ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
P40316 | MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKDADLPQLQNTLSIRKNDQLRKLSQISRSRSRANHNDLLSNSRKLQKYGSVLGYNALPKMKSLVLKDLADSGKNEESSDDDEGNEDSESKLGKKLQSALLKQDSSDGENELNGGLGLFNEQGGLQQLIKNSTKNEQKTKNDKSDKTDDYDIEIAPQRQEPLPYVPEGYSPFQQDDIEKLKTFNSPYKLDLEDEDDTPDKVDLLPLEQIDEEGEKDETECITRNQEEGAALPLLSKNFKEVAAVPTMELVYSEEGLDPEELEDLVT | 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 is ubiquitinated, conducting to its destruction and to the liberation of ESP1.
PTM: Phosphorylated by CDC28. The phosphorylation may be important for ESP1 localization to the nucleus.
Sequence Mass (Da): 41838
Sequence Length: 373
Domain: The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Subcellular Location: Cytoplasm
|
F6CD01 | MFSTLKNAFKDKEIRNKIYFTLFILLLYRIGANITVPGINVKAITQVAQTGLVPMLDTVSGGGLDNYSIFSLGVSPYITAQIVIQLLQMDIVPTLVEWGKQGEVGRRKTNQVTRYLTLVVAFVQSIGITLGFNALTQMGLVKNQTPQTYVEIAIIMTAGTMLLTWLGDEITDKGLGNGVSVIIFAGIIARLPSGLYQIYKEEIINNSASDRWQGILFFIAVIVAILIVTQLVTWVEQADRRIPIQYTRRATISGSESFLPLKVNVSGVIPVIFASSFIVTPATILMAFQRTQGDQQWFKVMNQIFSLQTTPGVIIYTLLIILFTFFYAFVQVNPEKLAENLQKQGAYIPSVWPGKDTQDYVSKMLIKLSTVGSIFLGLVALLPQLATNFWNLPSSIGLGGTSLLIVIGVVLELSRQINGLLMKREYVGFIR | 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 composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47691
Sequence Length: 431
Subcellular Location: Cell membrane
|
Q74L41 | MEKKNLLNVIKKVSFSLFIVIIYVMGLYIPLPFAEGTKQYMEAVKNTPISILGAFSGANFTRISIFSIGLNPLMFSMLIIQLLSFTHSFGFDALSPKQVQYLMQFLTMIITIIQAALLVFAFTNRRNGLEDFEMILILSAGSCLVVWLCYRNMKYGVGASAPVILTSILNGAIPNIISNVKLLLTMKYAWIWLAALAIFILLLIKFWLAFTKAYYPLKVVNPSLPASSNLMTVPLGLNMAAMMMYMVGMAILTLPLMVGRYFSSSSLINNWVFQASFSAVMGILIFYFFTFVNFDPKEQAKSFRNNHYYIPNIAPGRPTQRYLNRLIWIIAFPGAVLNAFQLVFGLYGGNFLGNYAGFAIIPMNVVMITMFMGGIKDQIDTILFPYRYDRLLKDN | 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
|
F6CFW7 | MILIIYRALFFVTIPGVNSAALAKLSNNSSLTMLSMFSGGGFENFSIMSLGVTAYITAQIIVQLLQADVIPTFTQWSKEGQTGRKKLDQVTRSLTLVLGLVQATGITLGINTLTNGKFMIENNPFTIIVIAVSMTAGSFIAMWLGDLITENGLGNGISVIITAGILVRFPSMINDVIKGVTFGTKVNWIRFSELMIGAAILILLIVWFTRSELRIPIQYARRAQLTGKDSYLPLKIIVPGVIPVIFASTIMTIPQTILMFFNAGQNSSWYRVVQTFFTLSTTSGVIIYGLMIIFFEYLYSIVQIEPDKFADNLEKQEAYIPNVYPGDPTKEFIQNMLNYLSLPGSLFLMLVSIIPLLVANSVSSSLQIGLSGSSILIITGVLIEIGRQIKGLKLKREYGTFLSTDFSLDD | 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 composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45057
Sequence Length: 410
Subcellular Location: Cell membrane
|
D8MEB8 | MKGENINNIHLVLKKMLWTSLIVFIFLIGRNILIPGVDAKQLARFLNNQYLLQIVNGTTGGDLSRMSLFALGLGPWMSATILWRVLTLIKRFDLKKIPIERTFLFKIAIAIIIGFIQSIAIISNIDINPKISIFAQTQFGAMATISLIMVSGAVFLVWLSNMNEILGIGGPTVLILASMIINWPTNVSLYILENVRSSLDINSVILMLVIMISIVFLVLLTVVVQRAQRQIPIRRILVNNNFYQQSYLPIQINPAGGMPLMYSMTLLVLPQYILQAVHYWLPNNVLVENGLDNIAITKPLGVTAYIIILFALSIGFAFININPDQIAEDLQQNSDYIDNVEPGDATREYITEIVFRLSFVGALYMSLIAGFPLYFGIIDKQYTQYALTAGSIIILVNLVINIIDQMKALLTKNNYSALFFE | 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
|
Q2FUW2 | MLKLLQQYEYKIIYKRMLYTCFILFIYILGTNISIVSYNDMQVKHESFFKIAISNMGGDVNTLNIFTLGLGPWLTSMIILMLISYRNMDKYMKQTSLEKHYKERILTLILSVIQSYFVIHEYVSKERVHQDNIYLTILILVTGTMLLVWLADKNSRYGIAGPMPIVMVSIIKSMMHQKMEYIDASHIVIALLIILVIITLFILLFIELVEVRIPYIDLMNVSATNMKSYLSWKVNPAGSITLMMSISAFVFLKSGIHFILSMFNKSISDDMPMLTFDSPVGISVYLVIQMLLGYFLSRFLINTKQKSKDFLKSGNYFSGVKPGKDTERYLNYQARRVCWFGLALVTVIIGIPLYFTLFVPHLSTEIYFSVQLIVLVYISINIAETIRTYLYFDKYKPFLNQYW | 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 Length: 403
Subcellular Location: Cell membrane
|
G5EDF7 | MERKGRERKLPGMKIVMPTPVETPTMNLEDRCLIKLTNESEEIEIAATDLVVLEELGKGGYGIVEKMQHRQSGIIMAVKRIKSSINDQSQKQMLNELDACRRSDCCPQMVRFYGAMFREGDVWICMEVMDTSLDKFYRHAYKIGKHIPEPFIGKMALSVIEGLNFMKEQLNLIHRDVKPSNILLNRHGQVKICDFGISGHLTNSMAKTVQAGCKPYMPPERIDGETKSAYDVRADVWSLGITIIEIAVGTHPYANWKTPFEQLKQVVKEPPPKLPMESGFSVDCQYFVKRCLEKDYNERPKYPELLAMPFMEQARNEKQFSMARFINEILDTVWRR | 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 cell fates in olfactory AWC neurons during neuronal development. Activation results in the repression of odorant receptor str-2 expression in one of the 2 AWC neurons . Involved in resistance to pathogenic Gram-positive and Gram-negative bacterial and fungal infection . Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 . Probably by promoting pmk-1-mediated activation of skn-1, involved in the up-regulation of gcs-1 and glutathione-S-transferase gst-4 expression upon bacterial infection . Probably downstream of tir-1, required for the expression of antimicrobial peptide nlp-29 in the epidermis in response to fungal infection or physical injury . Regulates susceptibility of B.thuringiensis pore-forming toxin Cry5B and Cry21A . Involved in the response to oxidative stress . May regulate transcription factor daf-16 localization during oxidative stress . By phosphorylating pmk-1, regulates skn-1 localization during oxidative stress . By phosphorylating and activating pmk-1, plays a role in the stabilization of transcription factor rnt-1 in the intestine during oxidative stress . Up-regulates expression of gcs-1 in intestine upon arsenite treatment . Regulates germline proliferation in response to osmotic stress, starvation and germline apoptosis induced by heavy metals, such as Cu(2+) . In association with mek-1, regulates germline cell apoptosis in response to oxidative, osmotic and heat shock stresses . Plays a role downstream of tir-1/nsy-1 in regulating susceptibility to anoxia . In males, by regulating pqn-41 expression, involved in non-apoptotic death of the linker cell which guides gonad elongation during larval development . Involved in egg laying .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38700
Sequence Length: 336
EC: 2.7.12.2
|
O13858 | MSHASKNYNAQLTAAAASTALHGTKKIYNSNENDRAVNSFLGNRTSYGEAVNGSPQYDYMRSRMSTLGSANQPMAPPSLRNRSSVYLPTPAGPPQIPVNTGKRYTLTSSSANYMTKSERQMRPPKSYDFPPSQQVRPSTSRSPSYASYNSEEVNFQSYQDPRLLPRTSQMYMPDNNYSPAVKSPAAQRRSSSYMVPANSRGSPANYNTPYYPTAIPPPIEEYSPSVSLPTSPVAEESYNNVQRSSTVRNNTTQKSVLKKPSRKMSPAYTSSYRQNSPSSQVPPVSKKHVIIYENKEGSSSSESVYEDVFEDFDPSGSNQASLRSTSTIHYTPSSKRISVIPPNTSNIGSRVVSRSGQNNNQPAQPGQYNQQSQPVQSYQSGQSTQHFQPVQPIQPVQSTQYYQPSSPVQPVQNGVPAPPMQPVQSTQYYQPSSPVQPVQNVKPAQPAQPSLEDAAKRRVEEMLRQMDITPTASSTTANNAYASAEPHPSAFPDDMNSVFSDSSFERERDSGRGRSTNLFSKFKSGRSRSKASGEAPYSYPAPPVPSVNNAGARLTLRDSGAAPEATYSLRQPSNHAYSEGRSYTFTGGQPPSVPTMPYGSRFANDSDSMMGSTADFSSKKKGGKFKAFKKFFKMRF | 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
Subcellular Location: Cell membrane
|
A6TQL2 | MNKGRILSQLPSVDELIKNLEHDKLEKMIPRSVVVEQTRITVDTYRKAILTMDEGSLRDYQIDITSMHDEIKQACESFCSMNLREVINGTGVILHTNLGRSLLSEEIKGQIWEVASGYSTLEIDVTTGKRGSRYNHVVDVLKHLTGAEDALVVNNNAAAVMLVLGTIAKGKEVIVSRGELVEIGGSFRVPDVMEQSGGKLREVGTTNKTHLWDYEGAISDETAALLKVHTSNYRIMGFTESVGLEEIVELGNRYHIPTIEDIGSGVLIDLQKYGLAHEPTVQESVKAGVDIVTFSGDKLLGGPQAGIIVGKRKWIEKMKKNPLTRAIRVDKLTMAALEATLKLYLDEDTAIKHIPTLKMLTENLDTISERASDLFRKLQALDEHLLVRIEEDFSQVGGGSMPLEKLPTKVITLEHTILSAAQMETKLRNFKRPIFTRIRDEKVMMDLRTIREKDFVFIVEALKTVAK | 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) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.9.1.1
|
O67140 | MKSLLRQIPQISKVVEIFKKKYPEIYVVKAAREVAEKYRKEIIEGKRKDLNGFLEDVERKIKSLMKPNIKRVINATGVVINTNLGRAPLSKDVINFISEIANGYSNLEYNLEEGKRGSRIAHIEKYLNELTGAESSFVVNNNAGAVFLVLNTLAEGKEVIISRGELVEIGGSFRIPDIMKKSGAILREVGTTNKTKVSDYEGAINQNTALLMKVHKSNFYMEGFVEEVKLEDLVKLGHKYGIPTYYDAGSGLLINLKEFGISVDEPNFRDCISLGIDLVSGSGDKLLGGPQAGIIVGKKNLIEKIKKNPIARALRIDKLTLSGLEMTLKLYFEKRYEDIPVIRMLTQDEKALRQKAKRLEKLLKDIPGLKISVIKDKAKPGGGSLPELELPTYCVAIRHDRLSSQELSRRLRLAEPPIVCRIREDQLLFDMRTVFHEDLKTIKKTLQELLSI | 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) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.9.1.1
|
Q8R8W4 | MEDLYRKLPSVDEILREEKINEVLKFNKREVVKNCIREVLERYREKIRRGEVKKIDIEKILEDVVSQIEEKKKMSLRRVVNGTGIILHTNLGRALFPPQVKEHLLDIAFCYSTLEYDVEKGERGSRYSHVEKLLCELLDVEAALVVNNNAAAVLLALNTLAKGKEVIVSRGQLIEIGGSFRIPDVMLQSGAILKEVGTTNKTYDFDYINAITENTALLLKVHTSNYRIVGFTHDIATEELVQIGRKYDIPTMEDLGSGVMVDLREYGLPHEPTVQEVVKAGVDIVTFSGDKLLGGPQAGIIVGKKKYIDLMKKNPLTRALRVDKLCLVSLECVLRIYRDSNPVEAIPTLKMLTAKPSQLYEKAAILNKLVLTIPKVKSKVVEITSLSGGGSLPEESLPSYGITLEVEGFDTEDLERRLRIRDIPIITRIVDGVVTIDVRTLLEGDEEVILHALEEITGVCQ | 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) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.9.1.1
|
A0RR46 | MRKAMNKLPKIDKIPNLKEFQNYFKPALLDISKSVLEEIRSKNQNETISEQDVINLIKNAYAKFQNIEPKPLINATGVIIHTNLGRSPISEDLIKQATHLMTSYSNLEYGLSSGKRGDRYAYTSYLLKLLFGCEDALIVNNNAAAVFLILNSFADEKEVLVSRGELVEIGGSFRVPEVMKNSGAILKEIGTTNKTHLSDYENSINENTAMILKVHKSNYDIVGFSSEVSINDIAKLTQKRGILNYYDLGSGYVNTLPYSLSKDEPNVKKLIQSGVDIISFSGDKLFGSVQCGIILGKKELINKLKNNQILRMLRVDKMVLSMLNETIKAYLNKDFHLIKPINQIYKTLSELEVQAKKVLENIKLEASIKETKTFVGGGTMPNKSYPSIGLFFKGNANKNEFKFRKYGIIGRIENAEFLLDFRSIFENDIENIIKIINGMSDE | 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) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.9.1.1
|
Q9PMS2 | MNKFRTFPQINTLIEDESLKSYPFYIKAFFCKKVVAKLKENFFQDEISKDKLLLEIKKEIKTFYRKDLQSVINASGVVIHTNLGRSVIHEELYEACKDIICNYSNVEFDLENGKRGSRYALVLEKLKMLFECEDALVVNNNAAAVFLVLNSLCYDKEVISSRGELVEIGGSFRVPEVIKAAGVKLCEVGTSNKTHLKDYEQAINENTALILKTHKSNFALMGFHSEVNIKDLHELAKEKELLSYYDLGSGWCENLNEKLIKNEPKIRKLVQECDILSFSGDKLFGSVQAGIILGKKELIEKLKQNQLLRMLRVDKLTLSFLNESLKAYLQKDYEKIITLKLLNDDLSFIEKKALRVQKELKFQTQLKKSKSLVGGGSMPDKSLDTYILTFQGDALKLQTRFRKENIIGRIENDEFVLDFRTIRENELQKLILTINQMENL | 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) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.9.1.1
|
Q21VU1 | MTVATQNLTALDVGLAWRNSFAQLGKSFYTPLAPWPLPAPYWVGRSTSTARELGLSESWLDSPELLQVLTGNQPMAGTQPLASVYSGHQFGQWAGQLGDGRAILLGETGGLEVQLKGSGLTPYSRMGDGRAVLRSSIREFLCSEAMQGLGIATSRALCVVGSDAPIRRETVETAAVVTRVAPSFIRFGHFEHFSHHDQHAQLKVLADYVIDRFYPECRASDKFAGNPYAALLEAVSERTAALVAQWQAVGFCHGVLNTDNMSILGLTIDYGPFQFLDAFNPGHVCNHSDQEGRYAFDKQPNIAYWNLFCLGQALLPLIGEQELAIAALESYKTVFPAAFERLMFAKLGLLDASDSTATVDRALLQDILQLLAREQVDYTIFWRRLSHCGVATDAQTVRDLFVDRSAADAWLLRYSERLEHIPQGLAADLMLKTNPKFVLRNYLGEQAIQAAKLKDFSQVETLLMLLESPFEEHPGFDKYADFPPDWASSIEISCSS | 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
|
Q5E3Y2 | MSFWNSLSITTRYSRLPRCFFTYVQPTPLDNSRWLIWNSELAKQFDLPENVHNHSELLDAFSGETVPSVFSPLAMKYAGHQFGCYNPDLGDGRGLLLAEIKDKKGNSFDLHLKGAGLTPYSRSGDGRAVLRSTIREYLCSEAMAGLGIPTTRALGMMTSDTPVFREGYETGALLIRMAETHIRFGHFEHLFYSNLLEELKLLSDKVIEWHFPCCLGEDKPYLAMFNNIVDRTAYMIAQWQAVGFAHGVMNTDNMSIIGQTFDYGPFGFLDDYEPGYICNHSDYQGRYAFNQQPRIGLWNLSALAHSLSPLIDKSDLEKALEQYEIKLHDYFSQLMRKKLGLLSKQEGDTRLFESMFELLSQNAVDYTRFMRALSYLDSQDKQTVVDLFVDREAATLWIDLYLTRCKLEVDSFDMRCSKMRKVNPKYVLRNYLAQQAIVKANEGDFSDVKILSTLLASPFDEHPDFERYAELPPEWGKRMEISCSS | 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
|
Q5NYD9 | MKNLVLDNRFVHELPGDPNPSPDVRQVHGACYSRVMPTPVSAPHLIAWSPEVAALLGFDESDVRSPEFAAVFAGNALMPGMEPYAACYGGHQFGNWAGQLGDGRAITLGEAVTTRGDGHTGRWELQLKGAGPTPYSRHADGRAVLRSSIREFLCSEAMHHLGVPTTRALCLVGTGEKVVRDMFYDGRPKAEPGAVVCRVAPSFIRFGNFEIFTSRGDEALLTRLVDFTIARDFPELGGEPATRRAEWFCKVCERTARMIAQWMRVGFVHGVMNTDNMSILGLTIDYGPYGWIDNFDPGWTPNTTDAGGKRYRFGNQPHIAHWNLLQLANALYPVFGAAEPLHEGLDLYARVFDEENRRMLAAKLGFEAFGDEDATLVETLHALLTRAEVDMTIFFRGLASLDLEAPSIDPLRDAFYSAEKAAVAEPEMNSWLAAYTKRTKQERTPGDQRRVRMNAVNPRFVLRNYLAQEAIDAAEQGEYALVSELLDVMRHPYDEQPGRERFAARRPDWARNRAGCSMLSCSS | 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
|
B7JH71 | MTKNNEAGWNLDHSYTTLPQSFYTEIPPTPVSSPELVKLNHSLAISLGFNPEELKKEAEIAIFAGNALPEGAHPLAQAYAGHQFGHFNMLGDGRALLIGEQMTPSGKRFDIQLKGSGPTPYSRRGDGRAALGPMLREYIISEAMYALDIPTTRSLAVVTTGEPTYRETKLPGAILTRVASSHIRVGTFQYAAARGSIEDLQSLADYTIKRHYPEIEAHENRYTALLQEVIKKQASLIAKWQLVGFIHGVMNTDNITISGETIDYGPCAFMDNYDQGTVFSSIDTQGRYAYGNQPYMAAWDLARLAESLIPILHEDEEEALKIAQDEISKFSVQYEKQWFLGMKKKLGLFSNEEQDQSLIEQLLKMMEKFKADYTNTFRSLTLNTIENTALFESPEFKEWYKLWQSRLEKQEESKENAYEMMKNNNPSIIPRNHRVEEALEAAVTNGDYSVMEKLLEALSNPYAYATEQEEYCVPPAPTNRPYRTFCGT | 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
|
Q87VB1 | MKALDELVFDNRFARLGDAFSTHVLPEPIDAPRLVVASESALALLDLAPEQSELPLFAEIFSGHKLWAEAEPRAMVYSGHQFGSYNPRLGDGRGLLLGEVYNDAGEHWDLHLKGAGRTPYSRMGDGRAVLRSSIREFLASEALHALGIPSSRAACVVSSNTPVWREKQEYAAMVLRLAQSHVRFGSLEYLFYTKQPEHLKTLAEHVLTMHYPHCQEQPEPYLAMFREIVERNAELIAKWQAYGFCHGVMNTDNMSILGITFDFGPFAFLDDFDEHFICNHSDHEGRYSFSNQVPIAQWNLSALGQALTPFVSVEALRETIGLFLPLYQAHYLDLMRRRLGLTVAQDQDDKLVSQLLQLMQNSGVDYTLFFRRLGDQPAAQALRALRDDFVDIKVFDDWAQAYQARIAAEENGTEQARKERMHAVNPLYILRNYLAQNAIEAAEKGDYEEVRRLHQVLCTPFTEQPGMEGYAQRPPDWGKHLEISCSS | 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
|
Q3IJ32 | MNLMPRYRQVADNFAIEDRPSKVAAPQLLLWNDSLAKAFNINVVPELRASTFSGNEQQAIAAVALGYSGHQFGHFSPRLGDGRAHLLGAVEDAQNQLWDIQLKGSGATPYSRGGDGRCALGPAIREYIMSEAMQALGIKTTRCLAVVGSGETVYRNPPQPGAIVTRLASSHIRVGSFQYLATQGDVAGLKNLADLAIERHYPKIQATGPERYLAFLAAVIKNQVELVVSWMRVGFIHGVMNTDNTLVSGETIDYGPCAMMNSFDFDTVFSSIDKQGRYAFGNQPNIANWNCARLAESLIPLVNDDDEQAVALMTPIIDGFAEQFNVEFSAMWATKLGLAGTDTADKELIAELLQLLKEHQLDYTNTFDALTESLTGGMSIPEVLVQWAGKWQKRTDDRSYTVMRAANPRVIPRNHVIEKILSEYNKTGSSELLHEFMQVMHTPYENTDKLAKFQDAPSSDKEYYTFCGT | 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
|
Q2KAV8 | MTSALEKNRPGAAFAFDNSYAGLPQRFFAPQAPTPVAEPWLIKLNEPLAEELGLDVEVLRRDGAAIFSGNLVPEGALPLAMAYAGHQFGGFSPVLGDGRAILLGEVVGRNGKRYDIQLKGAGQTPFSRRGDGRAALGPVLREYIISEAMFALGIPATRALAAVTTGEPVYREEVLPGAVFTRVAASHIRVGTFQFFAARGDAEGVRALADYVIDRHYPELKEAENPYAALFEAVSERQAALIARWLHIGFIHGVMNTDNMTVSGETIDFGPCAFMDIYNPSTVFSSIDHHGRYAYANQPAIGQWNLARLGETLLPLIDADQDSAVDKANAVIRAYGERFQAHWLKGMRAKIGLEGEEDGDLELVQALLALMQAQGADFTLTFRRLSDLAGDDAAEPGFATSFREPDSSGEWLARWRGRLSRDPQTAAGRAAAMRSVNPVFIPRNHRVEQAIEAAVESADFSLFEALLKVLAKPYEDQPSFAAYMEPPKPNERVLQTFCGT | 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
|
Q7UKT5 | MTFDLTFDNRFTRDLPADTEPRNFTRQVHQAGFSRVKPTPVSAPKWVAGSKEVAELIGLDPKWLGSAELTEVLAGNALADGMDPFAMCYGGHQFGNWAGQLGDGRAINLGEVVTADEKHWTLQLKGAGLTPYSRTADGLAVLRSSVREFLCSEAMHHLGVPTTRALSLVLTGEKVLRDMFYDGHPEHELGAIVCRVAPSFIRFGNFEIFASREDTETLQTLVEHTIRSEFSHLLSEPDAEIGPDVIAAMFEEVCRTTAEMVVHWMRVGFVHGVMNTDNMSILGLTIDYGPYGWLEDYDPDWTPNTTDAQGRRYRYAHQPQIAQWNLVALANALVPLVKEAEPLQRGIAVYVEEFQKSWHSMMAGKLGLSKYESETDDELVDSLLTLLQLAETDMTIFYRRLADIELGTREQPVTLELAAVLRHLSEAHYVADEVTEEYQQALMDWMRSYQSRVLADDGFPAEDSQRRQRMNAVNPKYVLRNYLAQLAIDACDKGDDSLVSELLEVLRRPYDDQPGKERFAEKRPEWARHRPGCSMLSCSS | 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
|
Q0SJ74 | MRGGPCGGYPRRMTAIPDSTVGTNTAVAGLESTFADELGALTVPWQGAHAPDPTLLVLNEQLAASLRLDVQTLRSEDGVGVLSGSTAPAGAKPVAMAYAGHQFGGYAPLLGDGRALLLGELTSSDGQRVDLHLKGSGPTPFSRGGDGFAVIGPMLREYLVSEAMYALGIPTTRALSVVATGQNVHRYGAEPGAVLARVAASHLRVGTFEYAVRQGEVLQPLADYAIARHYPELTELPPGRDGNRYLSFFEAVVEAQASLVAKWMLTGFVHGVMNTDNTTISGETIDYGPCAFLDAFDPAAVFSSIDHGGRYAFGNQPVVLKWNLARLAETLLTLFDSTPDDAITAVSAVLATFDERYDGHYAAGMAAKLGLAGELVDRALVDDLLTLLEEHGADWTGTFRALADELRGHSTPLDGLVPREHIGPWLERWRGDLTKHGRGAAETADAMDCVNPLYIPRNHQLDAALRAATDGRLAPFEKLLEVVTHPFDRRDEWSDYTTPAPPSFSKSFQTFCGT | 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
|
Q24322 | MLNSHNTNHNNNSASNSNYNKGHKMHLKSATAKATIMKHKLSKFYGYGWMQVFLLLTVLVIGNQSAWQENIRPKLYVELGPEDVLKFVGNESVVDHFKLVTKDGNSLLIGARNTVFNLSIHDLVEQQRLVWTSPEDDTKMCLVKGKDEEACQNYIRIMVVPSPGRLFVCGTNSFRPMCNTYIISDSNYTLEATKNGQAVCPYDPRHNSTSVLADNELYSGTVADFSGSDPIIYREPLQTEQYDSLSLNAPNFVSSFTQGDFVYFFFRETAVEFINCGKAIYSRVARVCKWDKGGPHRFRNRWTSFLKSRLNCSIPGDYPFYFNEIQSASNLVEGQYGSMSSKLIYGVFNTPSNSIPGSAVCAFALQDIADTFEGQFKEQTGINSNWLPVNNAKVPDPRPGSCHNDSRALPDPTLNFIKTHSLMDENVPAFFSQPILVRTSTIYRFTQIAVDAQIKTPGGKTYDVIFVGTDHGKIIKSVNAESADSADKVTSVVIEEIDVLTKSEPIRNLEIVRTMQYDQPKDGSYDDGKLIIVTDSQVVAIQLHRCHNDKITSCSECVALQDPYCAWDKIAGKCRSHGAPRWLEENYFYQNVATGQHAACPSGKINSKDANAGEQKGFRNDMDLLDSRRQSKDQEIIDNIDKNFEDIINAQYTVETLVMAVLAGSIFSLLVGFFTGYFCGRRCHKDEDDNLPYPDTEYEYFEQRQNVNSFPSSCRIQQEPKLLPQVEEVTYAEPVLLPQPPPPNKMHSPKNTLRKPPMHQMHQGPNSETLFQFQPDGYNTQQSYRGRDNFGTLRSHQVMGDNYRRGDGFSTTRSVKKAVNNTNTRNRSLGRARRQPPRHGIVTQHRSNSPQQQQQQSQQPHSSSGSSPVMSNSSSSPAPPSSSPSPQESPKNCSYIYRD | 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
|
Q26473 | MRAALVAVAALLWVALHAAAWVNDVSPKMYVQFGEERVQRFLGNESHKDHFKLLEKDHNSLLVGARNIVYNISLRDLTEFTEQRIEWHSSGAHRELCYLKGKSEDDCQNYIRVLAKIDDDRVLICGTNAYKPLCRHYALKDGDYVVEKEYEGRGLCPFDPDHNSTAIYSEGQLYSATVADFSGTDPLIYRGPLRTERSDLKQLNAPNFVNTMEYNDFIFFFFRETAVEYINCGKAIYSRVARVCKHDKGGPHQFGDRWTSFLKSRLNCSVPGDYPFYFNEIQSTSDIIEGNYGGQVEKLIYGVFTTPVNSIGGSAVCAFSMKSILESFDGPFKEQETMNSNWLAVPSLKVPEPRPGQCVNDSRTLPDVSVNFVKSHTLMDEAVPAFFTRPILIRISLQYRFTKIAVDQQVRTPDGKAYDVLFIGTDDGKVIKALNSASFDSSDTVDSVVIEELQVLPPGVPVKNLYVVRMDGDDSKLVVVSDDEILAIKLHRCGSDKITNCRECVSLQDPYCAWDNVELKCTAVGSPDWSAGKRRFIQNISLGEHKACGGRPQTEIVASPVPTQPTTKSSGDPVHSIHQAEFEPEIDNEIVIGVDDSNVIPNTLAEINHAGSKLPSSQEKLPIYTAETLTIAIVTSCLGALVVGFISGFLFSRRCRGEDYTDMPFPDQRHQLNRLTEAGLNADSPYLPPCANNKAAINLVLNVPPKNANGKNANSSAENKPIQKVKKTYI | 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
|
Q26972 | MVVKILVWSICLIALCHAWMPDSSSKLINHFKSVESKSFTGNATFPDHFIVLNQDETSILVGGRNRVYNLSIFDLSERKGGRIDWPSSDAHGQLCILKGKTDDDCQNYIRILYSSEPGKLVICGTNSYKPLCRTYAFKEGKYLVEKEVEGIGLCPYNPEHNSTSVSYNGQLFSATVADFSGGDPLIYREPQRTELSDLKQLNAPNFVNSVAYGDYIFFFYRETAVEYMNCGKVIYSRVARVCKDDKGGPHQSRDRWTSFLKARLNCSIPGEYPFYFDEIQSTSDIVEGRYNSDDSKKIIYGILTTPVNAIGGSAICAYQMADILRVFEGSFKHQETINSNWLPVPQNLVPEPRPGQCVRDSRILPDKNVNFIKTHSLMEDVPALFGKPVLVRVSLQYRFTAITVDPQVKTINNQYLDVLYIGTDDGKVLKAVNIPKRHAKALLYRKYRTSVHPHGAPVKQLKIAPGYGKVVVVGKDEIRLANLNHCASKTRCKDCVELQDPHCAWDAKQNLCVSIDTVTSYRFLIQDVVRGDDNKCWSPQTDKKTVIKNKPSEVENEITNSIDEKDLDSSDPLIKTGLDDDSDCDPVSENSIGGCAVRQQLVIYTAGTLHIVVVVVSIVGLFSWLYSGLSVFAKFHSDSQYPEAPFIEQHNHLERLSANQTGYLTPRANKAVNLVVKVSSSTPRPKKDNLDVSKDLNIASDGTLQKIKKTYI | 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
|
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' . Involved in nuclear export of specific sets of mRNAs . Links the mRNA adapter mlo3 to rae1 for targeting mRNA-protein complex to the proteins of the nucleoporin complex (NPC) . Involved in recombinational repair of DNA. Plays a critical role in linking repair and checkpoint factors to damaged DNA sites by specifically recruiting rad24 and cdc25 to the DSBs .
Sequence Mass (Da): 8111
Sequence Length: 71
Domain: Two unstructured ubiquitin-binding sites (UBSs) mediate interaction with ubiquitin. UBS-I is the strong and UBS-II the weak binding site.
Subcellular Location: Cytoplasm
|
Q14563 | MGWLTRIVCLFWGVLLTARANYQNGKNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFDLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLKAYNQTHLYACGTGAFHPICTYIEIGHHPEDNIFKLENSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPKFISAHLISESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNFKDPKNPVVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPMNNRPIVIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSIPKETWYDLEEVLLEEMTVFREPTAISAMELSTKQQQLYIGSTAGVAQLPLHRCDIYGKACAECCLARDPYCAWDGSACSRYFPTAKRRTRRQDIRNGDPLTHCSDLHHDNHHGHSPEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEERKEEIRVDDHIIRTDQGLLLRSLQQKDSGNYLCHAVEHGFIQTLLKVTLEVIDTEHLEELLHKDDDGDGSKTKEMSNSMTPSQKVWYRDFMQLINHPNLNTMDEFCEQVWKRDRKQRRQRPGHTPGNSNKWKHLQENKKGRNRRTHEFERAPRSV | 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): 88889
Sequence Length: 771
Domain: Strong binding to neuropilin is mediated by the carboxy third of the protein.
Subcellular Location: Secreted
|
O08665 | MGWFTGIACLFWGVLLTARANYANGKNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEILLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRCDIYGKACAECCLARDPYCAWDGSSCSRYFPTAKRRTRRQDIRNGDPLTHCSDLQHHDNHHGPSLEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEDRKEEIRMGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQTLLKVTLEVIDTEHLEELLHKDDDGDGSKIKEMSSSMTPSQKVWYRDFMQLINHPNLNTMDEFCEQVWKRDRKQRRQRPGHSQGSSNKWKHMQESKKGRNRRTHEFERAPRSV | 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: Strong binding to neuropilin is mediated by the carboxy third of the protein.
Subcellular Location: Secreted
|
P80146 | MKRGGLWLLLGLLVLSACSSNPPAASTQEAPLLGLEAPEAIPGRYIVVYKENADVLPALEALKAALEPGLMQPQGLQAQALRTLGLEGARVDKVYTAALRGVAVEVPDQELARLRQDPRVAYIEADQEVRAFAVQSPATWGLDRIDQRTLPLDGRYTYTATGAGVHAYVVDTGILLSHQEFTGRIGKGYDAITPGGSAQDCNGHGTHVAGTIGGTTYGVAKGVTLHPVRVLDCNGSGSNSSVIAGLDWVTQNHVKPAVINMSLGGGASTALDTAVMNAINAGVTVVVAAGNDNRDACFYSPARVTAAITVGATTSTDYRASFSNYGRCLDLFAPGQSITSAWYTSSTATNTISGTSMATPHVTGAAALYLQWYPTATPSQVASALLYYATPNVVKNAGRYSPNLLLYTPF | 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.-
|
O30126 | MKFDPQKYRELAEKDFEAAWKAGKEILAERSPNELYPRVGFSFGKEHPLFATIQRLREAYLSIGFSEVVNPLIVEDVHVKKQFGREALAVLDRCFYLATLPKPNVGISAEKIRQIEAITKREVDSKPLQEIFHRYKKGEIDGDDLSYLIAEVLDVDDITAVKILDEVFPEFKELKPISSTLTLRSHMTTGWFITLSHIADKLPLPIKLFSIDRCFRREQGEDATRLYTYFSASCVLVDEELSVDDGKAVAEALLRQFGFENFRFRKDEKRSKYYIPDTQTEVFAFHPKLVGSSTKYSDGWIEIATFGIYSPTALAEYDIPYPVMNLGLGVERLAMILYGYDDVRKMVYPQIHGEIKLSDLDIAREIKVKEVPQTAVGLKIAQSIVETAEKHASEPSPCSFLAFEGEMMGRNVRVYVVEEEENTKLCGPAYANEVVVYKGDIYGIPKTKKWRSFFEEGVPTGIRYIDGFAYYAARKVEEAAMREQEEVKVKARIVENLSDINLYIHENVRRYILWKKGKIDVRGPLFVTVKAEIE | 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
|
A7I4Y4 | MRFNPQDWKEKSHTNFEGAWHDGPSVITPPGEDKKYPRLRYTRAQPHPIFATINRLREIYLSMGFDECENPVIVEESDIYRQFGPEAMAVLDRVFYIGGLPRPNVGISRKQLDEINDILQSHRSPLVHGHEIPAGDSGNKEPFRPMSRETEEQLRETLHAYKKSEIDGDELTHELAKVLGVDDGIVVHILDSVFPEFRSLVPESSRSTLRSHMTSGWFMTLGSLWERTPLPIKLFSVDRCFRREQAEGPTRLMTYHSASCVVAREDVTIEDGKAVSEALLSAFGYEDFRFQPDDKRSKYYMPDSQTEVYAKHPVHGWVEVATFGMYSPSALGEYGIGVPVMNLGLGVERLAMIAYNANDVRQLSYPQFFPRLAGDREIACAVHLREEPVTVEGKALALAIARVAAAHATEQGPCSFTVWEGTLYGRNVNVIIEETEANAKLCGPACANEIFVHEGNILGVPDNEKWKDVRIKGIPTGISYLSAVSALAAANIEHAARCGTGTQVQVKMAKHPGDINLKIEEYAMRTITDTKKKVDVRGPVFLAVRSEIAE | 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
|
Q59054 | MRFDIKKVLELAEKDFETAWRETRALIKDKHIDNKYPRLKPVYGKPHPVMETIERLRQAYLRMGFEEMINPVIVDEMEIYKQFGPEAMAVLDRCFYLAGLPRPDVGLGNEKVEIIKNLGIDIDEEKKERLREVLHLYKKGAIDGDDLVFEIAKALNVSNEMGLKVLETAFPEFKDLKPESTTLTLRSHMTSGWFITLSSLIKKRKLPLKLFSIDRCFRREQREDRSHLMSYHSASCVVVGEDVSVDDGKVVAEGLLAQFGFTKFKFKPDEKKSKYYTPETQTEVYAYHPKLGEWIEVATFGVYSPIALAKYNIDVPVMNLGLGVERLAMIIYGYEDVRAMVYPQFYEYRLSDRDIAGMIRVDKVPILDEFYNFANELIDICIANKDKESPCSVEVKREFNFNGERRVIKVEIFENEPNKKLLGPSVLNEVYVYDGNIYGIPPTFEGVKEQYIPILKKAKEEGVSTNIRYIDGIIYKLVAKIEEALVSNVDEFKFRVPIVRSLSDINLKIDELALKQIMGENKVIDVRGPVFLNAKVEIK | 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 | MPFDRDKLEELRSLAQRDFDRAWKEGAKLVREPGLRDRYPRLKVETGEPHPLFETIQQLREAYLRAGFREVVNPVIIPEEEVYKQFGPEAAAVLDRCFYLAGLPRPDVGLGADKVEKLAEVLGREPSEDEVERLRETLHAYKKGEIDGDELTHEIAEALDTDDGTAVRILDEVFPELKRLKPEPLEPPLTLRSHMTAGWFITLSEILKREDPPLKLFSIDRCFRREQREDESHLMTYHSASCVVVSDDVTVDTGKAVAEAILRQFGFEDFEFVPDEKMSKYYVPGTQTEVYAYHPDLEDSIEDEELGPGWVEIATFGLYSPVALAEYGIDYPVMNLGIGVERLCMVLHGIDDVRSLAYVEYEPWEPSDLELARMIDYERKPATSFGERLVREVVRGLHEHADEEGPVEVELFRGEFGDREVVVHAVEEEKGEPLAGPAAFNRVYVLDGNLYAVPPEGDFGREIREEGVYSGVSFEEGLAARLAYEVEELLATGGGETTVSVRKVSRPSQVNLSLPRKLLRYVTKKGGEIEIKGPVFVTLRAEVR | 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
|
Q6LZE1 | MFKREEIIEMANKDFEKAWIETKDLIKAKKINESYPRIKPVFGKTHPVNDTIENLRQAYLRMGFEEYINPVIVDERDIYKQFGPEAMAVLDRCFYLAGLPRPDVGLSDEKISQIEKLGIKVSEHKESLQKILHGYKKGTLDGDDLVLEISNALEISSEMGLKILEDVFPEFKDLTAVSSKLTLRSHMTSGWFLTVSDLMNKKPLPFKLFSIDRCFRREQKEDKSHLMTYHSASCAIAGEGVDINDGKAIAEGLLSQFGFTNFKFIPDEKKSKYYTPETQTEVYAYHPKLKEWLEVATFGVYSPVALSKYGIDVPVMNLGLGVERLAMISGNFADVREMVYPQFYEHKLNDRNVASMVKLDKVPVMDEIYDLTKELIESCVKNKDLKSPCELAIEKTFSFGKTKKNVKINIFEKEEGKNLLGPSILNEIYVYDGNVIGIPESFDGVKEEFKDFLEKGKSEGVATGIRYIDALCFKITSKLEEAFVSNTTEFKVKVPIVRSLSDINLKIDDIALKQIMSKNKVIDVRGPVFLNVEVKIE | 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 | MDMDALTTLPIKKHTALLNRFPETRFVTQLAKKRASWIVFGHYLTPAQFEDMDFFTNRFNAILDMWKVGRYEVALMDGELTSEHETILKALELDYARIQDVPDLTKPGLIVLDMDSTAIQIECIDEIAKLAGVGEEVAEVTERAMQGELDFEQSLRLRVSKLKDAPEQILSQVRETLPLMPELPELVATLHAFGWKVAIASGGFTYFSDYLKEQLSLDYAQSNTLEIVSGKLTGQVLGEVVSAQTKADILLTLAQQYDVEIHNTVAVGDGANDLVMMAAAGLGVAYHAKPKVEAKAQTAVRFAGLGGVVCILSAALVAQQKLSWKSKP | 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 | MGSVLGLCSVASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPGMEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAAVHNGFWFFKFATAVAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNESWVEKMEEGNSRCWYAALLSATALNYLLSLVAIILFFVYYTHPASCSENKAFISVNMLLCIGASVMSILPKIQESQPRSGLLQSSVITIYTMYLTWSAMTNEPETNCNPSLLSIIGFNTTRPVPKDGQSVQWWHPQGIIGLVLFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGNGRSDGSLDDGEGVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQWTAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD | 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 | MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVVPTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEGVQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS | 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 Length: 473
Subcellular Location: Cell membrane
|
A6NH21 | MVGAKAGPSPGTSLGLAQQHSGGSSVLVKSPFCQVCCCGPAPCASCCHSRWPSLTASTCSRLFYILLHVGASAICCLLLSRTVVERVWGKTHRIQMPSGLCAHLFGLSDCPVLSGSGAVYRVCAGTATFHLLQAVLLVHLHSPTSPRAQLHNSFWLLKLLFLLGLCAIAFCIPDEHLFPAWHYIGICGGFAFILLQLVLITAFAHSWNKNWQTGAAQDCSWFLAVLLATLGFYSMAGVGAVLLFHYYTHPAGCLLNKMLLSLHLCFCGLISFLSIAPCIRLKQPRSGLLQASVISCYIMYLTFSALSSRPPERVILQGQNHTLCLPGLSKMEPQTPDISLAMLSASIMYACVLFACNEASYLAEVFGPLWIVKVYSYEFQKPSLCFCCPETVEADKGQRGGAARPADQETPPAPPVQVQHLSYNYSAFHFVFFLASLYVMVTLTNWFSYEGAELEKTFIKGSWATFWVKVASCWACVLLYLGLLLAPLCWPPTQKPQPLILRRRRHRIISPDNKYPPV | 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
|
A8WCG0 | MGAKDITGRSTTQGFAQQHGGVSDVVVKTPFYQVSCCGPVSWTSGCHSLTESTCSRLFYILLHMGASAICCLLLSKTVVERVWGKAHGIQMPSVLCAHLFGNSDCPVLSGSGAVYRVCAGTATFHLLQAVLLVRLHSPTSPRAQLHNSFWSLKLLFLLGLCTAAFCIPDEHLFPAWHYIGICGGFTFILLQLVLITAFAQSWNKNWQTGAAQDCSWFLGVLLATLGFYSMAGVGAVLLFHHYTHPDGCLLNKMLLSLHLCFCGLLSLLSIAPCIRLRQPNSGLLQASIISCYIMYLTFSALSSRPPETIIFQGQNHTLCLPGQNKMEPQIPDASVAVFSASIMYACVLFACNEASYLAQLFGPLWIIKVYKYEFQKPSVCFCCPQTVEPEDGQGSRARPADQETPPAAQVQSQHLSYSYSGFHFAFFLASLYVMVTLTNWFSYEEAELEKTFTKGSWATFWVKVASCWACVLLYLGLLLAPLLAHHSESPPP | 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
|
Q86VE9 | MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLCLLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFHLLP | 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 providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47009
Sequence Length: 423
Subcellular Location: Cell membrane
|
P52878 | MKPTRVPNNPCFSSGPCAKHPGYSIEELKDTPFGRSHRSNLGKEKLAEAIKKTRDMLGLPDDYLVGIVPASDTGAFEMCLWSMLGCRGVDVLVWESFSKGWATDITKQLKLKDVRVFEAEYGKLPDLKKVDFKNDVVFVWNGTTSGVKVPNGDWIPENREGLTLCDATSAIFAMDIPYHKLDVITFSWQKVLGGEGAHGMLILSPRAVQRLESYTPAWPLPKIFRLTKGGKLNKKIFEGSTINTPSMLANEDWLATLKWAESVGGLKPLIQRTNDNLAVFEAFVAKNNWIHFLAETKEIRSSTSVCFKVDLSDEKLKELIKTLEKEKVAYDIGSYRDAPSGLRIWCGATVEKEDLQCLCEWIEWAYNLVK | 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 Mass (Da): 41544
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
Q99K85 | MEATKQVVNFGPGPAKLPHSVLLEIQKQLLDYRGLGISVLEMSHRSSDFAKIIGNTENLVRELLAVPNNYKVIFVQGGGSGQFSAVPLNLIGLKAGRSADYVVTGAWSAKAAEEAKKFGTVNIVHPKLGSYTKIPDPSTWNLNPDASYVYFCANETVHGVEFDFVPDVKGAVLVCDMSSNFLSRPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFSLRECPSVLDYKVQAGNNSLYNTPPCFSIYVMGMVLEWIKNNGGAAAMEKLSSIKSQMIYEIIDNSQGFYVCPVERQNRSRMNIPFRIGNAKGDEALEKRFLDKAVELNMISLKGHRSVGGIRASLYNAVTTEDVEKLAAFMKNFLEMHQL | 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 Mass (Da): 40473
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
EC: 2.6.1.52
|
O33062 | MADQLTPSLDIPAALKPRDGRFGSGPSKVRPEQLQALTNTAATLFGTSHRQAPVKNLVGRVRAGLAELFSLPDGYQVILGNGGATAFWDAAAFGLIDKRSLHLTYGEFSSKFASAVAKNPFIDEPIVIKSDPGSAPKPTGDPSVDVIAWAHNETSTGVAVPVRRPTGSGGALIAIDATSGAGGLPVDIAQTDAYYFAPQKNFASDGGLWLAIMSPAALARVDSITASGRWVPDFLSLPIAVENSLKNQTYNTPAICTLALLAEQLDWLLGNGGLEWAVKRTADSSQRLYAWAEDRPYTTPFVVDPALRSQVVGTIDFTDDVDAAAVAKILRANGIIDTEPYRKLGRNQLRVAMFPAVEPDDVRALTECVDWIVERL | 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 Mass (Da): 40113
Sequence Length: 376
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
Q742L2 | MSMADQLQIPADIKPRDGRFGCGPSKVRPEQLQALSTTAAPLFGTSHRQAPVKNLVGRLRSGLAELFSLPDGYQVILGNGGATAFWDAAAFGLIDKRSLHLSYGEFSSKFAAAVAKNPFVGDPVVIKSDAGSAPEPQSDPSVDLIAWAHNETSTGVAVPVRRPVDSGDALVAIDATSGAGGLPVDIGETDAYYFSPQKNFAGDGGLWLALMSPAALARVESIAASGRWVPDFLSLPIAVENSLKDQTYNTPAIGTLALMAEQVDWMLGNGGLDWAVKRTADSAGRLYSWAEERDYTTPFVADPKLRSQVVGTIDFVDDVDAAAVAKILRANGVVDTEPYRKLGRNQLRVGMFPAVDPDDVSALTQCVDWVVERL | 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 Mass (Da): 39789
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
A3Q635 | MAELTIPADLKPRDGRFGSGPSKVRPEQLQALAAAGDLFGTSHRQAPVKNLVGRVRDGIKQLFSVPEGYDVILGNGGSTAFWDAAAFGLIDKRSLHLTYGEFSAKFASAVAKNPFVGDPIVVKADPGSAPEPQSDPSVDVIAWAHNETSTGVAVPVQRPADSGDALIVIDATSGAGGLPVDIAQADAYYFAPQKNFAGDGGLWLAVVSPAALARIEAIGQSGRWVPDFLSLPIAVENSLKNQTYNTPAIGTLVLLADQLDWLNGNGGLDWAVKRTADSSQRLYSWAEASSYATPFVTDPALRSQVVGTIDFADDVDAAAVAKVLRANGIVDTEPYRKLGRNQLRVAMFAAVDPEDVSALTRCVDWVVERL | 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 Mass (Da): 39170
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
Q1D2L9 | MRVINFNAGPAGLPLPALERARDELIDFQGSGMSVMEHSHRGREYEGVHDEAISLLTRLLGIPDTHQVLFLTGGASQQFAQVPMNFLRPGASADYLMTGVWSEKAFDEAKYYGTPRVAVSTARPDKRYTRVPRQDELRLESSAAYVHLTSNNTIFGTQWHTFPDVGNVPLVADMSSDFLWKGFDVSRFGLIYAGAQKNLGPSGVTLVVADKAFIARGRTDIPKIFRYTTHAENNSLYNTPPTLAIYLVRNVLAWIQSVGGLAQLEQWNREKAALLYGAVDRHPEFYRAPVERESRSVMNVVFQLPTEALDASFVADAKQQGMVGLKGHRTAGGIRVSMYNAVSVENVRTLAAFMDHFVKTRG | 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 Mass (Da): 40154
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
O34370 | MSLYPIYNFSAGPAVLPEAVLETARQEMLDYNGTGFPVMAMSHRSEMFLSILHHAEQDLRQLLKVPDNYKILFLQGGATTQFNMAAMNLAHGFRTADAVVTGNWSRIAYEQMSRLTDTEIRLAAHGGEQFDYLDLPPVETWDVAPDSAFVHFAVNETVNGLQYREVPRLSEGMPPLVCDMSSEILSREFDVADYGLIYAGAQKNIGPAGVTVVIVREDLLERCPNDIPDVFNYRSHINRDGMYNTPSTYAIYMSGLVFRWLQAQGGVKKIEAVNRLKAQTLYETIDGSGGFYINRIRPNARSKMNVVFQTGDEELDRRFVLEAELQGLCLLKGYKTVGGMRASIYNAMPLEGVRALADFMRDFQRRYG | 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 Mass (Da): 41388
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
Q59196 | MSKRAYNFNAGPAALPLEVLERAQAEFVDYQHTGMSIMEMSHRGAVYEAVHNEAQARLLALLGNPTGYKVLFIQGGASTQFAMIPMNFLKEGQTANYVMTGSWASKALKEAKLIGDTHVAASSEASNYMTLPKLQEIQLQDNAAYLHLTSNETIEGAQFKAFPDTGSVPLIGDMSSDILSRPFDLNQFGLVYAGAQKNLGPSGVTVVIVREDLVAESPKHLPTMLRYDTYVKNNSLYNTPPSFGIYMVNEVLKWIEERGGLEGVQQANRKKASLIYDAIDQSGGFYRGCVDVDSRSDMNITFRLASEELEKEFVKASEQEGFVGLKGHRSVGGLRASIYNAVPYESCEALVQFMEHFKRSRG | 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 Mass (Da): 39924
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.52
|
P58004 | MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT | 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 signaling pathway . This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via TORC1 . May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1 . May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress . Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein . Was originally reported to contribute to oxidative stress resistance by reducing PRDX1 . However, this could not be confirmed .
PTM: Phosphorylated by ULK1 at multiple sites.
Catalytic Activity: a hydroperoxide + L-cysteinyl-[protein] = an alcohol + S-hydroxy-L-cysteinyl-[protein]
Sequence Mass (Da): 54494
Sequence Length: 480
Domain: The N-terminal domain has an alkylhydroperoxide reductase activity.
Subcellular Location: Cytoplasm
EC: 1.11.1.-
|
P58005 | MNRGGGSPSAAANYLLCTNCRKVLRKDKRIRVSQPLTRGPSAFIPEKEVVQANTVDERTNFLVEEYSTSGRLDNITQVMSLHTQYLESFLRSQFYMLRMDGPLPLPYRHYIAIMAAARHQCSYLINMHVDEFLKTGGIAEWLNGLEYVPQRLKNLNEINKLLAHRPWLITKEHIQKLVKTGENNWSLPELVHAVVLLAHYHALASFVFGSGINPERDPEISNGFRLISVNNFCVCDLANDNNIENASLSGSNFGIVDSLSELEALMERMKRLQEEREDEEASQEEMSTRFEKEKKESLFVVSGDTFHSFPHSDFEDDMIITSDVSRYIEDPGFGYEDFARRGEEHLPTFRAQDYTWENHGFSLVNRLYSDIGHLLDEKFRMVYNLTYNTMATHEDVDTTMLRRALFNYVHCMFGIRYDDYDYGEVNQLLERSLKVYIKTVTCYPERTTKRMYDSYWRQFKHSEKVHVNLLLMEARMQAELLYALRAITRHLT | 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 similarity). May prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity).
Catalytic Activity: a hydroperoxide + L-cysteinyl-[protein] = an alcohol + S-hydroxy-L-cysteinyl-[protein]
Sequence Mass (Da): 57291
Sequence Length: 492
Domain: The N-terminal domain may have an alkylhydroperoxide reductase activity.
Subcellular Location: Cytoplasm
EC: 1.11.1.-
|
Q9CYP7 | MNRGGSSASASANYLLCTNCRKVLRKDKRIRVSQPLTRGPSAFIPEKEVVQANTADERTNFLVEEYSTSGRLDNITQVMSLHTQYLESFLRSQFYMLRMDGPLPLPDRHYIAIMAAARHQCSYLINMHVDEFLKTGGIAEWLNGLEYVPQRLRNLNEINKLLAHRPWLITKEHIQKLVKTGENNWSLPELVHAVVLLAHYHALASFVFGSGINPERDPGIANGFRLISVSSFCVCDLANDNSIENTSLAGSNFGIVDSLGELEALMERMKRLQEDREDDETTREEMTTRFEKEKKESLFVVPGETLHAFPHSDFEDDVIVTADVSRYIEDPSFGYEDFARRGEEHLPTFRAQDYTWENHGFSLVNRLYSDIGHLLDEKFRMVYNLTYNTMATHEDVDTTTLRRALFNYVHCMFGIRYDDYDYGEVNQLLERSLKVYIKTVTCYPERTTKRMYDSYWRQFTHSEKVHVNLLLMEARMQAELLYALRAITRHLT | 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). May prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity).
Catalytic Activity: a hydroperoxide + L-cysteinyl-[protein] = an alcohol + S-hydroxy-L-cysteinyl-[protein]
Sequence Mass (Da): 57021
Sequence Length: 492
Domain: The N-terminal domain may have an alkylhydroperoxide reductase activity.
Subcellular Location: Cytoplasm
EC: 1.11.1.-
|
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 for binding to OCRL and INPP5B.
Subcellular Location: Early endosome
|
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 for binding to OCRL and INPP5B.
Subcellular Location: Early endosome
|
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 for binding to OCRL and INPP5B.
Subcellular Location: Early endosome
|
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 for binding to OCRL and INPP5B.
Subcellular Location: Early endosome
|
O74738 | MEKLLHEALQNGCKLHKSVEFIQSRDDNACFGSYIAVAQNDIAPDQLLISCPFEYAITYNKAKEELKKLNPNFESCNPHITLCTFLALESLKGIQSKWYGYIEYLPKTFNTPLYFNENDNAFLISTNAYSAAQERLHIWKHEYQEALSLHPSPTERFTFDLYIWSATVFSSRCFSSNLIYKDSESTPILLPLIDSLNHKPKQPILWNSDFQDEKSVQLISQELVAKGNQLFNNYGPKGNEELLMGYGFCLPDNPFDTVTLKVAIHPDLPHKDQKAAILENDCQFQLSNLVFFLPKSPDKEIFQKILQCLAVVTASSLELRKLTAHLLTGDLASYVPSLRGQIKSLEVLLMYIDSRADLLLKSNPQVSPTSERQVWAKIYRDSQINILQDSITYVKNYMEESLQKTYKPLPNLLQYLILNSISIFLLQHPLFAPLSHAIESLYGSTDAEALVATDEQDILMILICVYCLSISEKLPFSISMLVEGYPAVANPEGVEVFEILDEMFFQQFTNVFGESKHFNKENVSWALQLVNDESLDFSGFTFIIAHN | 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 | MSNKQNIESEVSWVKSKGAFVHPSLEFSVIPDAGSCVLANNDINENTVLLKLPPNILINKRTCSRYSFRDKLTSFQFLSWLISEDVHSNLEISPYYTKALPQGFSFHPVTLTSDHPLWSILPDEVRNSLLERKNVMAFDYEQVKKFVSVDQPTFQWGWLCVNTRCLYYDTGSKNTEDHLTLAPIFEYFNHSPEAQTALINTRGTITIKSTRRIDKGEQIFLCYGPHGNDKLFTEYGFCLSNNPNISIQLDRFIEFDKWQQSFLQDHGYWNDYTCSLHGASFRTLVGVRTLLVSPSEKLNDASYDQTRRVLQYINGFSDGSRDRQDVEDYLKKVLQELLCEAEECKEKVKGISDGSYVFICAEQLWKDRIMCCQYLMEHSFE | 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 Length: 381
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
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 . Together with spr-5, required for transgenerational fertility .
Catalytic Activity: N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32028
Sequence Length: 277
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q99287 | MADRPAIQLIDEEKEFHQSALQYFQQCIGNRDVGLDYHVISVFGSQSSGKSTLLNVLFNTNFDTMDAQVKRQQTTKGIWLAHTKQVNTTIEIDNDRPDIFVLDVEGSDGSERGEDQDFERKAALFAIAVSEVLIVNMWEQQIGLYQGNNMALLKTVFEVNLSLFGKNDNDHKVLLLFVIRDHVGVTPLSSLSDSVTRELEKIWTELSKPAGCEGSSLYDYFDLKFVGLAHKLLQEDKFTQDVKKLGDSFVMKGTENYYFKPQYHHRLPLDGWTMYAENCWDQIERNKDLDLPTQQILVARFKTEEISNEALEEFISKYDESIAPLKGNLGSLTSQLVKLKEECLTKYDEQASRYARNVYMEKREALNTKLNSHISGTINEFLESLMEKLWDDLKLEVSSRDKATTSFVESVAAGKSKIEKEFNESMETFKKLGLLISNEEITCKFSDDIEERIKQLRDAELKAKIGRIKKNLVPELKDHVIHLLSHPSKKVWDDIMNDFESTIKDNISAYQVEKDKYDFKIGLSESENAKIYKNIRILAWRTLDTTVHDYLKIDTIVSILRDRFEDVFRYDAEGSPRLWKTEEEIDGAFRVAKEHALEVFEVLSLAVTSDNVEIIPDVPMAEEESGEDNEIYRDNEGVFHSRRFAHILTELQKENVLDQFRRQINITVLDSKRSIITTRTHIPPWIYVLLAVLGWNEFVAVIRNPLFVTLTLILGATFFVIHKFGLWGPVVNVVQSAVGETRTAIKDKLRQFVVEDHEVKESFEMKDFSKNEQKEK | 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
Sequence Mass (Da): 89432
Sequence Length: 776
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.6.5.-
|
Q7TSK2 | MRPAALLLLPSLLALLAHGLSSEAPITGEGHATGIRETDGELTAAPTPEQSDRGVHFVTTAPTLKLLNHHPLLEEFLQEGLEREEAPQPALPFQPDSPTHFTPSPLPRLTNQDNRPVFTSPTPAVAAAPTQPHSREKPWNLESKPPELSITSSLPPGPSMAVPTLLPEDRPSTTPPSQAWTPTQEGPGDMDRPWVPEVMSKTTGLGVEGTIATSTASGDDEETTTTIITTTVTTVQPPGPCSWNFSGPEGSLDSPTAPSSPSDVGLDCFYYISVYPGYGVEIKVENISLQEGETITVEGLGGPDPLPLANQSFLLRGQVIRSPTHQAALRFQSLPLPAGPGTFHFRYQAYLLSCHFPRRPAYGDVTVTSLHPGGSAHFHCATGYQLKGARFLTCLNATQPFWDSQEPVCIAACGGVIRNATTGRIVSPGFPGNYSNNLTCHWLLEAPESQRLHLHFEKVSLAEDDDRLIIRNGNNVEAPPVYDSYEVEYLPIEGLLSSGRHFFVEFSTDSSGAAAGMALRYEAFQQGHCYEPFVKYGNFSSSAPSYPVGTTVEFSCDPGYTLEQGSIIIECVDLHDPQWNETEPACRAVCSGEITDSAGVVLSPNWPEPYGRGQDCIWGVHVEEDKRIMLDIRVLRIGSGDVLTFYDGDDLTARVLGQYSGPRGHFKLFTSMADVTIQFQSDPGTSALGYQQGFVIHFFEVPRNDTCPELPEIPNGWKNPSQPELVHGTVVTYQCYPGYQVVGSSILMCQWDLSWSEDLPSCQRVTSCHDPGDVEHSRRLISSPKFPVGATVQYVCDQGFVLTGSAILTCHDRQAGSPKWSDRAPKCLLEQFKPCHGLSAPENGARSPEKRLHPAGATIHFSCAPGYVLKGQASIKCVPGHPSHWSDPPPICRAASLDGFYNGRSLDVAKAPAASSALDAAHLAAAIFLPLVAMVLLVGGVYLYFSRFQGKSPLQLPRTHPRPYNRITVESAFDNPTYETGSLSFAGDERI | 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 connectivity.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 107433
Sequence Length: 991
Subcellular Location: Cell membrane
|
Q6AX42 | MMPLAGIAWNLMLLFSAVQGLPLQDGEGTQHPDLLNNPPKGSVEPVALEQLVHQAILKKDFLAQDVFFPGTTAIPTRAAPISLTEGVSDASGVLTTAVGGAFSLPPQLSTLIPPSPAPTGGPGPSPEAEEETTTTLITTTTVTTVHSPVLCNNNISESEGLLEAPEYGGSTFFGGLDCTYSVSVYLGYGVEIRVERLNLSKEEALSIEGLEEDRRFLLANETLMAEGQVIRSPTNHVAVRFQTYRATSPGAFRLRYQAFVLSCVFPPRPENGEVTVTDLHPGGAANFRCSAGFTLKGGESLVCLNISRPEWSGKPPVCAASCGGVIRNATVGRIVSPDISTSHSNNHGNNLSCHWLIEAAEGQRLHLHFERVSLDEDNDRLVVRSGSSPLSPVIYDSDIDDVPERGLLSDAQSLYIELISDNPAVPLLLSLRYEVFSESRCYEPFLAHGNFTTTDPLYSPGSLVSFFCNAGYMLEQGPPVIECVDPADPHWNESEPVCKALCGGEISEPAGVILSPDWPQNYGKGQDCVWGIHVQEDRRVLLEIEILNIRRSDALTVYDGDDLTARVLGQYMGVHQRFNLFSSANDVTLQFQSDSNDPVFSLSQGFIIHFKEVPRNDTCPALPEVPNGWKTSSHPDLIRGTVVTYQCEPGYDISGSDILTCQWDLSWSNAPPTCEKILNCADPGEIANGVRRASDPRFPIGSHVQYSCNEGYTLEGSRTLTCYNRDTGTPKWSDRIPKCVLKYEPCLNPGVPENGYQTLYKHHYQAGEALRFFCYEGFELIGEVTITCAPGHPSQWTSQPPLCKVAYEELLDDRKLEVTQTTDPSHQMEGGNIALAIFLPIILVILLIGGIYIYYTKFQGKSLFGFSFPASHSYSPITVESDFNNPLYEAGDTREYEVSI | 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
|
Q15637 | MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPANNPPPPSLMSTTQSRPPWMNSGPSESRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN | 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.
Sequence Mass (Da): 68330
Sequence Length: 639
Subcellular Location: Nucleus
|
Q64213 | MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHTLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPASNPPPPSLMSTTQSRPPWMNSGPSENRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGTPQMQGNPTMVPLPPGVQPPLPPGAPPPPPCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA | 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): 70403
Sequence Length: 653
Subcellular Location: Nucleus
|
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 PRKDC. PRKDC inhibits, whereas PKA activates the splicing factor.
Sequence Mass (Da): 25023
Sequence Length: 228
Domain: The tiny Arg-Ser repeat region (RS repeat) is necessary for the splicing enhancer function.
Subcellular Location: Host nucleus
|
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 PRKDC. PRKDC inhibits, whereas PKA activates the splicing factor (By similarity).
Sequence Mass (Da): 25164
Sequence Length: 229
Domain: The tiny Arg-Ser repeat region (RS repeat) is necessary for the splicing enhancer function.
Subcellular Location: Host nucleus
|
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 by human PKA and PRKDC. PRKDC inhibits, whereas PKA activates the splicing factor (By similarity).
Sequence Mass (Da): 24741
Sequence Length: 217
Domain: The tiny Arg-Ser repeat region (RS repeat) is necessary for the splicing enhancer function.
Subcellular Location: Host nucleus
|
Q15459 | MPAGPVQAVPPPPPVPTEPKQPTEEEASSKEDSAPSKPVVGIIYPPPEVRNIVDKTASFVARNGPEFEARIRQNEINNPKFNFLNPNDPYHAYYRHKVSEFKEGKAQEPSAAIPKVMQQQQQTTQQQLPQKVQAQVIQETIVPKEPPPEFEFIADPPSISAFDLDVVKLTAQFVARNGRQFLTQLMQKEQRNYQFDFLRPQHSLFNYFTKLVEQYTKILIPPKGLFSKLKKEAENPREVLDQVCYRVEWAKFQERERKKEEEEKEKERVAYAQIDWHDFVVVETVDFQPNEQGNFPPPTTPEELGARILIQERYEKFGESEEVEMEVESDEEDDKQEKAEEPPSQLDQDTQVQDMDEGSDDEEEGQKVPPPPETPMPPPLPPTPDQVIVRKDYDPKASKPLPPAPAPDEYLVSPITGEKIPASKMQEHMRIGLLDPRWLEQRDRSIREKQSDDEVYAPGLDIESSLKQLAERRTDIFGVEETAIGKKIGEEEIQKPEEKVTWDGHSGSMARTQQAAQANITLQEQIEAIHKAKGLVPEDDTKEKIGPSKPNEIPQQPPPPSSATNIPSSAPPITSVPRPPTMPPPVRTTVVSAVPVMPRPPMASVVRLPPGSVIAPMPPIIHAPRINVVPMPPSAPPIMAPRPPPMIVPTAFVPAPPVAPVPAPAPMPPVHPPPPMEDEPTSKKLKTEDSLMPEEEFLRRNKGPVSIKVQVPNMQDKTEWKLNGQVLVFTLPLTDQVSVIKVKIHEATGMPAGKQKLQYEGIFIKDSNSLAYYNMANGAVIHLALKERGGRKK | 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 spliceosome 'B' complexes .
Sequence Mass (Da): 88886
Sequence Length: 793
Domain: SURP motif 2 mediates direct binding to SF3A3.
Subcellular Location: Nucleus
|
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
Subcellular Location: Cell membrane
|
Q8GMH4 | MTDQCVVSAPVRVRTRRLDVKETGALPAYRALAEHFGPDEVYLLESAAGPARDRRHQFVGFGALLSLSVTDRVVRVEGVPALRGLLLERAGALLEDGPQGLRLRTAGGLWPLLRAMRDMFDAEGSASGFRFGFLGFFGYDTARYIEDLPHLIENRPGLPDVRMVLHRGSVVTDLATGRCELLLHESPYWPGLAPETVTGLLADVEQAWPDPSADGFPASAVTDDSAPEVFANDVERCLKHIAVGDIYQVQIGHELSIRSTADPADVYQRLRGRNASPYMYLAGIDGHRLIGASPELFVRIEDGEVTMRPIAGTVPRSGADGGIAAGVRLRSDPKEIAEHTMLVDLCRNDIGRIARPNTLDVPDQLDVEGYSHVLHLVSTVVGRARVDTDAFDTIAALFPAGTMTGAPKIRAMEIIESVERSRRGLYAGALGLLDVGGYTNLALCIRTLFHHEGVYRTRASAGIVADSEPGAEWTETLAKMSATHWAVTGEELL | 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: 2.6.1.86
|
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 + NAD(+) = FAD + 2 H(+) + NADH
Sequence Mass (Da): 19486
Sequence Length: 182
Pathway: Antibiotic biosynthesis.
EC: 1.5.1.37
|
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.-
|
O43556 | MQLPRWWELGDPCAWTGQGRGTRRMSPATTGTFLLTVYSIFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEISNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEDFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDLKEGVYVMVGADVPFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVIRGEGILPDGGEYKPPSDSLKSRDYYTDFLITLAVPSAVALVLFLILAYIMCCRREGVEKRNMQTPDIQLVHHSAIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEIIPPLHTDNYDSTNMPLMQTQQNLPHQTQIPQQQTTGKWYP | 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: Cell membrane
|
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
Subcellular Location: Cell membrane
|
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
Subcellular Location: Cell membrane
|
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)anthranilate + FMNH2
Sequence Mass (Da): 24133
Sequence Length: 223
EC: 1.3.8.16
|
Q7CXU0 | MTDMPNRKPPLSGIRVIELARVLAGPWAGQMLADMGADVIKVENPEGGDDTRAWGPPFVESADGENLSAAYYHATNRGKRSIVADLKTPEGCALVRRLVRTADVVIENFKRDGLAKYGLDYESLRVLNPKLIYCSITGFGQTGPYADFAGYDYIVQGMSGFMSITGEPDGQPMKAGVAVADIFTGIYSVSAIQAALIHAMRSGEGQHIDMALLDVQSAVLANQNMNYLISGRPPIRLGNAHPNISPYEVVPTADGFLILAVGNDGQFRRLCNILGIGAIADDERYATNKARVAHKVEVRQIISTETLKWNKRDLLTACETNAVPAGPINSIEEMFADPQVQARGLRVDLEAEDGTVIPGVRTPIIMSQTPLRYERPSPKLGEHQAQVLAELETIERTATP | 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: Amino-acid degradation.
EC: 2.8.3.-
|
Q9NP31 | MEFPLAQICPQGSHEAPIPTFSTFQITDMTRRSCQNLGYTAASPQAPEAASNTGNAERAEEVPGEGSLFLQAETRAWFQKTQAHWLLQHGAAPAWFHGFITRREAERLLEPKPQGCYLVRFSESAVTFVLTYRSRTCCRHFLLAQLRDGRHVVLGEDSAHARLQDLLLHYTAHPLSPYGETLTEPLARQTPEPAGLSLRTEESNFGSKSQDPNPQYSPIIKQGQAPVPMQKEGAGEKEPSQLLRPKPPIPAKPQLPPEVYTIPVPRHRPAPRPKPSNPIYNEPDEPIAFYAMGRGSPGEAPSNIYVEVEDEGLPATLGHPVLRKSWSRPVPGGQNTGGSQLHSENSVIGQGPPLPHQPPPAWRHTLPHNLSRQVLQDRGQAWLPLGPPQ | 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 of KDR with effector proteins important to endothelial cell survival and proliferation.
PTM: Phosphorylated on tyrosine residues.
Sequence Mass (Da): 42934
Sequence Length: 389
Subcellular Location: Cytoplasm
|
Q9NRF2 | MNGAPSPEDGASPSSPPLPPPPPPSWREFCESHARAAALDFARRFRLYLASHPQYAGPGAEAAFSRRFAELFLQHFEAEVARASGSLSPPILAPLSPGAEISPHDLSLESCRVGGPLAVLGPSRSSEDLAGPLPSSVSSSSTTSSKPKLKKRFSLRSVGRSVRGSVRGILQWRGTVDPPSSAGPLETSSGPPVLGGNSNSNSSGGAGTVGRGLVSDGTSPGERWTHRFERLRLSRGGGALKDGAGMVQREELLSFMGAEEAAPDPAGVGRGGGVAGPPSGGGGQPQWQKCRLLLRSEGEGGGGSRLEFFVPPKASRPRLSIPCSSITDVRTTTALEMPDRENTFVVKVEGPSEYIMETVDAQHVKAWVSDIQECLSPGPCPATSPRPMTLPLAPGTSFLTRENTDSLELSCLNHSESLPSQDLLLGPSESNDRLSQGAYGGLSDRPSASISPSSASIAASHFDSMELLPPELPPRIPIEEGPPTGTVHPLSAPYPPLDTPETATGSFLFQGEPEGGEGDQPLSGYPWFHGMLSRLKAAQLVLTGGTGSHGVFLVRQSETRRGEYVLTFNFQGKAKHLRLSLNEEGQCRVQHLWFQSIFDMLEHFRVHPIPLESGGSSDVVLVSYVPSSQRQQEPTTSHDPPQPPEPPSWTDPPQPGAEEASRAPEVAAAAAAAAKERQEKEKAGGGGVPEELVPVVELVPVVELEEAIAPGSEAQGAGSGGDAGVPPMVQLQQSPLGGDGEEGGHPRAINNQYSFV | 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 factor (BDNF), glial cell line-derived neurotrophic factor (GDNF), platelet-derived growth factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone (GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1, which in turn is phosphorylated by JAK2 on tyrosine residues. These phosphotyrosines form potential binding sites for other signaling proteins. GH also promotes serine/threonine phosphorylation of SH2B1 and these phosphorylated residues may serve to recruit other proteins to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP) signaling, binds to and potentiates the activation of JAK2 by globally enhancing downstream pathways. In response to leptin, binds simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-kinase pathway. Acts as positive regulator of NGF-mediated activation of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase activity of the cytokine receptor-associated tyrosine kinase JAK2 and of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2, the mechanism seems to involve dimerization of both, SH2B1 and JAK2. Enhances RET phosphorylation and kinase activity. Isoforms seem to be differentially involved in IGF-I and PDGF-induced mitogenesis (By similarity).
PTM: Phosphorylated on tyrosine residues in response to receptor kinase stimulation. Phosphorylated by RET.
Sequence Mass (Da): 79366
Sequence Length: 756
Subcellular Location: Cytoplasm
|
O14492 | MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTRGGCLASRVASCSCELLTDAVDLPRPPETTAVGAVVTAPHSRGRDAVRESLIHVPLETFLQTLESPGGSGSDSNNTGEQGAETDPEAEPELELSDYPWFHGTLSRVKAAQLVLAGGPRNHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVLDMLRHFHTHPIPLESGGSADITLRSYVRAQDPPPEPGPTPPAAPASPACWSDSPGQHYFSSLAAAACPPASPSDAAGASSSSASSSSAASGPAPPRPVEGQLSARSRSNSAERLLEAVAATAAEEPPEAAPGRARAVENQYSFY | 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 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3.
PTM: Tyrosine phosphorylated by JAK2, KIT and other kinases activated by B-cell receptor in response to stimulation with cytokines, IL3, IL5, PDGF, IGF1, IGF2, CSF2/GM-CSF and cross-linking of the B-cell receptor complex.
Sequence Mass (Da): 67738
Sequence Length: 632
Subcellular Location: Cytoplasm
|
Q9JID9 | MNGATPSSAAAPAPVPDWRQFCELHAQVAAVDFAHKFCRFLRDNPTYDTPDAGTSFSRHFAANFLAVFSEEVRRVLGSAADTMEPEPAVTSVTSALKTATYGHSRSSEDVSAHAATKARVRKGFSLRNMSLCVVDGVRDLWHRRSSPEPDGGATPKAAEPASEPRDKWTRRLRLARTLAAKVELVDIQREGALRFMVADDAASGPGGTAQWQKCRLLLRRAVAGERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTGLSCARGGCLASRVASCSCELLTDADMPRPPETTTAVGAVVTAPHGRARDTVGESLAHVPLETFLQTLESSGGVSENNNPGDEGAELDTDAEAELELSDYPWFHGTLSRVKAAQLVLAGGPRSHGLFVIRQSETRPGECVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVFDMLRHFHTHPIPLESGGSADITLRSYVRAQGPPPDPGPAPNTAAPVPACWTEPAGQHYFSSLATATCPPASPSNGAGASSSSGSSSSATSLPPRPAEGPLSAHSRSNSTEHLLDAASGATEEPTEATLGRARAVENQYSFY | 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 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3 (By similarity).
PTM: Tyrosine phosphorylated by JAK2, KIT and other kinases activated by B-cell receptor in response to stimulation with cytokines, IL3, IL5, PDGF, IGF1, IGF2, CSF2/GM-CSF and cross-linking of the B-cell receptor complex.
Sequence Mass (Da): 66557
Sequence Length: 621
Subcellular Location: Cytoplasm
|
Q6FMH8 | MSLENAVRVVSTDEKGNQASSTKLIELLHSRVDALTTTNIELTTKLQELLGNLDTVQQRERKLKESAASLRHEGDNVTLMLNRKERKLTEVKEAIVELTTKLGEAKEVNHSLKQKFEDEGLTSEESLRESISEVKTEYDTLVKSHEIYESSNDIQCKSLEDRFSQALLIHGENMKALDGTAEQILANNSELVSQLRATENKAESARTSIRNASIDTAAKVDLEKWLFLYKEAQRICEEFASKTDTKLPDELQAIIDDPVLKELDARFALDEIQYGKTRNKRIPSNPLLSNSQAAARRVASPSANYSPRVSSAQGSLPGITRTPSMKVNNKFSDSNAQEVPTRLHSHGSRSKRSSMVFK | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40029
Sequence Length: 358
Subcellular Location: Endoplasmic reticulum membrane
|
Q6CRH4 | MKMTEAQEFLTPTKGVNSSKFNINHGHFITNLENQESPSKLGAYTPGKYSTSRVIESLHKQIDELTSTNLKMTSQCHQLVNELESSGKKQNKQLETISRLQTENMNLNAILDRKTNRMNELESSLKKQTVFNEDAAKKNLELEETVKKLSLENEKLTEQSTLYKIQYEAIVDAHQSYKQFFTNETSTLRNDLMSLKQSMTKQLESKTKEVLAIDEKIQNKLESLDSAQESFKKHASEQIEDNIKELRLDSWQSSLREAQALLKEYKSQAQAEGITIQEQPKASIPQLRNPKRKTSGQKRTSFYGTPTGFSIPSNKQTPPSSSSTQLPGLKRASSIRISSDPNRNR | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39235
Sequence Length: 345
Subcellular Location: Endoplasmic reticulum membrane
|
C5DLA5 | MSNQEVDFQAAHLESPMKMSPSKVSMNHGAFMANMQNGYSPTREGATAGSSSTRVIEALHAQIDSLTKTNLDLTVQSNNLLSRLESSNNTQSKHLESISTLKHENDNLGLMLSRKERRVRDLEQQLSQLKHSYEEAAMDNKTMRHQLQTSGQREGTLENQLQQLQVQYDALVDGQKRYREKYDLEVEELKKSLQDFKRDNEMYLTKNIQTVVSNNTALQTKINQYSGKYKNLESLSQQHMQELSREVEGMASKLDLAKWEKLYEESRNMAIEYSEKTNVPLSPSFLAQHGAKSGSRSPSTSSSSTFVHPSQIRVPKVRHSSSSAKRSSFYGSNVSVPGGTVPGVKQPSASPTTPSSGGLPGVRRSSSVRGSSSSSRNSSGDLASAESAAQSQKGASKNSANNKKKRMSSHSYSKSNGFSFGEP | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46671
Sequence Length: 423
Subcellular Location: Endoplasmic reticulum membrane
|
A5E5U9 | MAGDSASLSLSPIKSDKAAVVSESPVKMKPGSSSSKVIDTLHTTIDSLSLEIATLKQTNQELSRKSQVATAKNDSFVDQLANLKHENDMLSALLKRKERRILDLEDQNSELSNSVESLNMLTKQMKMRCEKLSDSSMQSMAEYERLKISYDALVASCNEYKQHYKTELDTLQKSLDTYKQENHKQWETLNELISSNDKDIDTLLDSLNNKKKLMDNIYVNKNTKVLTMLSTLATLVKAHGTESKNVLGDNAQTIEFLLEKYPDLEEKILEKEQIEIDINSILYASKDALENTSFDEEDVTLINSPELEPSSDGNFPAQQLQKRNNVGNQQTSNSNNSNNSNSNSSSNSNSNSNSNNGSSNHAQNKRKGKRTPLSGNSPSVHMPSMWSNNSSSSSTSHTPFNSQNQNNHHHNSHHQQQLHARSNNTNKSYGNLSHDLQHGHLPKKHAAINNITNTYSRSSGGGGGGHNSGNNNGPNAASNSNNNNNRRRSGYYKKAVSSQT | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55370
Sequence Length: 500
Subcellular Location: Endoplasmic reticulum membrane
|
A3LXM3 | MEDNTASNKPTSRVIDSLHSQIDDLKTELETVKISHDDYKKKYVLVSQKNDSFVDQLANAKHENDMINALLKRKERRIADLEDQYNELSSSNESLQLNNKNMKIRCENLQQSSASSTAEYERLKIAYDALIASQVEYKRHYQKELNTLASKLEAYKTENKQRFQDLSSKLSSNDKDIDTLLDSMTNKRKALDNLYVNKNKTILELLTSLAKAAKIHGLDTKSTLEENTVAISSLLEKYPDLQEKILTHEKVEVDLDELISESNETLSNCSFESEATLVNSPELSDSASQSKNADHLKQDVKASSLSRSNTLQAKKRKNKRNSVRIDSKSGPDFSSITTPTTGQFALPKKPTFTSNNDNRGFSSRSPSDSSRNITPPHQDYEINPKFQNQNVHLNNDTNNKGGNYNNNNNNRSKRKSLYGGQYNSKRNSQIIDPNALNISMTT | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49999
Sequence Length: 442
Subcellular Location: Endoplasmic reticulum membrane
|
A7TJJ7 | MSLEDSRISNEDDSELLPPNKVVSSHGVFMASMNGSPQKIMRPSSVSGGSVNGSVSGSSQIGSGPNSNNNNNSSNNNNNSGSISSTKVIEALHEQIDALTNTNLKLTVQSQGLLEKLENSQQREGKFMENIASLRHENDNLSTMLNRKTRKLKDTELELEELKEKFDKITTEKKVLDDDLNKTSASETKLKEEMSMIENQYNSLIDSHEYYKDKYLQEINQLKRSLEDLTTEQENYLKRTNENNKLVEEKIDNYNNSFNQLKEINESLNNIIITKCESAIQELDLPNWVNLYKESKILVIDYAQQMNLEIPNNFKELVRDRTLEILESRSTSMSSQSSSENRQQFNNNNNNSHNQSSGNEEPLRMVKLRTVSPNSFNNSGSSLPSHIKRSSFYGGTKSLSSSNSGIPGTLPGVKRSGSLRKPSSRLPSTNTEPFSSPSSPSLNGTNKFGQNQNQASNSNSNPSQHNNSNIQLPGSRVSSVSHNPMHRKKRNSMMFHGN | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55690
Sequence Length: 498
Subcellular Location: Endoplasmic reticulum membrane
|
P38272 | MSDQDNTQTSSSKLAPHHNIFMANLESSPTKDRNTSSQNASSSRVIESLHDQIDMLTKTNLQLTTQSQNLLSKLELAQSKESKLLENLNLLKNENENLNSIFERKNKKLKELEKDYSELSNRYNEQKEKMDQLSKLAKNSSAIEQSCSEKLQNMEVNYNSLLESQNLYRDHYSDEISKLNEKIGLLELELSNQNLNYGSDTSSNSDIELNLNKFNDSVKDLKSLETEKDSKLSKIITHSLDELNLQSWLNLYQTNENLISTFAEKMDLKDVLKRNDEKISNKGAVVQTLKKNVQTQVESNNADALSSNNAQDMLPIKMVKLRKTPNTNDSSSNGNSSNNKRRSFYTASPLLSSGSIPKSASPVLPGVKRTASVRKPSSSSSKTNVTHNNDPSTSPTISVPPGVTRTVSSTHKKKGNSMVVHGAQS | 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 the emerging bud.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47417
Sequence Length: 425
Subcellular Location: Endoplasmic reticulum membrane
|
C5DUI8 | MTEDFEVNLGTGGEDNSSSTMEHRVLDSPPRVVIPEDTESPAKLAPNHGIFMASINKSSPAGKKSGEGAVLGMGAQSTKDNSTPRQNSSMLSTRVIESLHDQVDTLTSTNLQLTVQSKNLLDKLDTAQQKESKMLENSASLKHENENLVSMLNRKTRRLKDVEEELASHKKNHDSLEEEKTALQKKWESSSSEEATLRQQMEMVQAQYDALVDSHQYYKSHYSSQISTLSEQLENLKLEQRNYTQRVSDEANTFNAKLLEFDSKHANLQQAEETRVKYLESKYDSLTQQLDLPSWVQLYRESKNMVLEFAEKMKLKIPSDFETLIQDPELTALEAKNPNSNNAAALPLRVAKQRAGGGNATSTQSGTSGSNAAHGKRSSFYGGMASSYPASTLPGTLPGVRRSSSRRKPSSRVASDNSNSGDSSPIFPHSAVATAPRSSATAPSSRVSSTSTSSSTNHFAFHNNNSNNTYRKRQESTSVGNS | 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 the emerging bud (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52960
Sequence Length: 482
Subcellular Location: Endoplasmic reticulum membrane
|
Q753C3 | MPIYQLALPRSVLPRCRAVRYSRLLHSARCYSQDSQPKPGNTILQQLRKKLEPFCNSTKDKLEQTCAQVRYSSMQLRYHLEKARASVQEANKKLVQQEREGENSMLTFNDDLENKSKIVDLPSERERKRRQWSRKLEFYIDSLQETIFTATKALNDVTGYSSIEKLRKSIDMMETQLQETKRKLMQLREAHSDAVAVRNQSQRQVNELLQRKHMWSPGDLESFTRLYKEDADNVRRQEEANASLKAMEAKEEELSNSLHRAILTRYHEEQIWSDKIRRTSTWGTFILMGLNILLFLVVQLLLEPWKRRRLTNSFEDKVKRALEDHSLQHNLVLDRLSDRISEKIDAEMVHGIAPVPLPERTEQPEQPPAATTSGQPLGLREALASVGAAIAAEFGFFQAWIADHVRAIGGPTLSALQGFSGWPVLHIDLYNTVIFTCGMLLGLLVSH | 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: Mitochondrion inner membrane
|
Q4WV30 | MQPMPLLLRQSLRSSANFARTSLPIRPQFLPAAGPNLQPAREIQRSFSVCVRCQFRSQSPLYSSPEKDTSKDDAATQQSKDGSSTLTPGDESAKVEPDAETQRPSPAAGEQDTLQGFYQDAKNEPKRESAEKKGLPSYLEERRSQLSKQFTEMMDNLQSNIFVAGQRLNDLTGYSAIEALKKDIQLQEERLREARQRVREAKNAYAAAINRRSASQREVNELLQRKHAWSAADLERFTHLYRNDHTNEVAEMETQEALSAAERESEEAAAQLSKSILSRYHEEQVWSDKIRRMSTWGTWGLMGVNVLLFLVFQIAVEPWRRKRLVKGFEEKVIEAIEKEKAINHIEILKPQPALTSTSPSSKEEAAEPTPTSTAAGDTPTTDESTPAATDETITSEPVVWDSDPIPTFVTNITAEIATETTEDSAPKSATINGVEPRKSQLSRILPPLPPPTSLDSWRHTLNELFSDRSMVITQRDLTTVALQSAAAGAAIMGLVIALIRPR | 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: Mitochondrion inner membrane
|
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
Sequence Mass (Da): 30738
Sequence Length: 288
Subcellular Location: Cell membrane
|
Q5AQ36 | MGFSLSNFTSDPFAISTVSFGIMAWVVAIAGAASSKQENFPHFSWWGISYQIVIILIIFVLYANNNIELYKFTLVGLVSIAFIYTTNSTNNLIYNSNSAGNLCCAAGCILLSILNLIWILYFGGHPESPTNQFIDSFSLRGQGHEQLGSGSHNHNANNANNNIPIGAGNAIIGKGEMSPYDDRFAASGVNQPTSESLRLASGPQMGNGPFTTTGAIINPNLQQPLSGSIGGSAHHTPTNINNNNNNNNNTGYMTSSHLTGLENFSSPHVPGSGAGAGLGVGAGRDLTHNSNGGGGGSGGGPASANNSNNTNKRNTIYTDSETGTGITFRYKAKALYSYDANPDDINEISFVKDEILEVDDIDGKWWQARRANGQVGICPSNYVKLLDT | 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 invasive filamentation into semi-solid medium and plays a role in morphological dimorphic transition which is a differentiation program characteristic of C.albicans and which is known to play a major role in pathogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41071
Sequence Length: 388
Subcellular Location: Cell membrane
|
Q6FTC4 | MSGRRGKIINPRTRGAVRNVGFRNLISDPFAISSILIGLISWVITLGGCISVQVNEDFPRFTWWGIAFQFLIILMLIGFYIYDLVDYYRNFLTASIGVAFVYSTNSANYLIYGSGNQKAAASAGVVLLSMVNLIWIFYYGGDNASPINRWVDSFSLNGIRPSPFEAAKIKAYRRSSKQTQFRGSSVKLTHSTNNLHSASENLGLDNGFYNNPHTSNYVSSTALTEFENTGPPYPSASDLPTNNNAPLRSPQLGNNTIGDTYITATTNNNTNTTMGDTMGLYADLADESFPYRVKALYSYEADSADAYEMSFEQGEILMVSDIEGRWWKAKKESGETGIIPSNYVTIIDNDTEA | 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
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.