGIACLFWGVLLTARANYANGKNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPK... | Function: Plays a role in growth cones guidance. May function to pattern sensory projections by selectively repelling axons that normally terminate dorsally. Involved in the development of the olfactory system and in neuronal control of puberty (By similarity).
Sequence Mass (Da): 88813
Sequence Length: 772
Domain: Str... |
P80146 | MKRGGLWLLLGLLVLSACSSNPPAASTQEAPLLGLEAPEAIPGRYIVVYKENADVLPALEALKAALEPGLMQPQGLQAQALRTLGLEGARVDKVYTAALRGVAVEVPDQELARLRQDPRVAYIEADQEVRAFAVQSPATWGLDRIDQRTLPLDGRYTYTATGAGVHAYVVDTGILLSHQEFTGRIGKGYDAITPGGSAQDCNGHGTHVAGTIGGTTYGVAKGVTLHPVRVLDCNGSGSNSSVIAGLDWVTQNHVKPAVINMSLGGGASTALDTAVMNAINAGVTVVVAAGNDNRDACFYSPARVTAAITVGATTSTDYRA... | Function: Serine proteinase with preferred activity for amino acids with aromatic side groups at the P1' side of the scissible bond.
PTM: Contains 4 Cys residues that form two disulfide bonds.
Sequence Mass (Da): 42876
Sequence Length: 410
Subcellular Location: Secreted
EC: 3.4.21.-
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O30126 | MKFDPQKYRELAEKDFEAAWKAGKEILAERSPNELYPRVGFSFGKEHPLFATIQRLREAYLSIGFSEVVNPLIVEDVHVKKQFGREALAVLDRCFYLATLPKPNVGISAEKIRQIEAITKREVDSKPLQEIFHRYKKGEIDGDDLSYLIAEVLDVDDITAVKILDEVFPEFKELKPISSTLTLRSHMTTGWFITLSHIADKLPLPIKLFSIDRCFRREQGEDATRLYTYFSASCVLVDEELSVDDGKAVAEALLRQFGFENFRFRKDEKRSKYYIPDTQTEVFAFHPKLVGSSTKYSDGWIEIATFGIYSPTALAEYDIP... | Function: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Catalytic Activity: ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys)
Sequence Mass (Da): 61181
Sequence Length: 534
EC: 6.1.1.27
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A7I4Y4 | MRFNPQDWKEKSHTNFEGAWHDGPSVITPPGEDKKYPRLRYTRAQPHPIFATINRLREIYLSMGFDECENPVIVEESDIYRQFGPEAMAVLDRVFYIGGLPRPNVGISRKQLDEINDILQSHRSPLVHGHEIPAGDSGNKEPFRPMSRETEEQLRETLHAYKKSEIDGDELTHELAKVLGVDDGIVVHILDSVFPEFRSLVPESSRSTLRSHMTSGWFMTLGSLWERTPLPIKLFSVDRCFRREQAEGPTRLMTYHSASCVVAREDVTIEDGKAVSEALLSAFGYEDFRFQPDDKRSKYYMPDSQTEVYAKHPVHGWVEV... | Function: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Catalytic Activity: ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys)
Sequence Mass (Da): 61483
Sequence Length: 550
EC: 6.1.1.27
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Q59054 | MRFDIKKVLELAEKDFETAWRETRALIKDKHIDNKYPRLKPVYGKPHPVMETIERLRQAYLRMGFEEMINPVIVDEMEIYKQFGPEAMAVLDRCFYLAGLPRPDVGLGNEKVEIIKNLGIDIDEEKKERLREVLHLYKKGAIDGDDLVFEIAKALNVSNEMGLKVLETAFPEFKDLKPESTTLTLRSHMTSGWFITLSSLIKKRKLPLKLFSIDRCFRREQREDRSHLMSYHSASCVVVGEDVSVDDGKVVAEGLLAQFGFTKFKFKPDEKKSKYYTPETQTEVYAYHPKLGEWIEVATFGVYSPIALAKYNIDVPVMNL... | Function: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Catalytic Activity: ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys)
Sequence Mass (Da): 62153
Sequence Length: 539
EC: 6.1.1.27
|
Q8TY66 | MPFDRDKLEELRSLAQRDFDRAWKEGAKLVREPGLRDRYPRLKVETGEPHPLFETIQQLREAYLRAGFREVVNPVIIPEEEVYKQFGPEAAAVLDRCFYLAGLPRPDVGLGADKVEKLAEVLGREPSEDEVERLRETLHAYKKGEIDGDELTHEIAEALDTDDGTAVRILDEVFPELKRLKPEPLEPPLTLRSHMTAGWFITLSEILKREDPPLKLFSIDRCFRREQREDESHLMTYHSASCVVVSDDVTVDTGKAVAEAILRQFGFEDFEFVPDEKMSKYYVPGTQTEVYAYHPDLEDSIEDEELGPGWVEIATFGLYS... | Function: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Catalytic Activity: ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys)
Sequence Mass (Da): 61614
Sequence Length: 544
EC: 6.1.1.27
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Q6LZE1 | MFKREEIIEMANKDFEKAWIETKDLIKAKKINESYPRIKPVFGKTHPVNDTIENLRQAYLRMGFEEYINPVIVDERDIYKQFGPEAMAVLDRCFYLAGLPRPDVGLSDEKISQIEKLGIKVSEHKESLQKILHGYKKGTLDGDDLVLEISNALEISSEMGLKILEDVFPEFKDLTAVSSKLTLRSHMTSGWFLTVSDLMNKKPLPFKLFSIDRCFRREQKEDKSHLMTYHSASCAIAGEGVDINDGKAIAEGLLSQFGFTNFKFIPDEKKSKYYTPETQTEVYAYHPKLKEWLEVATFGVYSPVALSKYGIDVPVMNLGL... | Function: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Catalytic Activity: ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys)
Sequence Mass (Da): 61148
Sequence Length: 537
EC: 6.1.1.27
|
Q9KPM2 | MDMDALTTLPIKKHTALLNRFPETRFVTQLAKKRASWIVFGHYLTPAQFEDMDFFTNRFNAILDMWKVGRYEVALMDGELTSEHETILKALELDYARIQDVPDLTKPGLIVLDMDSTAIQIECIDEIAKLAGVGEEVAEVTERAMQGELDFEQSLRLRVSKLKDAPEQILSQVRETLPLMPELPELVATLHAFGWKVAIASGGFTYFSDYLKEQLSLDYAQSNTLEIVSGKLTGQVLGEVVSAQTKADILLTLAQQYDVEIHNTVAVGDGANDLVMMAAAGLGVAYHAKPKVEAKAQTAVRFAGLGGVVCILSAALVAQQ... | Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 36116
Sequence Length: 328
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
|
Q7M7U5 | MKLAVFDFDSTLMDGETIDILAHHYGVGEEVDRITKGAMEGGLDFYESLKRRVALLRGMELSLVEEICANLTLMEGAKELIQELKRRDYKVVVFSGGFKNATSKARETLGLDADFSNILHHKEGKLTGEVGGEMMFGSSKGEMMQTLQRLLGISPELTMAVGDGANDASMFPFAKQRVAFCAKPILREKANIIIEKKDLREILAHL | Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 22828
Sequence Length: 206
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
|
P42941 | MSKFVITCIAHGENLPKETIDQIAKEITESSAKDVSINGTKKLSARATDIFIEVAGSIVQKDLKNKLTNVIDSHNDVDVIVSVDNEYRQAKKLFVFDMDSTLIYQEVIELIAAYAGVEEQVHEITERAMNNELDFKESLRERVKLLQGLQVDTLYDEIKQKLEVTKGVPELCKFLHKKNCKLAVLSGGFIQFAGFIKDQLGLDFCKANLLEVDTDGKLTGKTLGPIVDGQCKSETLLQLCNDYNVPVEASCMVGDGGNDLPAMATAGFGIAWNAKPKVQKAAPCKLNTKSMTDILYILGYTDDEIYNRQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 34207
Sequence Length: 309
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
|
Q7TNK0 | MGSVLGLCSVASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPGMEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAAVHNGFWFFKFATAVAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNESWVEKMEEGNSRCWYAALLSATALNYLLSLVAIILFFVYYTHPASCSENKAFISVNMLLCIGASVMSILPKIQESQPRSGLLQSSVITIYTMYLTWSAMTNEPETNCNPSLLSIIGFNTTRPVPKDGQSVQWWHPQGIIG... | Function: Enhances the incorporation of serine into phosphatidylserine and sphingolipids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50553
Sequence Length: 453
Subcellular Location: Endoplasmic reticulum membrane
|
Q13530 | MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVV... | Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52580
Sequence Len... |
A6NH21 | MVGAKAGPSPGTSLGLAQQHSGGSSVLVKSPFCQVCCCGPAPCASCCHSRWPSLTASTCSRLFYILLHVGASAICCLLLSRTVVERVWGKTHRIQMPSGLCAHLFGLSDCPVLSGSGAVYRVCAGTATFHLLQAVLLVHLHSPTSPRAQLHNSFWLLKLLFLLGLCAIAFCIPDEHLFPAWHYIGICGGFAFILLQLVLITAFAHSWNKNWQTGAAQDCSWFLAVLLATLGFYSMAGVGAVLLFHYYTHPAGCLLNKMLLSLHLCFCGLISFLSIAPCIRLKQPRSGLLQASVISCYIMYLTFSALSSRPPERVILQGQN... | Function: Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56870
Sequence Length: 518
Subcellular Location: Membrane
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A8WCG0 | MGAKDITGRSTTQGFAQQHGGVSDVVVKTPFYQVSCCGPVSWTSGCHSLTESTCSRLFYILLHMGASAICCLLLSKTVVERVWGKAHGIQMPSVLCAHLFGNSDCPVLSGSGAVYRVCAGTATFHLLQAVLLVRLHSPTSPRAQLHNSFWSLKLLFLLGLCTAAFCIPDEHLFPAWHYIGICGGFTFILLQLVLITAFAQSWNKNWQTGAAQDCSWFLGVLLATLGFYSMAGVGAVLLFHHYTHPDGCLLNKMLLSLHLCFCGLLSLLSIAPCIRLRQPNSGLLQASIISCYIMYLTFSALSSRPPETIIFQGQNHTLCL... | Function: Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54011
Sequence Length: 492
Subcellular Location: Membrane
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Q86VE9 | MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLCLLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSL... | Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm . Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providi... |
P52878 | MKPTRVPNNPCFSSGPCAKHPGYSIEELKDTPFGRSHRSNLGKEKLAEAIKKTRDMLGLPDDYLVGIVPASDTGAFEMCLWSMLGCRGVDVLVWESFSKGWATDITKQLKLKDVRVFEAEYGKLPDLKKVDFKNDVVFVWNGTTSGVKVPNGDWIPENREGLTLCDATSAIFAMDIPYHKLDVITFSWQKVLGGEGAHGMLILSPRAVQRLESYTPAWPLPKIFRLTKGGKLNKKIFEGSTINTPSMLANEDWLATLKWAESVGGLKPLIQRTNDNLAVFEAFVAKNNWIHFLAETKEIRSSTSVCFKVDLSDEKLKELI... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q99K85 | MEATKQVVNFGPGPAKLPHSVLLEIQKQLLDYRGLGISVLEMSHRSSDFAKIIGNTENLVRELLAVPNNYKVIFVQGGGSGQFSAVPLNLIGLKAGRSADYVVTGAWSAKAAEEAKKFGTVNIVHPKLGSYTKIPDPSTWNLNPDASYVYFCANETVHGVEFDFVPDVKGAVLVCDMSSNFLSRPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFSLRECPSVLDYKVQAGNNSLYNTPPCFSIYVMGMVLEWIKNNGGAAAMEKLSSIKSQMIYEIIDNSQGFYVCPVERQNRSRMNIPFRIGNAKGDEALEKRF... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
O33062 | MADQLTPSLDIPAALKPRDGRFGSGPSKVRPEQLQALTNTAATLFGTSHRQAPVKNLVGRVRAGLAELFSLPDGYQVILGNGGATAFWDAAAFGLIDKRSLHLTYGEFSSKFASAVAKNPFIDEPIVIKSDPGSAPKPTGDPSVDVIAWAHNETSTGVAVPVRRPTGSGGALIAIDATSGAGGLPVDIAQTDAYYFAPQKNFASDGGLWLAIMSPAALARVDSITASGRWVPDFLSLPIAVENSLKNQTYNTPAICTLALLAEQLDWLLGNGGLEWAVKRTADSSQRLYAWAEDRPYTTPFVVDPALRSQVVGTIDFTDD... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q742L2 | MSMADQLQIPADIKPRDGRFGCGPSKVRPEQLQALSTTAAPLFGTSHRQAPVKNLVGRLRSGLAELFSLPDGYQVILGNGGATAFWDAAAFGLIDKRSLHLSYGEFSSKFAAAVAKNPFVGDPVVIKSDAGSAPEPQSDPSVDLIAWAHNETSTGVAVPVRRPVDSGDALVAIDATSGAGGLPVDIGETDAYYFSPQKNFAGDGGLWLALMSPAALARVESIAASGRWVPDFLSLPIAVENSLKDQTYNTPAIGTLALMAEQVDWMLGNGGLDWAVKRTADSAGRLYSWAEERDYTTPFVADPKLRSQVVGTIDFVDDVD... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
A3Q635 | MAELTIPADLKPRDGRFGSGPSKVRPEQLQALAAAGDLFGTSHRQAPVKNLVGRVRDGIKQLFSVPEGYDVILGNGGSTAFWDAAAFGLIDKRSLHLTYGEFSAKFASAVAKNPFVGDPIVVKADPGSAPEPQSDPSVDVIAWAHNETSTGVAVPVQRPADSGDALIVIDATSGAGGLPVDIAQADAYYFAPQKNFAGDGGLWLAVVSPAALARIEAIGQSGRWVPDFLSLPIAVENSLKNQTYNTPAIGTLVLLADQLDWLNGNGGLDWAVKRTADSSQRLYSWAEASSYATPFVTDPALRSQVVGTIDFADDVDAAAV... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q1D2L9 | MRVINFNAGPAGLPLPALERARDELIDFQGSGMSVMEHSHRGREYEGVHDEAISLLTRLLGIPDTHQVLFLTGGASQQFAQVPMNFLRPGASADYLMTGVWSEKAFDEAKYYGTPRVAVSTARPDKRYTRVPRQDELRLESSAAYVHLTSNNTIFGTQWHTFPDVGNVPLVADMSSDFLWKGFDVSRFGLIYAGAQKNLGPSGVTLVVADKAFIARGRTDIPKIFRYTTHAENNSLYNTPPTLAIYLVRNVLAWIQSVGGLAQLEQWNREKAALLYGAVDRHPEFYRAPVERESRSVMNVVFQLPTEALDASFVADAKQQ... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
O34370 | MSLYPIYNFSAGPAVLPEAVLETARQEMLDYNGTGFPVMAMSHRSEMFLSILHHAEQDLRQLLKVPDNYKILFLQGGATTQFNMAAMNLAHGFRTADAVVTGNWSRIAYEQMSRLTDTEIRLAAHGGEQFDYLDLPPVETWDVAPDSAFVHFAVNETVNGLQYREVPRLSEGMPPLVCDMSSEILSREFDVADYGLIYAGAQKNIGPAGVTVVIVREDLLERCPNDIPDVFNYRSHINRDGMYNTPSTYAIYMSGLVFRWLQAQGGVKKIEAVNRLKAQTLYETIDGSGGFYINRIRPNARSKMNVVFQTGDEELDRRFV... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q59196 | MSKRAYNFNAGPAALPLEVLERAQAEFVDYQHTGMSIMEMSHRGAVYEAVHNEAQARLLALLGNPTGYKVLFIQGGASTQFAMIPMNFLKEGQTANYVMTGSWASKALKEAKLIGDTHVAASSEASNYMTLPKLQEIQLQDNAAYLHLTSNETIEGAQFKAFPDTGSVPLIGDMSSDILSRPFDLNQFGLVYAGAQKNLGPSGVTVVIVREDLVAESPKHLPTMLRYDTYVKNNSLYNTPPSFGIYMVNEVLKWIEERGGLEGVQQANRKKASLIYDAIDQSGGFYRGCVDVDSRSDMNITFRLASEELEKEFVKASEQE... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
P58004 | MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPT... | Function: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex . In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling . Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 s... |
P58005 | MNRGGGSPSAAANYLLCTNCRKVLRKDKRIRVSQPLTRGPSAFIPEKEVVQANTVDERTNFLVEEYSTSGRLDNITQVMSLHTQYLESFLRSQFYMLRMDGPLPLPYRHYIAIMAAARHQCSYLINMHVDEFLKTGGIAEWLNGLEYVPQRLKNLNEINKLLAHRPWLITKEHIQKLVKTGENNWSLPELVHAVVLLAHYHALASFVFGSGINPERDPEISNGFRLISVNNFCVCDLANDNNIENASLSGSNFGIVDSLSELEALMERMKRLQEEREDEEASQEEMSTRFEKEKKESLFVVSGDTFHSFPHSDFEDDMII... | Function: May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway . May also regulate the insulin-receptor signaling pathway through activation of TORC2 (By similarity). This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By... |
Q9CYP7 | MNRGGSSASASANYLLCTNCRKVLRKDKRIRVSQPLTRGPSAFIPEKEVVQANTADERTNFLVEEYSTSGRLDNITQVMSLHTQYLESFLRSQFYMLRMDGPLPLPDRHYIAIMAAARHQCSYLINMHVDEFLKTGGIAEWLNGLEYVPQRLRNLNEINKLLAHRPWLITKEHIQKLVKTGENNWSLPELVHAVVLLAHYHALASFVFGSGINPERDPGIANGFRLISVSSFCVCDLANDNSIENTSLAGSNFGIVDSLGELEALMERMKRLQEDREDDETTREEMTTRFEKEKKESLFVVPGETLHAFPHSDFEDDVIV... | Function: May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway . May also regulate the insulin-receptor signaling pathway through activation of TORC2 . This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). M... |
Q8N4B1 | MKLNERSLAFYATCDAPVDNAGFLYKKGGRHAAYHRRWFVLRGNMLFYFEDAASREPVGVIILEGCTVELVEAAEEFAFAVRFAGTRARTYVLAAESQDAMEGWVKALSRASFDYLRLVVRELEQQLAAVRGGGGMALPQPQPQSLPLPPSLPSALAPVPSLPSAPAPVPALPLPRRPSALPPKENGCAVWSTEATFRPGPEPPPPPPRRRASAPHGPLDMAPFARLHECYGQEIRALRGQWLSSRVQP | Function: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.
Sequence Mass (Da): 27215
Sequence Length: 249
Domain: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential fo... |
Q1RMU7 | MKLNERSVAHYALSDSPADHTGFLRTWGGAGTPPTPSGAGRKCWFVLKGNLLFSFESREGRAPLSLVVLEGCTVELAEAPVPEEFAFAIRFDAPGVRPHLLAADGPAAQEAWVKALSRASFGYMRLVVRELESQLREARHSLDLHRRSSWKAVSSRCKPQAPDRWSPGLENGHSLSRDCSPMGLVEEGGSRPAGRGLAEWELQGPASLLLGRGQSPVSPETSCFSTLHEWYGREIMELRRAWLQRAQENQPECKDQDRP | Function: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.
Sequence Mass (Da): 28626
Sequence Length: 259
Domain: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential fo... |
Q6ICB4 | MKLNERSVAHYALSDSPADHMGFLRTWGGPGTPPTPSGTGRRCWFVLKGNLLFSFESREGRAPLSLVVLEGCTVELAEAPVPEEFAFAICFDAPGVRPHLLAAEGPAAQEAWVKVLSRASFGYMRLVVRELESQLQDARQSLALQRRSSWKSVASRCKPQAPNHRAAGLENGHCLSKDSSPVGLVEEAGSRSAGWGLAEWELQGPASLLLGKGQSPVSPETSCFSTLHDWYGQEIVELRQCWQKRAQGSHSKCEEQDRP | Function: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.
Sequence Mass (Da): 28338
Sequence Length: 259
Domain: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential fo... |
Q14B98 | MKLNKRSVAHYALSDSPADHTGFLRSWGGPGSPPTPSGTGRRYWFVLKGNLLFSFETRESRVPLSLVVLEGCTVELAEAPVPEEFAFAIRFDAPGVRPHLLAADGQAAQEAWVKALSRASFGYMRLVVRELESQLQDARQSLALHRCASQRAVASCSKSQAPDHRAPDPENGHFLPRDRSSIGTVEERGIRPIGRDLTEWELQGPASLLLSMGQSPVSPESSCFSTLHDWYGKEIMELRRGWQQRAKGSQTENKSQNRP | Function: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.
Sequence Mass (Da): 28707
Sequence Length: 259
Domain: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential fo... |
O74738 | MEKLLHEALQNGCKLHKSVEFIQSRDDNACFGSYIAVAQNDIAPDQLLISCPFEYAITYNKAKEELKKLNPNFESCNPHITLCTFLALESLKGIQSKWYGYIEYLPKTFNTPLYFNENDNAFLISTNAYSAAQERLHIWKHEYQEALSLHPSPTERFTFDLYIWSATVFSSRCFSSNLIYKDSESTPILLPLIDSLNHKPKQPILWNSDFQDEKSVQLISQELVAKGNQLFNNYGPKGNEELLMGYGFCLPDNPFDTVTLKVAIHPDLPHKDQKAAILENDCQFQLSNLVFFLPKSPDKEIFQKILQCLAVVTASSLELR... | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates ribosomal protein L23 (rpl23a and rpl23b).
Sequence Mass (Da): 62320
Sequence Length: 547
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
O74405 | MSNKQNIESEVSWVKSKGAFVHPSLEFSVIPDAGSCVLANNDINENTVLLKLPPNILINKRTCSRYSFRDKLTSFQFLSWLISEDVHSNLEISPYYTKALPQGFSFHPVTLTSDHPLWSILPDEVRNSLLERKNVMAFDYEQVKKFVSVDQPTFQWGWLCVNTRCLYYDTGSKNTEDHLTLAPIFEYFNHSPEAQTALINTRGTITIKSTRRIDKGEQIFLCYGPHGNDKLFTEYGFCLSNNPNISIQLDRFIEFDKWQQSFLQDHGYWNDYTCSLHGASFRTLVGVRTLLVSPSEKLNDASYDQTRRVLQYINGFSDGS... | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates 60S ribosomal protein L12 (rpl1201 and rpl1202) at 'Lys-4' and may dimethylate L12 also at 'Lys-40' and 'Lys-41'. Overexpression causes a severe growth defect. Has a role in meiosis.
Sequence Mass (Da): 44080
Sequence Leng... |
A0A163UT06 | MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR | Function: Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro . Does not tri-methylate 'Lys-4' of histone H3 in vitro . Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes in primary spermatocytes . Togethe... |
Q99287 | MADRPAIQLIDEEKEFHQSALQYFQQCIGNRDVGLDYHVISVFGSQSSGKSTLLNVLFNTNFDTMDAQVKRQQTTKGIWLAHTKQVNTTIEIDNDRPDIFVLDVEGSDGSERGEDQDFERKAALFAIAVSEVLIVNMWEQQIGLYQGNNMALLKTVFEVNLSLFGKNDNDHKVLLLFVIRDHVGVTPLSSLSDSVTRELEKIWTELSKPAGCEGSSLYDYFDLKFVGLAHKLLQEDKFTQDVKKLGDSFVMKGTENYYFKPQYHHRLPLDGWTMYAENCWDQIERNKDLDLPTQQILVARFKTEEISNEALEEFISKYDE... | Function: Cooperates with the reticulon proteins RTN1 and RTN2 and the tubule-shaping DP1 family protein YOP1 to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
Location Topology: Multi-pass membrane protein
Se... |
Q7TSK2 | MRPAALLLLPSLLALLAHGLSSEAPITGEGHATGIRETDGELTAAPTPEQSDRGVHFVTTAPTLKLLNHHPLLEEFLQEGLEREEAPQPALPFQPDSPTHFTPSPLPRLTNQDNRPVFTSPTPAVAAAPTQPHSREKPWNLESKPPELSITSSLPPGPSMAVPTLLPEDRPSTTPPSQAWTPTQEGPGDMDRPWVPEVMSKTTGLGVEGTIATSTASGDDEETTTTIITTTVTTVQPPGPCSWNFSGPEGSLDSPTAPSSPSDVGLDCFYYISVYPGYGVEIKVENISLQEGETITVEGLGGPDPLPLANQSFLLRGQVI... | Function: May play a role in cell-cell recognition and in neuronal membrane signaling. Seems to be important for the achievement of the necessary balance between dendrite elongation and branching during the elaboration of a complex dendritic arbor. Involved in the development of appropriate excitatory synaptic connecti... |
Q6AX42 | MMPLAGIAWNLMLLFSAVQGLPLQDGEGTQHPDLLNNPPKGSVEPVALEQLVHQAILKKDFLAQDVFFPGTTAIPTRAAPISLTEGVSDASGVLTTAVGGAFSLPPQLSTLIPPSPAPTGGPGPSPEAEEETTTTLITTTTVTTVHSPVLCNNNISESEGLLEAPEYGGSTFFGGLDCTYSVSVYLGYGVEIRVERLNLSKEEALSIEGLEEDRRFLLANETLMAEGQVIRSPTNHVAVRFQTYRATSPGAFRLRYQAFVLSCVFPPRPENGEVTVTDLHPGGAANFRCSAGFTLKGGESLVCLNISRPEWSGKPPVCAA... | Function: May play a role in cell-cell recognition and in neuronal membrane signaling.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98394
Sequence Length: 900
Subcellular Location: Cell membrane
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Q15637 | MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAEL... | Function: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor.
PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly. Isoform 6 is phosphorylated on Ser-463.
... |
Q64213 | MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHTLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAEL... | Function: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor (By similarity).
PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly.
Sequence Mass (Da): 7040... |
P24939 | MAPKKKLQLPPPPPTDEEEYWDSQAEEVLDEEEEMMEDWDSLDEASEAEEVSDETPSPSVAFPSPAPQKLATVPSIATTSAPQAPPALPVRRPNRRWDTTGTRAAPTAPAAAAAAATAAVTQKQRRPDSKTLTKPKKSTAAAAAGGGALRLAPNEPVSTRELRNRIFPTLYAIFQQSRGQEQELKIKNRSLRSLTRSCLYHKSEDQLRRTLEDAEALFSKYCALTLKD | Function: Promotes alternative splicing of late transcripts by promoting splicing at weak 3' splice sites. Required for the temporal activation of major late pre-mRNA splicing at late times of infection. Induces the splicing and expression of the late capsid vertex protein.
PTM: Phosphorylated in vitro by human PKA and... |
P24940 | MAPKKKLQLPPPPTDEEEYWDSQAEEVLDEEEEDMMEDWESLDEEASEVEEVSDETPSPSVAFPSPAPQKSATGSSMATTSAPQAPPALPVRRPNRRWDTTGTRAAHTAPAAAAAAATAAATQKQRRPDSKTLTKPKKSTAAAAAGGGALRLAPNEPVSTRELRNRIFPTLYAIFQQSRGQEQELKIKNRSLRSLTRSCLYHKSEDQLRRTLEDAEALFSKYCALTLKD | Function: Promotes alternative splicing of late transcripts by promoting splicing at weak 3' splice sites. Required for the temporal activation of major late pre-mRNA splicing at late times of infection. Induces the splicing and expression of the late capsid vertex protein.
PTM: Phosphorylated in vitro by human PKA and... |
P19416 | MPPKGNKQAIADRRSQKQQKLQEQWDEEEESWDDSQAEEVSDEEEMESWESLDEELEDKPPKDEEEEIIASAAAPSSKEPARSQPPTGKVGPSPPRPGLLKASRRWDTVSIAGSPPAPVAPTKRSEKTTRPRKEKTSAIATRQDTPVAQELRKRIFPTLYAIFQQSRGQQLELKVKNRSLRSLTRSCLYHRREDQLQRTLEDAEALFNKYCSVSLKD | Function: Promotes alternative splicing of late transcripts by promoting splicing at weak 3' splice sites. Required for the temporal activation of major late pre-mRNA splicing at late times of infection. Induces the splicing and expression of the late capsid vertex protein (By similarity).
PTM: Phosphorylated in vitro ... |
Q15459 | MPAGPVQAVPPPPPVPTEPKQPTEEEASSKEDSAPSKPVVGIIYPPPEVRNIVDKTASFVARNGPEFEARIRQNEINNPKFNFLNPNDPYHAYYRHKVSEFKEGKAQEPSAAIPKVMQQQQQTTQQQLPQKVQAQVIQETIVPKEPPPEFEFIADPPSISAFDLDVVKLTAQFVARNGRQFLTQLMQKEQRNYQFDFLRPQHSLFNYFTKLVEQYTKILIPPKGLFSKLKKEAENPREVLDQVCYRVEWAKFQERERKKEEEEKEKERVAYAQIDWHDFVVVETVDFQPNEQGNFPPPTTPEELGARILIQERYEKFGES... | Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex . Involved in pre-mRNA splicing as a component of pre-catalytic sp... |
P82347 | MPQEQYSHHRSTMPSSEGPHIYKVGIYGWRKRCLYFFVLLLMILILVNLAMTIWILKVMNFTIDGMGNLRITEKGLKLEGDSEFLQPLYAKEIKSRPGNALYFKSARNVTVNILNDQTKVLTQLVTGPKAVEAYGKRFEVKTVSGKLLFSADDSEVVVGAERLRVLGAEGTVFPKSIETPNVRADPFKELRLESPTRSLVMEAPKGVEINAEAGNMEAICRSELRLESKDGEIKLDAAKIKLPRLPRGSYTPTGTRQKVFEVCVCANGRLFLSQAGTGSTCQINTSVCL | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
PTM: Disulfide bonds are present.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32133
Sequence Length: 289
S... |
Q8GMH4 | MTDQCVVSAPVRVRTRRLDVKETGALPAYRALAEHFGPDEVYLLESAAGPARDRRHQFVGFGALLSLSVTDRVVRVEGVPALRGLLLERAGALLEDGPQGLRLRTAGGLWPLLRAMRDMFDAEGSASGFRFGFLGFFGYDTARYIEDLPHLIENRPGLPDVRMVLHRGSVVTDLATGRCELLLHESPYWPGLAPETVTGLLADVEQAWPDPSADGFPASAVTDDSAPEVFANDVERCLKHIAVGDIYQVQIGHELSIRSTADPADVYQRLRGRNASPYMYLAGIDGHRLIGASPELFVRIEDGEVTMRPIAGTVPRSGAD... | Function: Converts chorismate to 2-amino-4-deoxychorismate (ADIC). Involved in the biosynthesis of the benzoxazolinate moiety of the enediyne antitumor antibiotic C-1027.
Catalytic Activity: (2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine
Sequence Mass (Da): 53461
Sequence Length: 493
EC: 2.6.1.... |
Q8GME2 | MSPIIAPPAELVDPKDRVQLRRVFGDFPTGVTVVTVGGSEPRGMTANSFTSVSLSPPLVLICVGKDAVMHQRLTALPTFAVSVLEAGQEKAARHFADHSRPPGVDQFDTVDWVLGEESGAPLIAGAVAHLECAIHRLYEGGDHTIFLGEVITATRWPAREGMLFSGGRFRRFAPDADEGRAA | Function: Reductase component of a two-component system involved in the biosynthesis of the enediyne antitumor antibiotic C-1027 . SgcE6 provides the FADH(2) required by both the halogenase SgcC3 and the monooxygenase SgcC through free diffusion . Accepts only NADH and FAD as substrates .
Catalytic Activity: FADH2 + NA... |
P39362 | MILHPSLASANPLHYGRELTALDNLDFGSLHLDIEDSSFINNITFGMKTVQAVARQTPHPLSFHFMLARPQRWFNALAEIRPAWIFVHAETLDYPSETLTEIRHTGARAGLVFNPATPIDAWRYLASELDGVMVMTSEPDGQGQRFIPSMCEKIQKVRTAFPQTECWADGGITLAAAQQLAAAGAQHMVIGRALFSSSDYRATLAQFATL | Cofactor: Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+).
Function: Probable pentose-5-phosphate 3-epimerase.
Sequence Mass (Da): 23214
Sequence Length: 210
Pathway: Carbohydrate degradation.
EC: 5.1.3.-
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O43556 | MQLPRWWELGDPCAWTGQGRGTRRMSPATTGTFLLTVYSIFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEISNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEDFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDLKEGVYVMVGADVPFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVIRGEGILPDGGEYKPPSDSLKSRDYYTDFLIT... | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49851
Sequence Length: 437
Subcellular Location: ... |
Q0VCU7 | MVREQYTTITEGTHIERPENQAVYKIGIYGWRKRCLYLFVLLLLIVLLVNFALTIWILRVMWFSPVGMGHLHVTADGLHLEGESEFLFPLYVKEIRSRVDSSLLLQSTQNVTMNARNTEGEVTGRLKVGPQMVEVQSQQFQIHSKDGKPLFTVDEEKVMVGTDKLRVTGPEGALFEHSVETPLVRPDPPQDLRLESPTRSLSMDAPKGIHIQAPAGKIEALTQMDIVLQSSDGTVVLDAETVCLPELALGSQGPAGSSQGLYEVCVCPDGKLYLSVAGMGTTCHEHSHLCL | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
PTM: Disulfide bonds are present.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32179
Sequence Length: 291
S... |
Q8SQ72 | MVREQYTTTTEGTHIQRPENQCVYKIGIYGWRKRCLYLFVLLLLIILLVNFALTIWILKVMWFSPTGMGHLRVTKDGLRLEGESEFLFPLYAKEIHSRVDSSLLLQSTQNVTVNARNSEGEVTGRLKVGPKMVEVQSQQFQINSKDGKPLFTVDEKEVVVGTDKLRVTGPEGALFEHSVETPLVRADPFQDLRLESPTRSLSMDAPKGVHIKAHAGKIEALSQMDIIFQSSDGMLVLDAETVCLPKLVQGTQGPAGSSQRLYEICVCPDGKLYLSVAGVGTTCHEHSHICL | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
PTM: Disulfide bonds are present.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32398
Sequence Length: 291
S... |
Q13326 | MVREQYTTATEGICIERPENQYVYKIGIYGWRKRCLYLFVLLLLIILVVNLALTIWILKVMWFSPAGMGHLCVTKDGLRLEGESEFLFPLYAKEIHSRVDSSLLLQSTQNVTVNARNSEGEVTGRLKVGPKMVEVQNQQFQINSNDGKPLFTVDEKEVVVGTDKLRVTGPEGALFEHSVETPLVRADPFQDLRLESPTRSLSMDAPRGVHIQAHAGKIEALSQMDILFHSSDGMLVLDAETVCLPKLVQGTWGPSGSSQSLYEICVCPDGKLYLSVAGVSTTCQEHNHICL | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32379
Sequence Length: 291
Subcellular Location: Cell membrane... |
P82348 | MVREQYTTVTEGTHIERPENQHIYKIGIYGWRKRCLYLFVLLLLAILVVNLALTIWILKVMWFSPIGMGHLHVTADGLRLEGESEFLFPLYAKEIRSRVDSSLLLQSTQNVTVSARNSEGEVTGRVKVGAQMVEVQSQHFQINSEDGKPLFSAEEQDVVVGTGRLRVTGPEGALFEHSVETPLVRADPFQDLRLESPTRSLSMDAPRGVHVKANAGKLEALSQMDIILQSSEGVLVLDAETVGLTKLKQGTQGPAGSSNGFYEICACPDGKLYLSMAGEVTTCEEHSHVCL | Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32082
Sequence Length: 291
Subcellular Location: Cell membrane... |
Q8GMH2 | MSAQLKILAINGSERDGNTADVLRHAARVAENRGVDFEAVDLRSIRMERCGPCGDCNDRPVACTLADGVPEVVAKMVAADGIIFAAPVHGFGTASLMQTFIERAGVGYLRFDRPLSNKVAGIISVARRYSAGEVWAQLTVNALLNRMILVGSGFPATVHALHRGDALKDEEGLTNVSRLVERMTDMIELLDEHRRLTGRSDVLASNEVNERVGLALNELQAQP | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2-amino-4-deoxychorismate (ADIC) to 3-O-enolpyruvoylanthranilic acid (OPA). Involved in the biosynthesis of the benzoxazolinate moiety of the enediyne antitumor antibiotic C-1027.
Catalytic Activity: (2S)-2-amino-4-deoxychorismate + FMN = 3-(1-carboxyvinyloxy)anthr... |
Q7CXU0 | MTDMPNRKPPLSGIRVIELARVLAGPWAGQMLADMGADVIKVENPEGGDDTRAWGPPFVESADGENLSAAYYHATNRGKRSIVADLKTPEGCALVRRLVRTADVVIENFKRDGLAKYGLDYESLRVLNPKLIYCSITGFGQTGPYADFAGYDYIVQGMSGFMSITGEPDGQPMKAGVAVADIFTGIYSVSAIQAALIHAMRSGEGQHIDMALLDVQSAVLANQNMNYLISGRPPIRLGNAHPNISPYEVVPTADGFLILAVGNDGQFRRLCNILGIGAIADDERYATNKARVAHKVEVRQIISTETLKWNKRDLLTACET... | Function: Is involved in L-lysine degradation and provides glutaryl-CoA for biotin synthesis. Catalyzes the conversion of glutarate to glutaryl-CoA via the transfer of CoA from succinyl-CoA.
Catalytic Activity: glutarate + succinyl-CoA = glutaryl-CoA + succinate
Sequence Mass (Da): 43385
Sequence Length: 400
Pathway: A... |
Q9NP31 | MEFPLAQICPQGSHEAPIPTFSTFQITDMTRRSCQNLGYTAASPQAPEAASNTGNAERAEEVPGEGSLFLQAETRAWFQKTQAHWLLQHGAAPAWFHGFITRREAERLLEPKPQGCYLVRFSESAVTFVLTYRSRTCCRHFLLAQLRDGRHVVLGEDSAHARLQDLLLHYTAHPLSPYGETLTEPLARQTPEPAGLSLRTEESNFGSKSQDPNPQYSPIIKQGQAPVPMQKEGAGEKEPSQLLRPKPPIPAKPQLPPEVYTIPVPRHRPAPRPKPSNPIYNEPDEPIAFYAMGRGSPGEAPSNIYVEVEDEGLPATLGHP... | Function: Could be a T-cell-specific adapter protein involved in the control of T-cell activation. May play a role in the CD4-p56-LCK-dependent signal transduction pathway. Could also play an important role in normal and pathological angiogenesis. Could be an adapter protein that facilitates and regulates interaction o... |
Q9NRF2 | MNGAPSPEDGASPSSPPLPPPPPPSWREFCESHARAAALDFARRFRLYLASHPQYAGPGAEAAFSRRFAELFLQHFEAEVARASGSLSPPILAPLSPGAEISPHDLSLESCRVGGPLAVLGPSRSSEDLAGPLPSSVSSSSTTSSKPKLKKRFSLRSVGRSVRGSVRGILQWRGTVDPPSSAGPLETSSGPPVLGGNSNSNSSGGAGTVGRGLVSDGTSPGERWTHRFERLRLSRGGGALKDGAGMVQREELLSFMGAEEAAPDPAGVGRGGGVAGPPSGGGGQPQWQKCRLLLRSEGEGGGGSRLEFFVPPKASRPRLS... | Function: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways mediated by Janus kinase (JAK) and receptor tyrosine kinases, including the receptors of insulin (INS), insulin-like growth factor I (IGF1), nerve growth factor (NGF), brain-derived neurotrophic... |
O14492 | MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTR... | Function: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 ac... |
Q9JID9 | MNGATPSSAAAPAPVPDWRQFCELHAQVAAVDFAHKFCRFLRDNPTYDTPDAGTSFSRHFAANFLAVFSEEVRRVLGSAADTMEPEPAVTSVTSALKTATYGHSRSSEDVSAHAATKARVRKGFSLRNMSLCVVDGVRDLWHRRSSPEPDGGATPKAAEPASEPRDKWTRRLRLARTLAAKVELVDIQREGALRFMVADDAASGPGGTAQWQKCRLLLRRAVAGERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTGLSCARGGCLASR... | Function: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 ac... |
Q6FMH8 | MSLENAVRVVSTDEKGNQASSTKLIELLHSRVDALTTTNIELTTKLQELLGNLDTVQQRERKLKESAASLRHEGDNVTLMLNRKERKLTEVKEAIVELTTKLGEAKEVNHSLKQKFEDEGLTSEESLRESISEVKTEYDTLVKSHEIYESSNDIQCKSLEDRFSQALLIHGENMKALDGTAEQILANNSELVSQLRATENKAESARTSIRNASIDTAAKVDLEKWLFLYKEAQRICEEFASKTDTKLPDELQAIIDDPVLKELDARFALDEIQYGKTRNKRIPSNPLLSNSQAAARRVASPSANYSPRVSSAQGSLPGIT... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
Q6CRH4 | MKMTEAQEFLTPTKGVNSSKFNINHGHFITNLENQESPSKLGAYTPGKYSTSRVIESLHKQIDELTSTNLKMTSQCHQLVNELESSGKKQNKQLETISRLQTENMNLNAILDRKTNRMNELESSLKKQTVFNEDAAKKNLELEETVKKLSLENEKLTEQSTLYKIQYEAIVDAHQSYKQFFTNETSTLRNDLMSLKQSMTKQLESKTKEVLAIDEKIQNKLESLDSAQESFKKHASEQIEDNIKELRLDSWQSSLREAQALLKEYKSQAQAEGITIQEQPKASIPQLRNPKRKTSGQKRTSFYGTPTGFSIPSNKQTPPS... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
C5DLA5 | MSNQEVDFQAAHLESPMKMSPSKVSMNHGAFMANMQNGYSPTREGATAGSSSTRVIEALHAQIDSLTKTNLDLTVQSNNLLSRLESSNNTQSKHLESISTLKHENDNLGLMLSRKERRVRDLEQQLSQLKHSYEEAAMDNKTMRHQLQTSGQREGTLENQLQQLQVQYDALVDGQKRYREKYDLEVEELKKSLQDFKRDNEMYLTKNIQTVVSNNTALQTKINQYSGKYKNLESLSQQHMQELSREVEGMASKLDLAKWEKLYEESRNMAIEYSEKTNVPLSPSFLAQHGAKSGSRSPSTSSSSTFVHPSQIRVPKVRHS... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
A5E5U9 | MAGDSASLSLSPIKSDKAAVVSESPVKMKPGSSSSKVIDTLHTTIDSLSLEIATLKQTNQELSRKSQVATAKNDSFVDQLANLKHENDMLSALLKRKERRILDLEDQNSELSNSVESLNMLTKQMKMRCEKLSDSSMQSMAEYERLKISYDALVASCNEYKQHYKTELDTLQKSLDTYKQENHKQWETLNELISSNDKDIDTLLDSLNNKKKLMDNIYVNKNTKVLTMLSTLATLVKAHGTESKNVLGDNAQTIEFLLEKYPDLEEKILEKEQIEIDINSILYASKDALENTSFDEEDVTLINSPELEPSSDGNFPAQQL... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
A3LXM3 | MEDNTASNKPTSRVIDSLHSQIDDLKTELETVKISHDDYKKKYVLVSQKNDSFVDQLANAKHENDMINALLKRKERRIADLEDQYNELSSSNESLQLNNKNMKIRCENLQQSSASSTAEYERLKIAYDALIASQVEYKRHYQKELNTLASKLEAYKTENKQRFQDLSSKLSSNDKDIDTLLDSMTNKRKALDNLYVNKNKTILELLTSLAKAAKIHGLDTKSTLEENTVAISSLLEKYPDLQEKILTHEKVEVDLDELISESNETLSNCSFESEATLVNSPELSDSASQSKNADHLKQDVKASSLSRSNTLQAKKRKNKR... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
A7TJJ7 | MSLEDSRISNEDDSELLPPNKVVSSHGVFMASMNGSPQKIMRPSSVSGGSVNGSVSGSSQIGSGPNSNNNNNSSNNNNNSGSISSTKVIEALHEQIDALTNTNLKLTVQSQGLLEKLENSQQREGKFMENIASLRHENDNLSTMLNRKTRKLKDTELELEELKEKFDKITTEKKVLDDDLNKTSASETKLKEEMSMIENQYNSLIDSHEYYKDKYLQEINQLKRSLEDLTTEQENYLKRTNENNKLVEEKIDNYNNSFNQLKEINESLNNIIITKCESAIQELDLPNWVNLYKESKILVIDYAQQMNLEIPNNFKELVRD... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
P38272 | MSDQDNTQTSSSKLAPHHNIFMANLESSPTKDRNTSSQNASSSRVIESLHDQIDMLTKTNLQLTTQSQNLLSKLELAQSKESKLLENLNLLKNENENLNSIFERKNKKLKELEKDYSELSNRYNEQKEKMDQLSKLAKNSSAIEQSCSEKLQNMEVNYNSLLESQNLYRDHYSDEISKLNEKIGLLELELSNQNLNYGSDTSSNSDIELNLNKFNDSVKDLKSLETEKDSKLSKIITHSLDELNLQSWLNLYQTNENLISTFAEKMDLKDVLKRNDEKISNKGAVVQTLKKNVQTQVESNNADALSSNNAQDMLPIKMVK... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
C5DUI8 | MTEDFEVNLGTGGEDNSSSTMEHRVLDSPPRVVIPEDTESPAKLAPNHGIFMASINKSSPAGKKSGEGAVLGMGAQSTKDNSTPRQNSSMLSTRVIESLHDQVDTLTSTNLQLTVQSKNLLDKLDTAQQKESKMLENSASLKHENENLVSMLNRKTRRLKDVEEELASHKKNHDSLEEEKTALQKKWESSSSEEATLRQQMEMVQAQYDALVDSHQYYKSHYSSQISTLSEQLENLKLEQRNYTQRVSDEANTFNAKLLEFDSKHANLQQAEETRVKYLESKYDSLTQQLDLPSWVQLYRESKNMVLEFAEKMKLKIPSD... | Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into th... |
Q753C3 | MPIYQLALPRSVLPRCRAVRYSRLLHSARCYSQDSQPKPGNTILQQLRKKLEPFCNSTKDKLEQTCAQVRYSSMQLRYHLEKARASVQEANKKLVQQEREGENSMLTFNDDLENKSKIVDLPSERERKRRQWSRKLEFYIDSLQETIFTATKALNDVTGYSSIEKLRKSIDMMETQLQETKRKLMQLREAHSDAVAVRNQSQRQVNELLQRKHMWSPGDLESFTRLYKEDADNVRRQEEANASLKAMEAKEEELSNSLHRAILTRYHEEQIWSDKIRRTSTWGTFILMGLNILLFLVVQLLLEPWKRRRLTNSFEDKVKR... | Function: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51476
Sequence Length: 447
Subcellular Location: Mitochond... |
Q4WV30 | MQPMPLLLRQSLRSSANFARTSLPIRPQFLPAAGPNLQPAREIQRSFSVCVRCQFRSQSPLYSSPEKDTSKDDAATQQSKDGSSTLTPGDESAKVEPDAETQRPSPAAGEQDTLQGFYQDAKNEPKRESAEKKGLPSYLEERRSQLSKQFTEMMDNLQSNIFVAGQRLNDLTGYSAIEALKKDIQLQEERLREARQRVREAKNAYAAAINRRSASQREVNELLQRKHAWSAADLERFTHLYRNDHTNEVAEMETQEALSAAERESEEAAAQLSKSILSRYHEEQVWSDKIRRMSTWGTWGLMGVNVLLFLVFQIAVEPWR... | Function: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55938
Sequence Length: 502
Subcellular Location: Mitochond... |
A1CAL7 | MARFRASNILGDPFALATISIAILAWIIAFISSIIANIKMADYPNHAWWAIAYMFCCTIGVTVVVGSDTGLVYGVAVVGYLSAGLVLTSLSVNTLVYKGNSSAQAAAAGFILLSMIIIVWIFYFGSTPQATHRGFIDSFALNKEGGNAYGNGRPISTAFGHRPETTSTSAPQMYTSAQLNGFETSSPISGYPGGAPGSENRSSSQPRFGNPSASNLPANNNGQSQDEVPQPTEYPYRAKAIYSYDANPEDANEISFSKHEILEVSDVSGRWWQARKSSGETGIAPSNYLILL | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31192
Sequence Length: 292
Subcellular Location: Cell membrane
|
B0Y3Z4 | MAKFRASNILGDPFALATVSISILAWLIACIASIISDIKTDYPNYSWWAVAYMFCCIMGVTIVFGSDTGLVYGVAVVGYLSTGLVLTTLAVNSLVYADESSSQAAAAGFILMSMVIVVWIFYFGSSPQATHRGFIDSFALNKESSGAYGNRPMSTAYGPRPDTMSTSAPQMYTSAQLNGFETSSPVSGYPGGGPGSENRSSSQARFGNPSASNVAGNNSGQDEVPPPTEYPYKAKAIYSYDANPEDANEISFSKHEILEVSDVSGRWWQARKSNGETGIAPSNYLILL | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Regulates radial hyphal growth and germination. Involved in virulence and mediates resistance to oxidative stress (By similarity).
Location Topology: Multi-pass membrane protein
... |
Q5AQ36 | MGFSLSNFTSDPFAISTVSFGIMAWVVAIAGAASSKQENFPHFSWWGISYQIVIILIIFVLYANNNIELYKFTLVGLVSIAFIYTTNSTNNLIYNSNSAGNLCCAAGCILLSILNLIWILYFGGHPESPTNQFIDSFSLRGQGHEQLGSGSHNHNANNANNNIPIGAGNAIIGKGEMSPYDDRFAASGVNQPTSESLRLASGPQMGNGPFTTTGAIINPNLQQPLSGSIGGSAHHTPTNINNNNNNNNNTGYMTSSHLTGLENFSSPHVPGSGAGAGLGVGAGRDLTHNSNGGGGGSGGGPASANNSNNTNKRNTIYTDS... | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Mediates resistance to oxidative stress. Controls the activation of the CEK1 MAP kinase. Influences the molecular weight and polymer distribution of cell wall mannan. Involved in... |
Q6FTC4 | MSGRRGKIINPRTRGAVRNVGFRNLISDPFAISSILIGLISWVITLGGCISVQVNEDFPRFTWWGIAFQFLIILMLIGFYIYDLVDYYRNFLTASIGVAFVYSTNSANYLIYGSGNQKAAASAGVVLLSMVNLIWIFYYGGDNASPINRWVDSFSLNGIRPSPFEAAKIKAYRRSSKQTQFRGSSVKLTHSTNNLHSASENLGLDNGFYNNPHTSNYVSSTALTEFENTGPPYPSASDLPTNNNAPLRSPQLGNNTIGDTYITATTNNNTNTTMGDTMGLYADLADESFPYRVKALYSYEADSADAYEMSFEQGEILMVS... | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39044
Sequence Length: 353
Subcellular Location: Cell membrane
|
E6RET3 | MFGGHSFDVGYVMRHPVFLVTFIIAIPSWIIAFAGQCAAEAKYSSSNGRTPVAGTLWFNIWLQLMLTVSLAISSDDLALHRFQLSIFLAIATALAVGGVEFIFQTPGAYIAIGVGWLLLTMVNLVWIVYLTSEEDTFLYNVLNSGGNGGLSSHNRRIGTSVQRRDETPGYGGGEMGLGNSMGGMPRGISSNTINSGGYGGGYAPASMEGTPQKVTSVTRNEYGHTGVQSPGIDESVPRPQRAKALYAYSASPDDPNEVSFMKGEILEVVDATGKWFQVRTPAGVTGIAPSNYLVLL | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31587
Sequence Length: 296
Subcellular Location: Cell membrane
|
Q9P864 | MSTPEYSTSAKSRFDITNLTTDPFVVATWSVAMISWVIAFIGSIVANIEGSFPRFTWWGLVFQLLMLVFLPAVYCFDVVEWYRLFLTCGYSIAFIYTTNSATNLVWSGGSATGAASAGVILLSMVNLIWVFYYGSDNASPINQWIDSFSLRGPKRSSVSPFHNSRPISHDKYSGSENDEFKHSSWNNQRYMSSTALSGLENVSQGDTLETTPFNSPDHDGLGTNITAGGTNITIDEFPYTARALYNYQKSPDDENEISFEKDEILKVNDIHSRWWQAKRANGEIGICPSNYVELIE | Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33134
Sequence Length: 296
Subcellular Location: Cell membrane
|
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