ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O16119 | MAFKTCGFSKKWLVIAVIVMCLCTECYCQCTGGADCTSCTGACTGCGNCPNAVTCTNSQHCVKANTCTGSTDCNTAQTCTNSKDCFEANTCTDSTNCYKATACTNSSGCPGH | Function: Contributes to protect body fluid from freezing at subzero temperatures. Lowers the freezing point of the hemolymph by about 2.5 degrees at a concentration of 1 mg/ml. Binds to nascent ice crystals and prevents further growth.
Sequence Mass (Da): 11558
Sequence Length: 112
Domain: Forms a right-handed beta-he... |
P24856 | VTAAPAATAATAATPATAALNFAATAATPATPATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAAAAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATAACNFAATAATPATAATPALIFAATAATAATPATAACNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPAT... | Function: Antifreeze proteins lower the blood freezing point.
PTM: O-glycosylated; contains disaccharide galactose-N-acetylgalactosamine attached to threonines in AFGP8 and AFGP7.
Sequence Mass (Da): 71267
Sequence Length: 790
Domain: Contains 44 copies of AFGP8 and two copies of AFGP7.
Subcellular Location: Secreted
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Q9SYT0 | MATLKVSDSVPAPSDDAEQLRTAFEGWGTNEDLIISILAHRSAEQRKVIRQAYHETYGEDLLKTLDKELSNDFERAILLWTLEPGERDALLANEATKRWTSSNQVLMEVACTRTSTQLLHARQAYHARYKKSLEEDVAHHTTGDFRKLLVSLVTSYRYEGDEVNMTLAKQEAKLVHEKIKDKHYNDEDVIRILSTRSKAQINATFNRYQDDHGEEILKSLEEGDDDDKFLALLRSTIQCLTRPELYFVDVLRSAINKTGTDEGALTRIVTTRAEIDLKVIGEEYQRRNSIPLEKAITKDTRGDYEKMLVALLGEDDA | Function: Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.
PTM: Phosphorylated.
Sequence Mass (Da): 36204
Sequence Length: 317
Domain: A pair of annexin repeats may form one binding site for calciu... |
Q9XEE2 | MASLKVPSNVPLPEDDAEQLHKAFSGWGTNEKLIISILAHRNAAQRSLIRSVYAATYNEDLLKALDKELSSDFERAVMLWTLDPPERDAYLAKESTKMFTKNNWVLVEIACTRPALELIKVKQAYQARYKKSIEEDVAQHTSGDLRKLLLPLVSTFRYEGDDVNMMLARSEAKILHEKVSEKSYSDDDFIRILTTRSKAQLGATLNHYNNEYGNAINKNLKEESDDNDYMKLLRAVITCLTYPEKHFEKVLRLSINKMGTDEWGLTRVVTTRTEVDMERIKEEYQRRNSIPLDRAIAKDTSGDYEDMLVALLGHGDA | Function: May mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.
Sequence Mass (Da): 36266
Sequence Length: 317
Domain: A pair of annexin repeats may form one binding site for calcium and phospholipid.
Subcellular Location: Cytoplasm
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Q9NFS4 | MANKNYQMSTGVTAVVQKVVEACQDESKRLDLIEIARSYPPNQLRNMQRTFQAITGTFLDAFLKKHLSKDFESLVLMLYKPRAQLLCELIRGATKGAGTDEKCLVDVLLTIETHEVREIRQLYYQLYNDSLGDVVRKDCGDKYMWAKLINAVATGDRIPRDTHELEEDLVLVRKAIETKGVKKDEVSTWIRIFATYTRADFRQLHKMYSAKYNGDSLRAGVEDEFQGLDEYAFKLAHDFLYDPCCAAAFSMNVAFAGSGSDSNRLNRITAMHFRECKGCKYYYKKVYGQAFDERCATELKGVYGDAIKLLWEPVTVPLLS... | Function: May function as a calcium-regulated structural element linking phospholipid bilayer and underlying axoneme.
Sequence Mass (Da): 38584
Sequence Length: 337
Domain: A pair of annexin repeats may form one binding site for calcium and phospholipid.
Subcellular Location: Cell projection
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Q8J0I8 | MTVRDWANRGQTYVNARAPNLLGRFRSTDDEDENNPSTELATDTTSAYGSTAASVVTMANSKPDDVSLYATSSHHHEYFTGSAWIHPVYTKEQMDALEVNHRKTETFSDRVALRAILLMRIIFDLCTGYKHPKEGEAHLPKFRMTTRQWLDRFLFLESIAGVPGMVAGMIRHLHSLRALRRDRAWIESLVEEAYNERMHLLTFLKLQKPSVQMRTGLLIGQIIFYNLFFISYLISPATCHRFVGYLEEEAVITYTRCLEDIDAGRLPELASMEVPDIARTYWHMEDDCTMRDLIQYVRADEAKHCEVNHTFGNLHQTSDR... | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40652
Sequence Length:... |
Q05140 | MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVADEVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAK... | Function: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces the... |
P38856 | MTTYFKLVKGATKIKSAPPKQKYLDPILLGTSNEEDFYEIVKGLDSRINDTAWTIVYKSLLVVHLMIREGSKDVALRYYSRNLEFFDIENIRGSNGSASGDMRALDRYDNYLKVRCREFGKIKKDYVRDGYRTLKLNSGNYGSSRNKQHSINIALDHVESLEVQIQALIKNKYTQYDLSNELIIFGFKLLIQDLLALYNALNEGIITLLESFFELSHHNAERTLDLYKTFVDLTEHVVRYLKSGKTAGLKIPVIKHITTKLVRSLEEHLIEDDKTHNTFVPVDSSQGSAGAVVAKSTAQERLEQIREQKRILEAQLKNEQ... | Function: Involved in endocytosis and clathrin cage assembly.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71660
Sequence Length: 637
Subcellular Location: Bud
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P53309 | MSSLYTKLVKGATKIKMAPPKQKYVDPILSGTSSARGLQEITHALDIRLSDTAWTIVYKALIVLHLMIQQGEKDVTLRHYSHNLDVFQLRKISHTTKWSSNDMRALQRYDEYLKTRCEEYGRLGMDHLRDNYSSLKLGSKNQLSMDEELDHVESLEIQINALIRNKYSVSDLENHLLLYAFQLLVQDLLGLYNALNEGVITLLESFFELSIEHAKRTLDLYKDFVDMTEYVVRYLKIGKAVGLKIPVIKHITTKLINSLEEHLREETKRQRGEPSEPQQDRKPSTAISSTSSHNNNSNDKNKSIAQKKLEQIREQKRLLE... | Function: Involved in endocytosis and clathrin cage assembly.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64328
Sequence Length: 568
Subcellular Location: Bud
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Q63HQ0 | MGNCCWTQCFGLLRKEAGRLQRVGGGGGSKYFRTCSRGEHLTIEFENLVESDEGESPGSSHRPLTEEEIVDLRERHYDSIAEKQKDLDKKIQKELALQEEKLRLEEEALYAAQREAARAAKQRKLLEQERQRIVQQYHPSNNGEYQSSGPEDDFESCLRNMKSQYEVFRSSRLSSDATVLTPNTESSCDLMTKTKSTSGNDDSTSLDLEWEDEEGMNRMLPMRERSKTEEDILRAALKYSNKKTGSNPTSASDDSNGLEWENDFVSAEMDDNGNSEYSGFVNPVLELSDSGIRHSDTDQQTR | Function: Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-adaptin attenuates the release of the AP-1 com... |
Q08DS7 | MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKESDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQE... | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane ... |
Q10567 | MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPSSNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYGTLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKRPEILKHE... | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes . The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane... |
O43079 | MVPKLFQSSRFKAFKKSETSELQKGLVSQYAYERIDAVKRTIAAMTVGKDVSSLFPDVLKNLATRDITLKKLVYLYLINYAKTHPDLCILAVNTFVKDSEEYNPTLRALAIRTMGCIRVNKIIGYLADPLRKALKDEHPYVRKAAAVCVVKMYDLDREYCASNGFIEQLQALVSDPNPVVVANAVRSLAEIHDQDPEKGYFNVVYTMTDRLMVALSECNEWGRITILNSLARFRTSDIKEAEYVCERVVPQFQHANSGVVLSAVKVIMVHIPLFSSDFTDFLYKKMAPPLLTLLSTDSEIQYVALRNINLILQKRPSIFD... | Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin ... |
P36000 | MPPLDKRIKKFLKDSIRIAPKISGKGELSELRTGLVSQYPQTRKDAIKKTIQQMTLGKDVSSLFPDVLKNIATIDVEQKKLVYLYVMNYAETHPELCILAVNTFITDAQDPNPLIRCMAIRTMSMIRVDKILEYIETPLRRTLHDDNAYVRKTAVICVAKLFQLNKDLCVELGVVEDLVNALDDSNPLVIANATAALIEIHNMDMDAVDLSSLIQSHVSQFLLALNECTEWARIIILGTLSEYSAKDSLEAQDIIDRVTAHLQHVNPAVVLATIKVIVRNLPQIEYSSNSLIMKRLSSAFVSLMSTPPEMQYVALKNIRI... | Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin.... |
P54672 | MISALFLMNGKGEVLISRIYRDDISRGVANAFRLEVIGSQETRSPVKLIGSTSFMYIKVGNIYIVGVSRQNVNACMVFEVLHQLVDIFKSYFDNLDEDSIRNNFVLVYELLDEILDFGYPQNCSTDVLKLYITQGQGKLKSLDKLKQDKISKITIQATGTTPWRTPDIKYKRNELYIDVVESVNLLMSAEGNILRADVSGQVMMKCFLSGMPECKFGMNDKVIMDREKSTNGGSAARSGARRANGIEIDDITFHQCVRLGKFDSDRTVSFIPPDGEFELMRYRTTEHINLPFKVIPIVREMGRTRLECSVTVKSNFSSKM... | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP50 is a subunit of the plasma membrane adaptor.
PTM: Phosphory... |
Q09718 | MISGLFIFNLKGDTLICKTFRHDLKKSVTEIFRVAILTNTDYRHPIVSIGSSTYIYTKHEDLYVVAITKGNPNVMIVLEFLESLIQDLTHYFGKLNENTVKDNVSFIFELLDEMIDYGIIQTTEPDALARSVSITAVKKKGNALSLKRSHSSQLAHTTSSEIPGSVPWRRAGIKYRKNSIYIDIVERMNLLISSTGNVLRSDVSGVVKMRAMLSGMPECQFGLNDKLDFKLKQSESKSKSNNSRNPSSVNGGFVILEDCQFHQCVRLPEFENEHRITFIPPDGEVELMSYRSHENINIPFRIVPIVEQLSKQKIIYRISI... | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP50 is a subunit of the plasma membrane adaptor (Potential).
Lo... |
P53680 | MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE | Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... |
O50016 | MIRFILLQNRQGKTRLAKYYVPLEDSEKHKVEYEVHRLVVNRDPKFTNFVEFRTHKVIYRRYAGLFFSICVDITDNELAYLECIHLFVEILDHFFSNVCELDLVFNFHKVYRYLILDEFILAGELQETSKRQ | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP2S1/AP17 is a subunit of the plasma membrane adaptor. The comp... |
Q84WL9 | MIRFILLQNRQGKTRLAKYYVPLEESEKHKVEYEVHRLVVNRDAKFTNFVEFRTHKVIYRRYAGLFFSVCVDITDNELAYLESIHLFVEILDHFFSNVCELDLVFNFHKVYLILDEFILAGELQETSKRAIIERMSELEKLQ | Function: Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in ... |
Q4WS49 | MVLSFILVQNRQGKTRLAKWYAPYSDEEKVKLKGEVHRLVAPRDQKYQSNFVEFKRSTKIVYRRYAGLFFCVCVDATDNELAYLEAIHFFVEVLDQFFGNVCELDLVFNFYKVYAILDEVFLAGEIEETSKQVVLTRLEHLDKLE | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Location Topology: Peripheral membrane protein
S... |
Q54H39 | MIHFILIQNRQGKTRLSKWYTPYEDVEKRKLSHEIHKIVNSRETKFTNFVEFRTHRIVYRRYAGLFFSVCVDPTDNELFCLEAIHLFVEVLDAYFGNVCELDLVFNFYKVYAIIDEVFLAGELMEPSKHVILQRMEFLDNLP | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Location Topology: Peripheral membrane protein
S... |
Q5BFF8 | MVLSFILVQNRQGKTRLAKWYAPYSDEEKVKLKGEVHRLVAPRDQKYQSNFVEFKRSTKIVYRRYAGLFFCACVDATDNELAYLEAIHFFVEVLDQFFGNVCELDLVFNFYKVYAILDEVFLAGEIEETSKQVVLTRLEHLDKLE | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Location Topology: Peripheral membrane protein
S... |
Q7SAQ1 | MLSFILIQNRQGKTRLAKWYVPYSDEEKIKLKGEIHRLVAPRDQKYQSNFVEFRNHKVVYRRYAGLFFCACVDTNDNELAYLEAIHFFVEVLDSFFGNVCELDLVFNFYKVYAILDEVFLAGEIEETSKQVVLTRLEHLDKLE | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Location Topology: Peripheral membrane protein
S... |
Q9Y7L6 | MIQFILIQNRHGKNRLSKYYVPFDDDEKVRLKARIHQLISQRNQKFQANFLEWENSKLVYRRYAGLYFCFCVDSTDNDLAILEMIHFFVEILDSFFGNVCELDLIFNFYKVSAILDEIILGGEIGESNKKSVLERIEALEKLE | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Location Topology: Peripheral membrane protein
S... |
Q00381 | MAVQFILCFNKQGVVRLVRWFDVHSSDPQRSQDAIAQIYRLISSRDHKHQSNFVEFSDSTKLIYRRYAGLYFVMGVDLLDDEPIYLCHIHLFVEVLDAFFGNVCELDIVFNFYKVYMIMDEMFIGGEIQEISKDMLLERLSILDRLD | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Location Topology: Peripheral membrane protein
Sequence Mass (Da... |
B8GMY8 | MSIYAVGDLQGCLTPLKRLLEQVRFDPAADQLWLVGDLVNRGPESLEALRFVRDLGDAAITVLGNHDLHLLAIHQGVHKVRRKDTVQPILDAPDRAELMDWLRHRPLLHHDPRIQWTLLHAGLPPQWDLAMARACASEVETVLRGPDHPTLLERMYGDEPDQWSESLQGWARLRFITNCFTRLRYCTADGSVDMAYKGAPGGQLPHLMPWFAVPGRRSVGTRIVFGHWSTLGLYQGDDVLCLDTGCVWGQRMTLARLDSSALETMHTRCE | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 30483
Sequence Length: 270
EC: 3.6.1.41
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C4L9L6 | MATYFVGDIQGCNDELQQLLALAQFNPQHDELWLTGDLVARGPKSLDVLRFVYGLGDRATTVLGNHDLNLLAVDAGYSQAKKKDKTENILTAPDRHELMTWLRTQPIMAEHPTLPVMMTHAGLSPQWDLATARHCAREVEMLLRSDQGNWLLGHMYGEEPSHWDARLTGLPRWRYIINSFTRMRFCRNDGSLEFKCKEAPSDKPALLAPWFEVRQAAPDEPHLVFGHWAALMGKCPLPTIKALDTGCVWGNQLTLWRWDDNAMFSLNCPAYASGGE | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 31187
Sequence Length: 276
EC: 3.6.1.41
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Q8H1U4 | MAGLTRTAGAFAVTPHKISVCILLQIYAPSAQMSLPFPFSSVAQHNRLGLYLLSLTKSCDDIFEPKLEKLINQLREVGEEMDAWLTDHLTNRFSSLASPDDLLNFFNDMRGILGSLDSGVVQDDQIILDPNSNLGMFVRRCILAFNLLSFEGVCHLFSSIEDYCKEAHSSFAQFGAPNNNLESLIQYDQMDMENYAMDKPTEEIEFQKTASGIVPFHLHTPDSLMKATEGLLHNRKETSRTSKKDTEATPVARASTSTLEESLVDESLFLRTNLQIQGFLMEQADAIEIHGSSSSFSSSSIESFLDQLQKLAPELHRVHF... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degr... |
Q54VV5 | MDKYRLTPHKITICVLVEYYLNGTIKYHQKQSLSHLLIRHIKENNYQDTVKEVSLYDFIEKELKYVLPIQFINNEFLRMIQFDSVDDIYQFMSSLKELFNGSNDHESINSKQMQLLDSKSILGIFIKKVILNFNQILFDGLIKLYDQLDQYLNDFYNEINKIQQQQQQQQQKEHCENDNSIDMSMDQEQQQQQQEDYNEISNYENKIKFLSPLDEERFIYEETIRINSLIGIETPLEIENQVNRLKASLPNVKRVHLISLLFNIGYQDYDQSLEDLHRYFDYVNGQMTSSQWSSSASSFLFTPNDNYQSGNSNSSNYYYN... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence Mass (Da): 117792
Sequence Length: 1017
Pathway: Protein modification; protein ubiquitination.
Subcel... |
Q9UJX4 | MASVHESLYFNPMMTNGVVHANVFGIKDWVTPYKIAVLVLLNEMSRTGEGAVSLMERRRLNQLLLPLLQGPDITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMELTSRDEGERKMEKEELDVSVREEEVSCSGPLSQKQAEFFLSQQASLLKNDETKALTPASLQKELNNLLKFNPDFAEAHYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESKSNGEEGYGRSLRYAALNLAALHCRFGHYQQA... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q8BTZ4 | MMTNGVVHANLFGIKDWVTPYKIAVLVLLNEMGRTGEGAVSLVERRKLNQLLLPLLQGPDITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMDREDGEKQMEKEELDVSVREEEVSCSGPLSQKQAEFFLSQQAALLKNDETKALTPASLQKELNNLLKFNPDFAEAHYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAEGKSNGEEGYGRSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQESN... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
A1L1K3 | MMTNGVVHANLFGIKDWVTPYKIAVLVLLNEMGRTGEGAVSLVERRKLNQLLLPLLQGPDITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDLEQFFDDLSDSFSGTEPEVHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMDREDGERQMEKEELDVSVREEEVSCSGPLSQKQAEFFLSQQAALLKNDETKALTPASLQKELNNLLKFNPDFAEAHYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAEGKSNGEEGYGRSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQESN... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q08683 | MSKYGPLGITNFITPYDLCILILIHAHCSQDNGISVPTAVFLRLISPTRPSLEWNPLLKDNSNLRSSSIVPPPVLPILDNIIRILLDDKDGNKIALTLMGYLEAINGLDSINRLMMDLEKNCLVNNYRSMKMRTTSTRRQMTRASFLGTFLSTCIRKYQIGDFEMRETIWINLQNFKTVFKHTPLWLRFKDNVHIQKVKNCLLANDEISVEDQQMVEFFQHFNNGNDADSKTMNEENYGTLISIQHLQSIVNRQIVNWLDNTEFNLMGQEETSSTYEEQSGLVFDLLDTLSLNDATKFPLIFILKYLEAIKENSYQTALD... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... |
Q8VY89 | MEVPKEQIATLIEHGLYDSAEMLGCFLVSSPTVSAETSPQLKAENLILLGDALFHQREHRRAIHTYKQALHHYTRIPKQSSGISRSSLSLSTRSSVNASSISAINENEVRFKIASSHFALNETKAAIAEMESVKTRSLEMNILMAKLHRNSGYNRGAIAFYKECLRQCPYVLEAVIGLAELGVSAKDIISSFTQTSNRSAKVSLDQIDPTRWLQRYVEAQCCVASHAYKGALELFAELLQRFPNNVHLLTETAKVEAIIGKNDEAIMRFEKVRSIDPYTLTSMDEYAMLLQIKCDYSRLNKLVHDLLSVDHTRAEVFVAL... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degr... |
Q54D58 | MIQQLPMVNVELMISNLRILVESKQFSSAEFLGNFVISVPNQQKTPHQNIISFSLFGDSLFGKNEFVRSLKYFKQSLDILFKVYNNPNNNNNNNNKQADFDNKQFEYELKYKISLCYIKINRNNLAISYLESIPFSSRGLDTHLTIARLYKDIGKEKSKECIISYKEVIKLCPLCLEAINSLKEMGENVDQVLIPSINKFQQKNNSFNSNNIIDLSWISLLSMSQYEMKRNQPEKSLILLKKVESKFSTNLYVLEKLALSYLYHDEPSIINTFNIFQKIRLLDPYYIGSMDIFCSLLKRRSLQFELNKVCNDLVASNPYC... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence Mass (Da): 66851
Sequence Length: 580
Pathway: Protein modification; protein ubiquitination.
Subcellu... |
Q9UJX3 | MNVIDHVRDMAAAGLHSNVRLLSSLLLTMSNNNPELFSPPQKYQLLVYHADSLFHDKEYRNAVSKYTMALQQKKALSKTSKVRPSTGNSASTPQSQCLPSEIEVKYKMAECYTMLKQDKDAIAILDGIPSRQRTPKINMMLANLYKKAGQERPSVTSYKEVLRQCPLALDAILGLLSLSVKGAEVASMTMNVIQTVPNLDWLSVWIKAYAFVHTGDNSRAISTICSLEKKSLLRDNVDLLGSLADLYFRAGDNKNSVLKFEQAQMLDPYLIKGMDVYGYLLAREGRLEDVENLGCRLFNISDQHAEPWVVSGCHSFYSKR... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q12107 | MNQNGDKNEGKLFQLPSLPPWKTPRFNKANFNNFTTPLRKRSTRVINDDSMPITGEVLEERTADDLYGINMDVDEVDYLNTLSHIEEEKQYDYSPFCERNTLRESRIDSFLKAERAAHCLVFHKVGHLDGIDSYRPDIDIMCGEEANKYDSANPEGNGSMLLESVPGCNKEDLERLSRREFVTNSKPNMRRLDDIINHETNALKSFWNDSGLVNSLQSHHLHEEYLLLQEELKNVYKIKCHDRVPIESLRDKCRRHYSNEDSSFL | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... |
Q5P5G2 | MYTVDIDTGGTMTDALVSDGEQRHAIKVDTTPHDYTVSFNGCLSEAAKRLGYPSTEAFLAKVGMIRWSSTITTNVLGERRGSKVGLLVTEGNEENLYGTVQSPVVGELVDERNIIGLPSNPTAVDILSGVKQLLEGGVRRICVCLANAFPDNGAEREIKAVIEDQYPDHIIGAVPVLLGSEMAPLRHDQTRVHYSLMNAYTHTQLATSLFKAEDLLRDDHNWTGPLLIGNTNGGVARIGKTKSVDTIESGPVFGTFGGAYMARLYGLKDVVCFDVGGTTTKASIIRDGQPMFQRGGELMEVPVQSSFAMLRSAVVGGGSI... | Cofactor: Divalent metal cations. Magnesium or manganese are required for activity.
Function: Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.
... |
Q9M9A8 | MEPDLHDQQQQQRVHSVVIITLPPSDDPSQGKTISAFTLTDHDYPLEIPPEDNPNPSFQPDPLHRNQQSRLLFSDLSMNSPRLVLGLLGISLLAVAFYASVFPNSVQMFRVSPDERNRDDDDNLRETASFVFPVYHKLRAREFHERILEEDLGLENENFVESMDLELVNPVKVNDVLSTSAGSIDSSTTIFPVGGNVYPDGLYYTRILVGKPEDGQYYHLDIDTGSELTWIQCDAPCTSCAKGANQLYKPRKDNLVRSSEAFCVEVQRNQLTEHCENCHQCDYEIEYADHSYSMGVLTKDKFHLKLHNGSLAESDIVFGC... | Function: Involved in proteolytic processing of BAG6 and plant basal immunity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65349
Sequence Length: 583
Subcellular Location: Membrane
EC: 3.4.23.-
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S0DS17 | MSYQSILLRQVNSLCDNLEEVARDENGGLIDMAMQSDYFTFDVMSEVIFGMAYNALKDTSYRFVTGALGSSNIRIGTLVQSPLPAMCRIDKYLFPESIQGRNKFLGFIGSLLRDRSKASFAGNGNVFSFLETAKDPDGGNQLSKSEIRAECATLVAAGTDTSSSTLAATLFYLSRNSKCYSRVSEEVRNAFSSHQDIKIGPELNSCVYLRACIEETLRMSPPVGAALWREIGPGGMNIGPLTLPAGVDVGTGIYSLHHNAAYHPEPFKYLPERWLVGEGSSTSESVELARSAFAPFSRGPRSCVGKGFAYHELTLTIAHI... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the cyclic tetrapeptide apicidin F (APF) . The non-ribosomal peptide synthetase apf1 incorporates four different amino acids to produce apicidin F: L-phenylalanine, D-pipecolic acid (D-pip), N-methoxy-L-tryptophan and L-... |
S0DL65 | MKPHTVSLVLSNLASLAAATCKCTPGHACWPSLEEWSRFNSSIGGQLIQSSPVAEACYSGPKDNAACQNIEKSWTDDVFQVSQPIGYAWPLNLSCPLPTPGLDTKCSIGNSPVYVVNVTCEEDITRGIKFAQEKNLRLVVKSTGHDSQQRSTGYGSLSIWLHNFRKGFRFQGHNPVLATCPKSGWKGSTLTINGGYSWRDIYPAAQKQGLIVIGGLDRGPCSTGGWTQGGGHSPGTHYFGIGADQVLSARVVLASGKIVVASPCENEDLFFAIRGGGGGTFGVVTEITVKTYPTKALSTINLIVGSKGDETVPKFLDAVA... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the cyclic tetrapeptide apicidin F (APF) . The non-ribosomal peptide synthetase apf1 incorporates four different amino acids to produce apicidin F: L-phenylalanine, D-pipecolic acid (D-pip), N-methoxy-L-tryptophan and L-2-am... |
Q9VTU1 | MAETPESQAALSTSSSTPADKDGSKICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYYCKNQAWG | Function: Required for autophagy.
PTM: Conjugation of the G-112 to the K-132 of Autophagy protein 5-like is a covalent modification that is essential for autophagy.
Sequence Mass (Da): 12348
Sequence Length: 111
Subcellular Location: Cytoplasm
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O28523 | MPVLLIVVDGLSDRPIDGKTPLSVARKPNLDRLAEMGINGIMDTIAPGIRPGSDTSHLALLGYDPYKYYSGRGPIEAAGVGIEIKPGDVAFRANFATVEGEGSIFDKTVVDRRAGRIEDTSELIKALREIELPVELLVERGTGHRAAVVFRGEGLSDRVSDTDPKAVGKKVKRCVPLADDAKAKKTAEIVNEFMQKAHEVLENHPLNRERAEKGLLKANALLLRGAGEMPHVPSFKDKTGLRLCVIAATALIKGVGRVVGADVITPEGATGNKNTNLEAKVKAAINALESYDVVLLHIKATDELGHDGDFEGKKAFIEKL... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 44096
Sequence Length: 408
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q59007 | MKKGKCVIFIIDGLGDRPNEKGLTPLKEAKTPTMDKIAKEGICGLMNAIDIGIRPGSDTAHLAILGYNPYEVYTGRGPLEAFGVGLDLKEGDIAFRCNFATVDENFVVLDRRAGRISPEEAEELEKEIDGLEIDGVKVIFKSSKGYRGALVLRGEGLSCRVSDGDPHEEGVKVSEIKPLDDSEEAKRTAEILNKLLKIVYEKLNNHPINEERRKKGLPPANIILPRGAGVVPKIEKFSEKYNMKGACICGTGLIKGMAKMIGLDVIEVEGATGTPKTNFMGKAKALVEALKEYDFVLVNVKGADEASHDGNYELKKEVLE... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 45226
Sequence Length: 411
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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O28847 | MKYLLLIPDGMADWEVEELDGRTPLEVAETENMDFLAKEGACGIAKTVPDGFEPGSDVANLTILGVDVRKHYTGRGPIEALARGVKGKLVFRCNLVKVEDGVMVDYSGGRISDEEARKVIEELNRAKPYDFVKFYAGKSYRNLLVINKDFRDDVKTFPPHDITGKEIDKHLPSGGELAELLKELMGWSAEILPEITDKANMIWPWGGGRMPSFPNFGQRYGLRGAMITEVDLLEGIARGMGMEVVQVEGITGYIDTNYRGLVRETARALEEHDFVVLHTEGIDEVGHEGDAELKVRAIELYDSKIVGKLLNKVDLDETRI... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 42457
Sequence Length: 380
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q60326 | MRAILILLDGLGDRASEILNNKTPLQFAKTPNLDRLAENGMCGLMTTYKEGIPLGTEVAHFLLWGYSLEEFPGRGVIEALGEDIEIEKNAIYLRASLGFVKKDEKGFLVIDRRTKDISREEIEKLVDSLPTCVDGYKFELFYSFDVHFILKIKERNGWISDKISDSDPFYKNRYVMKVKAIRELCKSEVEYSKAKDTARALNKYLLNVYKILQNHKINRKRRKLEKMPANFLLTKWASRYKRVESFKEKWGMNAVILAESSLFKGLAKFLGMDFIKIESFEEGIDLIPELDYDFIHLHTKETDEAAHTKNPLNKVKVIEK... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 49350
Sequence Length: 428
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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O26518 | MITMKHVILVGDGMADYPLDELDGKTPLQVADKPNMDQLAGMGACGLLRTVPEGMEAGSDVANLSIMGYDPRRYYTGRGPLEAASIGVELGDDDVAFRCNLINADERIVDFNAGHIETAEASSLIDALNHELETRGRFYAGVSYRNLFVIEGRGYTSVRVEPPHDIVGESVAAHLPSGSEEADHIRELMLESAGVLRSHEVNLKRESMGKRPATMIWLWGQGLRPSMEPFSERYGIRGATITAVDLIKGLGVYAGLENIHVPGATGYLDTDYRAKGRYAAGALEEYDFLYVHVEAPDEAGHAGDAEEKIRAIENIDRFVL... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 44100
Sequence Length: 402
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q9YBI2 | MKILYIVLDGAADSPTSPRKTLEEASKPNIDSLGSHAVCGMVYTVKPGVAPQSDYATLSLLGYNPDEYYPGRGPLEAFGAGIEMRRGDIALRANFATVDPGTLRIIDRRVGRSLTSREARELASAVDGMELEDGEGTALFRATIGHRGVLVLRHRSKPLSDAISNTDPAYERRGRFSVALEKYEPFIKLSNPLVEDEAAVLAARMLNEFTLKAVEILDSHPVNLAREKRGLLKANAILSRDAGGLPEEKPPSFQERFGLRGASIVEMVVERGISRYIGLDDIRVEIEGRAREEVYREEAARAVEALETHDLVYVHLKGPD... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 46200
Sequence Length: 424
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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O66820 | MDVISELVKKNGSKILLIVLDGLGGLPVKEGKTELELAKTPNLDKLVKNSATGLHIPVDWGITPGSGPGHLGLFGYDPIKYQIGRGILEALGLGIDVKDTDIAVRGNYATVEYRNGKPIVVDRRAGRIPTEENKRITAKLQEAIKEIDGVQVIIKPGMEHRLAIVFRFPEKLSPGSDAINDTDPQQVGKEPLEPKGENPNAEKVAEVVRKFIQRATEILRNEPKANYILLRGFSQKPDIPTMEERFGVKPCCIAVYPMYKGLASLVGMDVIEFEGSTIQDEIDTLKKVWNEYDYFFVHIKKTDSYGEDGNYEGKVSVIED... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 45006
Sequence Length: 407
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q9RSA0 | MSDLLDTVRGLAKKTDSKILMVVLDGVGGLPLTVNGDTELATARTPNLDALAQESQLGQLELVGAGITPGSGPGHLSLFGYDPLKYVVGRGALSAVGIGVKLNRGDVAVRGNFATLGAGRLILDRRAGRPSDEKNAEIVAKLRAAIPEIDGVAVEVYTESEHRFVVVFRAPEGQPLGANISDVDPQVTGVEPKTAIANDPSSEVTAGLINTFVARAEVALADEPQVNGVLFRGYSDVPHFPSFEDAYQLKAACIASYPMYKGLASLVGMDVLPVEGHEDALEGKVKALRENWAKYDFFYFHIKKTDSTGEDGDFAEKVHK... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 44109
Sequence Length: 410
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q74C57 | MKYIVLLGDGMSDEPMQELGGKTPLQAARTPHMDAMARRGRIGLARTVPEGYPPGSDVANLSVFGYDPRACYTGRSPLEAASMGVELGSADVAFRVNLVNLAPTRGTLVMNDYSAGHISTAEGRELIEAIQGVMGTDEFQFYPGVGYRHLMVWRNGKCGMTVVPPHDISGQSILEHLPKGEGAERLIELMNSSQLVLNNHPQYRRRLEEGKVPANSIWLWGHGKAPRMASFHEKFGLTGAVISAVDLVRGIGVCAGLDVIKVEGATGYIDTNYEGKVTAALEALEAHDYVYLHVEAPDEAGHGGNLEHKLKAIEDFDARV... | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 43249
Sequence Length: 399
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q06481 | MAATGTAAAAATGRLLLLLLVGLTAPALALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCKSRFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTEYVCCPQTKIIGSVSKEEEEEDEEEEEEEDEEEDYDVYKSEFPTEADLEDFTEAAVDEDDEDEEEGEEVVEDRDYYYDTFKGDDYNEENPTEPGSDGTMSDKEITHDVKAVCSQEAMTGPCR... | Function: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kall... |
Q6Z6L4 | MAAAEQSAEQFRGQARLPGFAAPRRYDLRLVPDLDGCAFTGSVDVSVDVTAPTRFLVLNAAELEVSPGGVQFKPHGAEQELHPAEVTNVPEDEILIIRFNEVLPVGEGTLVIAFKGTLNDKMHGFYRSVYELNGEKKNMAVTQFEPADARRCFPCWDEPSFKAIFKITLEVPSETVALSNMPVVEEKVNGLIKAVYFQETPIMSTYLVAVIVGMFDYVEAFTTDGTRVRVYTQVGKSAQGKFALEVAVKTLVLFKEYFAVPYPLPKMDMIAIPDFASGAMENYGLVTYRETALLFDEKHSAAANKQRVAVVVAHELAHQW... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as ... |
Q0J2B5 | MAPAPAPAGSADQFRGQARLPRFAAPRRYELRLRPDLDACVFTGDASVVVDVSAPTRFLVLNAADLAVDRASIRFQGLAPTEVSLFEDDEILVLEFDGELPLGEGVLAMDFNGTLNDQMRGFYRSKYEYKGETKNMAVTQFEAVDARRCFPCWDEPAFKAKFKLTLEVPSELVALSNMPVACETIAGPIKTIHYEESPLMSTYLVAIVVGLFDYVEGVTSEGNKVRVYTQVGKSSQGKFALDIGVKSLNFYKDYFDTPYPLPKLDMVAIPDFAAGAMENYGLVTYREVSLLFDEQSSSASFKQNVAITVAHELAHQWFGN... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as ... |
Q8VZH2 | MDQFKGEPRLPKFAVPKRYDLRLNPDLIACTFTGTVAIDLDIVADTRFIVLNAADLSVNDASVSFTPPSSSKALAAPKVVLFEEDEILVLEFGEILPHGVGVLKLGFNGVLNDKMKGFYRSTYEHNGEKKNMAVTQFEPADARRCFPCWDEPACKATFKITLEVPTDLVALSNMPIMEEKVNGNLKIVSYQESPIMSTYLVAIVVGLFDYVEDHTSDGIKVRVYCQVGKADQGKFALHVGAKTLDLFKEYFAVPYPLPKMDMIAIPDFAAGAMENYGLVTYRETALLYDEQHSAASNKQRVATVVAHELAHQWFGNLVTM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metallopeptidase that binds to the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). Required for embryonic and seedling development as well as cell cycle progression. Homodimerization is required to proper localization and activity. May play a negative role ... |
P38700 | MSSSLFILDENLEPLVSKNIRALPNLSSVLSSFKQCYHDGSPPILSQNDWFFIHLKRDFLHFVSVIHTTDKPNIDLMTILAFLEQFYHLLQKYFEIEVLTKNVILDNILLVLELIDECIDFGIVQVTDPSIIKDYIRVKVNVPRVTVDNEEWSPGEESSSSSGSDSDSEYSNTNKRKDKKKKRKKKKGTKGKSVGKSKLKSIMVNNKENRGINVVETVKETLRNKNDTGKEAANDELPNDGNDLYINGDIAKTIIMPISWRTKGIHYAKNEFFLDVIERVQYLMDFEKGVIRKNLIHGEIVCRCYLSGMPKLKISINKIL... | Function: Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates of cargo protein sorting in clathrin-coated vesicles . AP-1R has a specific role in SNARE SNC1 sorting . In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3 .
Location Topology: Peripheral m... |
P0DMT9 | MDLKVVAVSFLLLVLCSEAAGYQLLTWEQANTAVKGVLDKVHSTGVEKLRDIYDKSVDAVGTYTSILTDQLYHWWCGEQ | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein ... |
P19034 | MGTRYFLVGFLILLVLGFEVQGAHVPQQDEASSPALLTQVQESLLGYWDTAKAAAQKLYKKTYLPAVDEKIRDIYSKSTAAVTTYAGIITDQVFSVLSGKD | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein ... |
P12278 | MGTRYLLVLLLVLLVLGFEVQGAHESQQDETTSSALLTQMQESLYSYWGTARSAAEDLYKKAYPTTMDEKIRDIYSKSTAAVSTYAGIFTDQLLSMLKGDS | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein ... |
P02749 | MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTI... | Function: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
PTM: N- and O-glycosylated. PubMed:6587378 also reports glycosylation on '... |
O14791 | MEGAALLRVSVLCIWMSALFLGVGVRAEEAGARVQQNVPSGTDTGDPQSKPLGDWAAGTMDPESSIFIEDAIKYFKEKVSTQNLLLLLTDNEAWNGFVAAAELPRNEADELRKALDNLARQMIMKDKNWHDKGQQYRNWFLKEFPRLKSELEDNIRRLRALADGVQKVHKGTTIANVVSGSLSISSGILTLVGMGLAPFTEGGSLVLLEPGMELGITAALTGITSSTMDYGKKWWTQAQAHDLVIKSLDKLKEVREFLGENISNFLSLAGNTYQLTRGIGKDIRALRRARANLQSVPHASASRPRVTEPISAESGEQVER... | Function: May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver.
PTM: Phosphorylated by FAM20C in the extracellular medium.
Sequence Mass (Da): 43974
Sequence Length: 398
Subcellular Location: Secreted
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Q650H6 | MIMSKEKLIKSIREIPDFPIPGILFYDVTTLFKDSERLQELSDIMYEMYKDKGITKVVGIESRGFIMGPILATRLGAGFIPIRKPGKLPAETMEESYDKEYGKDTVQIHKDALNENDVVLLHDDLLATGGTMKAACNLVKKLYPKKVYVNFIIELKELNGKQVFENDQDVDIQSVLSL | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20175
Sequence Length: 178
Pathway: Purine metabolism; AMP biosynthesis via salva... |
O34443 | MDLKQYVTIVPDYPKEGVQFKDITTLMDKGDVYRYATDQIVEYAKEKQIDLVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPREVIKVDYGLEYGKDVLTIHKDAIKPGQRVLITDDLLATGGTIEATIKLVEELGGVVAGIAFLIELSYLDGRNKLEDYDILTLMKY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18875
Sequence Length: 170
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q8A2N8 | MIMSKETLIKSIREIPDFPIPGILFYDVTTLFKDPWCLQELSNIMFEMYKDKGITKVVGIESRGFIMGPILATRLNAGFIPIRKPGKLPAEVIEESYDKEYGTDTVQIHKDALDENDVVLLHDDLLATGGTMKAACELVKKLKPKKVYVNFIIELKDLNGKSVFGDDVEVESVLTL | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19781
Sequence Length: 176
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q6MPK7 | MDLKSLIRDVPDFPKPGIIFRDMSPLLQNAEALSFVSHNLLKHVDLTHVDYFAGIESRGFILAAHMAATHKKGFLPIRKAGKLPPPTRKVSYALEYGTAEIELPPGRGNVVIVDDVLATGGTLQAAIDLCLLAGYSVESVAVLVNLTFLNKMTYNDQKVASLVQY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18006
Sequence Length: 165
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q8G6B5 | MAQSDITIDALSKVGQQDAEYLVSLVRSVPGFPKEGIIFRDFMPVLADPKGLKILLKALEEALPVSPSEFDSIAGLESRGFLFGPVMAAHLGKGFIAVRKAGKLPPETIGESYDLEYGTASVEIETDAVQAGKRVLIVDDLIATGGTAKAATDLIEKAGGTVVGFSFVMRLDGLDGLDKLDGKPSSSLIAMPA | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20251
Sequence Length: 193
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q8RDM9 | MDLKNYVASIENYPKEGIIFRDITPLMNDGEAYKYATEKIVEFAKDHHIDIVVGPEARGFIFGCPVSYALGVGFVPVRKPGKLPREVIEYAYDLEYGSNKLCLHKDSIKPGQKVLVVDDLLATGGTVEATIKLVEELGGVVAGLAFLIELVDLKGRERLDKYPMITLMQY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18910
Sequence Length: 170
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q74CZ3 | MDELKNIIRDVPDFPKKGIIFKDITTLLADAPSFQRMVDLIAHRYVGKKISKVVVVEARGFVIGAALAYKLGAGVVLVRKPGKLPSETYSKTYQLEYGSDTLEIHTDAIAKGERVIIADDILATGGTMAAVVDMVEALGGEIVECCFMAELEFLGGRKRLPEGKVYSLLTF | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18652
Sequence Length: 171
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q4KFF5 | MAFDSFDIKSLIRPVIDFPKPGVIFRDITPLFQSPRALRLVADSFAQRYVEEDFSHIGAMDARGFLIGSIIAYQLNKPLILFRKQGKLPADILAEGYRTEYGEAFIEVHADSLCEGDSVLLIDDLIATGGTLIAAANLVRRMGAKVYEAAAIIDLPELGGSQKLQDMGIPTFCLTQFSLTER | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20056
Sequence Length: 182
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q884U6 | MTFDQSNFKSLIRPVVDFPKPGVVFRDITPLFQSPKATRQVIDSFVQRYIDADFSHIGVMDARGFLIGSVVAYQLNKPLVLFRKQGKLPADVLSEAYQTEYGEAYLEVHADSLCEGNSVIMFDDLIATGGTLIAAANLIRRMGAQVHEAAAIIDLPELGGSKRLNDLNIPTFCLTEFALDEQ | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20112
Sequence Length: 182
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q8Y2B9 | MTDASISPSSPVPASTELGDVTRYLRERIRTVPDWPQLGVMFRDITPLLQDPKSLRVLVDVFVHRYMGQGLNLVAGIDARGFILGSIVAYELNLGFVPIRKKGKLPFTTVAEEYMLEYGSATVEIHADACKPGDRVLLIDDLIATGGTMMAGKRLLERLGATVVEGAAIVDLPELGGSRLLMDGGLPLFTVCRFDGH | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 21384
Sequence Length: 197
Pathway: Purine metabolism; AMP biosynthesis via salva... |
P36972 | MSESELQLVARRIRSFPDFPIPGVLFRDISPLLKDPDSFRASIRLLAGHLKSTHGGKIDYIAGLDSRGFLFGPSLAQELGVGCVLIRKRGKLPGPTVSASYSLEYGKAELEIQKDALEPGQKVVIVDDLLATGGTMCAACELLSQLRAEVVECVSLVELTSLKGREKLGPVPFFSLLQYE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19546
Sequence Length: 180
Pathway: Purine metabolism; AMP biosynthesis via salva... |
A9WQH7 | MGIHAEQPKESIEEQIQRLCATVPDYPEPGITFRDLTPVFADGAALRAVVDALVEPFAGQFDAVAGVEARGFLLAAAAAYATGTGVITVRKAGKLPRAVYTEHYSLEYGTAALELHRDDLPAGSRVLILDDVLATGGTLAATSKLFAKAGVNVAGYGVVLELAELHGREALAGHQIRSLVRL | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19150
Sequence Length: 182
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q6CA53 | MSLQTLQTELKAKLRQYQDFPSKGIVFEDILPIFQDPKSFQQLIDAFKLHIKDTFGDKKIDVIVGLDARGFLFGPTLALAIGAAFVPVRKQGKLPGKTVHAEFQKEYGKDVFEIQEDAIKPGQTVIVVDDIIATGGSAACAGDLVTKLKGEVLEFIFILELLFLKGRDKLCAPAYTLLSGQE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20029
Sequence Length: 182
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q89EG9 | MDMKKYAAEAIGTFWLTFAGCGSAVIAAGFPQVGIGLVGVSLAFGLSVVTMAYAIGHISGCHLNPAVTVGLAAGGRFPAGQILPYVIAQVCGAIVAAELLYIIASGAPGFDVTKGFASNGYDAHSPGQYSMMACFLTEVVMTMMFLFIIMGATHGRAPAGFAPLAIGLALVMIHLVSIPVTNTSVNPARSTGPALFVGGWAMAQLWLFWVAPLIGGALGGVIYRWLSEEPTGVVAGAKAA | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
Q2YR68 | MLNKLSAEFFGTFWLVFGGCGSAILAAAFPELGIGFLGVALAFGLTVLTMAYAVGGISGGHFNPAVSLGLTVAGRLPAKDLIPYWVAQVLGAIAAAAILYVIASGKDGFSAGGLASNGYGELSPGGYSMMAGLLIEIILTAFFIIIILGSTSSLAPAGFAPIAIGFGLTLIHLVSIPVTNTSVNPARSTGVALFADRAALSQLWLFWVAPLVGAVIGAIIWKGLLGRD | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
P60845 | MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGGHFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNGYGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
Q88F17 | MSLGKRMGAELIGTFWLVLGGCGSAVLAASSPLGIGVLGVAFAFGLTVLTMAFAIGHISGCHLNPAVSFGLVVGGRFPAKELLPYVIAQVIGAILAAGVIYLIASGKAGFELSAGLASNGYADHSPGGYTLGAGFVSEVVMTAMFLVVIMGATDARAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTGPALFVGGWALQQLWLFWVAPLIGAAIGGALYRGLAKEP | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
Q8EHC1 | MNMSQKMAAEFLGTLWLVLGGCGSAVLAAAFPEVGIGLLGVSLAFGLTVLTMAFAIGHISGCHLNPAVSFGLWAGGRFPTSELLPYIIAQVAGGIAGAGVLYLIASGQEGFSLAAGFASNGFGEHSPGGYSMISVMICEIVMTLFFLLVILGSTDERAPKGFAPIAIGLCLTLIHLISIPISNTSVNPARSTGPALFVGDWAVSQLWLFWAAPIIGAILAGVIYRYFNAAK | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
P73809 | MKKYIAEFIGTFWLVLGGCGSAVFAAFIAAPGGGNTNEFGLGYLGVALAFGLTVFTGAYALGHISGGHFNPAVSFGLWMGKRFPGSQLAPYIGAQVLGAIVASLFIFIVAQGGPNFSLDGSNPLATNGFGDHSPQGYGFLAALLIEFVLTFIFLIVILGVTDKTAPAGFAPAAIGLALTLIHLISIPITNTSVNPARSTGVALFCGNPALIGQLWLFWLAPIAGALLAGFVYHNVLEDLGRPEPEAE | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
P08202 | MTIFDNYEVWFVIGSQHLYGPETLRQVTQHAEHVVNALNTEAKLPCKLVLKPLGTTPDEITAICRDANYDDRCAGLVVWLHTFSPAKMWINGLTMLNKPLLQFHTQFNAALPWDSIDMDFMNLNQTAHGGREFGFIGARMRQQHAVVTGHWQDKQAHERIGSWMRQAVSKQDTRHLKVCRFGDNMREVAVTDGDKVAAQIKFGFSVNTWAVGDLVQVVNSISDGDVNALVDEYESCYTMTPATQIHGKKRQNVLEAARIELGMKRFLEQGGFHAFTTTFEDLHGLKQLPGLAVQRLMQQGYGFAGEGDWKTAALLRIMKV... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of L-arabinose to L-ribulose.
Catalytic Activity: beta-L-arabinopyranose = L-ribulose
Sequence Mass (Da): 56074
Sequence Length: 500
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabi... |
A5FKW3 | MIDISQKEVWFVVGSQELYGEETLRKVAEHSQIIAKGLDASSSIPVKVVYKDVVKSPSQILDVCLAANSAKNCIGIIAWMHTFSPAKMWIGGLNILKKPLCHLHTQYNAEIPWGSIDMDFMNLNQSAHGDREFGFIMSRLRKKRKVVVGHWEDQRVQKQLGIWSRVVLGWDELQNLKVARIGDNMREVAVTEGDKVEAQIRFGMSVNGYDSSDVTKHIEKVTDKQLADLLAVYESSYNLTDSLKEGGAQRSSLVEAAKIELGLRAFLEEGGFGAFTDTFENLGVWKQLPGIATQRLMADGYGFGGEGDWKTAAMVRALKV... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of L-arabinose to L-ribulose.
Catalytic Activity: beta-L-arabinopyranose = L-ribulose
Sequence Mass (Da): 55639
Sequence Length: 502
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabi... |
Q9S467 | MLSLRPYEFWFVTGSQHLYGEEALKQVEEHSMMIVNELNQDSVFPFPLVFKSVVTTPEEIRRVCLEANASEQCAGVITWMHTFSPAKMWIGGLLELRKPLLHLHTQFNRDIPWDSIDMDFMNLNQSAHGDREYGFIGARMGVARKVVVGHWEDPEVRERLAKWMRTAVAFAESRNLKVARFGDNMREVAVTEGDKVGAQIQFGWSVNGYGIGDLVQYIRDVSEQKVNELLDEYEELYDIVPAGRQEGPVRESIREQARIELGLKAFLQDGNFTAFTTTFEDLHGMKQLPGLAVQRLMAEGYGFGGEGDWKTAALVRLMKV... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of L-arabinose to L-ribulose. In vitro, converts D-galactose into D-tagatose.
Catalytic Activity: beta-L-arabinopyranose = L-ribulose
Sequence Mass (Da): 55957
Sequence Length: 496
Pathway: Carbohydrate degradation; L-arabinose degradation via... |
B0R9X5 | MSSESPESVDDSTKVQATAEWDPLQAVRMHLPGAETFVGIMDPEPNLFLNDFSLVDAQQEHLSLSQDLEAALPASNPIHYLHDDLANGNGMNALLSSRVNFDLSELGEDEQVNRRDKMWARLHELSPHTQIQAVLGNAEVIRHHSHSDEEVPGSNPDRWDTTSVQLEQPLTNMYFQRDQQFVTQNGVVLCSMKEDTRKPEVDIARASWEALDGDEFDVDIVADMSQVREHDVTEHVPERDDIQETEVLVEGGDFYPAGEFSLLGVSAKIPEGEAYPKHDIAEDDTEYVHRTTYAAGHRLLMDDAFGSEEVGLVRAPFEAA... | Function: Involved in the arginine deiminase pathway of fermentative arginine utilization.
Catalytic Activity: H2O + L-arginine = L-citrulline + NH4(+)
Sequence Mass (Da): 54706
Sequence Length: 486
Pathway: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2.
S... |
P07347 | MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQDENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV | Function: Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
Catalytic Activity: acety... |
P50166 | MDSSSYWSYDNIVPSFRLDGKLVIITGGSGGLSAVVSRALLAKGADIALIDMNLERTQQAARDVLQWGEEQMKGKHESPIGQVSAWSCNIGDAEAVELTFKAINEHHGKVASVLINTAGYAENFPAEEYPAKNAENIMKVNGLGSFYVSQAFARPLIQNNMTGSIILIGSMSGTIVNDPQPQCMYNMSKAGVIHLARSLACEWAKYNIRVNTLSPGYILTPLTRNVISGHTEMKTEWESKIPMKRMAEPKEFVGSILYLASDSASSYTTGHNLVVDGGYECW | Function: Catalyzes the NAD(+)-dependent oxidation of D-arabinitol at carbon 4 to produce D-ribulose.
Catalytic Activity: D-arabinitol + NAD(+) = D-ribulose + H(+) + NADH
Sequence Mass (Da): 30748
Sequence Length: 282
Pathway: Carbohydrate metabolism; D-arabinitol metabolism.
EC: 1.1.1.250
|
P0DW92 | MAQLVDEIVFQSGVKLHNRIVMAPMTIQSAFFDGGVTQEMINYYAARSGGAGAIIVESAFVENYGRAFPGALGIDTDSKIAGLTKLADAIKAKGSKAILQIYHAGRMANPEFNGGHQPISASPVAALRDNAETPLEMTKEQIEEMIERFGDAVNRAILAGFDGVEIHGANTYLIQQFFSPHSNRRNDKWGGNIERRTSFPLAVLAKTKQVAEQHNKSDFIIGYRFSPEEIEQPGIRFDDTMFLLDKLATHGLDYFHFSMGSWLRNSIVTPEDQEPLIDKYRKLQSESVAKVPVIGVGGIAQRKDAENALEQGYDMVSVGK... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the NADH-dependent reduction of acrylate to propanoate. The principal role of ARD in Vibrio seems to be the energy-saving detoxification of acrylate coming from the environment. May also use acrylate as the terminal electron acceptor for NADH regeneration at oxygen... |
P25628 | MTETKDLLQDEEFLKIRRLNSAEANKRHSVTYDNVILPQESMEVSPRSSTTSLVEPVESTEGVESTEAERVAGKQEQEEEYPVDAHMQKYLSHLKSKSRSRFHRKDASKYVSFFGDVSFDPRPTLLDSAINVPFQTTFKGPVLEKQLKNLQLTKTKTKATVKTTVKTTEKTDKADAPPGEKLESNFSGIYVFAWMFLGWIAIRCCTDYYASYGSAWNKLEIVQYMTTDLFTIAMLDLAMFLCTFFVVFVHWLVKKRIINWKWTGFVAVSIFELAFIPVTFPIYVYYFDFNWVTRIFLFLHSVVFVMKSHSFAFYNGYLWD... | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Catalytic Activity: an acyl-CoA + lanosterol = CoA + lanosteryl ester
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71613
Sequence Length: 610
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
P84285 | MGRTNTSDQLNAISDKNTKRKSLALDNEYHNNSSSEDDSSKIELSYTIPDNNNIISQETTTSVEDVLSLSSAPQNELRLRKQKSNNQDSPVDLNGVIVDVSKREKIFLKRKRQIDNKHGSDKSKYLSRFNDITFKAKSSTIFESDEFYKTDFFGMYVLFWLATAFAMVNNLIHTYFENSTPILQWTVVKVFKRDLFKVGLVDLAMYLSTYFAFFVQYACKNGYLSWKKVGWWLQAAFDGLFLFFWLWIASEYCLDFPWIAKVFLVLHSLVFIMKMHSYAFYNGYLWSIYKEGLYSEKYLDKLTNGKVTLPKGHTKNETEK... | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71347
Sequence Length: 609
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
P53629 | MDKKKDLLENEQFLRIQKLNAADAGKRQSITVDDEGELYGLDTSGNSPANEHTATTITQNHSVVASNGDVAFIPGTATEGNTEIVTEEVIETDDNMFKTHVKTLSSKEKARYRQGSSNFISYFDDMSFEHRPSILDGSVNEPFKTKFVGPTLEKEIRRREKELMAMRKNLHHRKSSPDAVDSVGKNDGAAPTTVPTAATSETVVTVETTIISSNFSGLYVAFWMAIAFGAVKALIDYYYQHNGSFKDSEILKFMTTNLFTVASVDLLMYLSTYFVVGIQYLCKWGVLKWGTTGWIFTSIYEFLFVIFYMYLTENILKLHW... | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Catalytic Activity: an acyl-CoA + ergosterol = CoA + ergosteryl ester
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74023
Sequence Length: 642
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
P15514 | MRAPLLPPAPVVLSLLILGSGHYAAGLDLNDTYSGKREPFSGDHSADGFEVTSRSEMSSGSEISPVSEMPSSSEPSSGADYDYSEEYDNEPQIPGYIVDDSVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEFQNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMKTHSMIDSSLSKIALAAIAAFMSAVILTAVAVITVQLRRQYVRKYEGEAEERKKLRQENGNVHAIA | Function: Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27895
Sequence Length: 252
Subcellular Location: Membrane
|
Q10269 | MTDTPRILITPSPLSDISTTINKPNVHPSMSLLKALPECRLVVKSKGDKNNANVVEFPLDRHKQLLIAGKVYHDYKFKPRKSIFDRVTDPNYFAKSEFRGFYVLFWLSMAAWVLQLYARSYWQRDTLLGLPLARQVFRQFFVLFSSDFLMICLSFFSYGLQVCIEKNMIRWANLGYTIQTLWQGFYMVLAVYWVKHRDFPIVQCVFFTLHCAVLIMKQFSYSHHMGYISEIRILHNEYEKLLKFVRECLNSTEKDEKYTFELTFPNKPAETISTLQAEEIVALTAKYLSRQMRSEVGNVVYPDNINFFNYVDYLLVPSLV... | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63098
Sequence Length: 537
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
Q9C7I9 | METGNVVNAQPELSGIIDGSKSYMYEQLWKLCAGPLCDIPKLGENVYYFPQGNIELVDASTREELNELQPICDLPSKLQCRVIAIHLKVENNSDETYAEITLMPDTTQVVIPTQSENQFRPLVNSFTKVLTASDTSAYGGFFVPKKHAIECLPPLPLPAQELLAKDLHGNQWRFRHSYRGTPQRHSLTTGWNEFTTSKKLVKGDVIVFVRGETGELRVGIRRARHQQGNIPSSIVSIDCMRHGVIASAKHALDNQCIFIVVYKPSIRSSQFIVSYDKFLDAMNNKFIVGSRFTMRFEGDDFSERRYFGTIIGVNDFSPHW... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate e... |
Q9AV47 | MKEVGEVEEVRCLDPQLWHACAGGMVQMPAPRSRVYYFAQGHAEHADGGGGAAAAAAELGPRALPPLVLCRVEGVQFLADRDSDEVYAKIRLAPVAPGEAEFREPDELCPLGAAGDAAEPSPEKPTSFAKTLTQSDANNGGGFSVPRYCAETIFPKLDYRADPPVQTVLAKDVHGVVWKFRHIYRGTPRRHLLTTGWSTFVNQKKLVAGDSIVFLRTRHGELCVGIRRAKRMACGGMECMSGWNAPGYGGGGFSAFLKEEESKLMKGHGGGGYMKGKGKVRMADVVEAASLASSGQPFEVAYYPRASTPDFVVKAASVQA... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 75610
Sequence Length: 698
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur throu... |
Q2R3F5 | MATAEVGGGGGEGDAAAAAVARAGGGGGGGGGGGEDALFTELWSACAGPLVTVPRVGEKVFYFPQGHIEQVEASTNQVGEQRMQLYNLPWKILCEVMNVELKAEPDTDEVYAQLTLLPESKQQEDNGSTEEEVPSAPAAGHVRPRVHSFCKTLTASDTSTHGGFSVLRRHADECLPPLDMSRQPPTQELVAKDLHGVEWRFRHIFRGQPRRHLLQSGWSVFVSAKRLVAGDAFIFLRGENGELRVGVRRAMRQQTNVPSSVISSHSMHLGVLATAWHAVNTGTMFTVYYKPRTSPAEFVVPYDRYMESLKQNYSIGMRFK... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 93984
Sequence Length: 853
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur throu... |
Q2QQX6 | MAAAATAAASPVEGLTGGGGGGGGGVDGLFVELWRACAGPLVTVPAVGERVFYLPQGHIEQVEASTNQVAEQQGAPLYNLPWKIPCKVMNVELKAEPDTDEVYAQLTLLPEKQQDGNGSGNGNVSKDKVEEEEVVPPAATERPRVHSFCKTLTASDTSTHGGFSVLRRHADECLPPLDMSQHPPTQELVAKDLHGVEWRFRHIFRGQPRRHLLQSGWSVFVSAKRLVAGDAFIFLRGENGELRVGVRRAMRQQANIPSSVISSHSMHLGVLATAWHAVNTGTMFTVYYKPRTSPSEFVVPRDLYKESLKRNHSIGMRFKM... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 92307
Sequence Length: 841
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur throu... |
C1F4F1 | MKYVVKLGGAALENPEIFMACARAVADLVKDGHQVALVHGGGVQLTRTLKQLGKQSEFIAGLRVTDAETRDAALMVLSGRVNKSLVAALGSLGQAAMGLSGGDGLIFRARKKRTVPDLGFVGEIVASDPRWLEAIWKMNAVPVISSIALGFDGEYYNVNADEMAAACAAACRADALVFLTDVPGVRGADGTIMRWLTVDQIPVLSQTEVISGGMLPKLGACREALLNGVKRVRILPAEAAHVLPDLCSARVTDGTEVMAS | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 27327
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
A3MYW5 | MLQNEVENFANLLEQATVYLAPYQEKIIVVKYGGNAMINEDRKKLVMQDILLLNQLGVKVVLVHGGGPEISQGVKLLGKEPQFINGLRVTDQDTINVVLQMLAGKVNKSLVALLKGKGVGLCGIDANMLQCEKLQAEVDYGFVGEIVKVNTQLLELALSANLIPVISTVGVDDQGVAYNINADTVASEIAMALGAAKLVSMTDIAGLLRDRFDESTLIPEVEVSEVQGLIDQGIIAGGMIPKIACCTDFINAGGIEANIIDGRVPHAILVSLFGGKNGTLFYKK | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 30318
Sequence Length: 284
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
B2URE3 | MDSKITRLIEQASVIVGALPYLQAYRDKTFLIKFGGSAMDDARLVKKLMRDIVLLEVLGFNPVIVHGGGKAISKAMAEAGLEARFVNGLRVTTPEAISIVERTLSGTINPGLVQMFRDYGGKGVGIPGTEIFVGERIHEKDEQGNPIDIGEVGNVIGCLTERITEALELQITPIVSPLAKELGTHKPLNVNADLAAAALAKELKPVKLIYISDVPGIMKDPSDPSTLIKSVTRTEALDLIKDGTVSGGMIPKIHSAIDALNAGVRKVHFIDGRLPHTLLLEIFTPDGIGTEIIREQR | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 31952
Sequence Length: 297
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q72C18 | MDCVENARLQSKVLIESLPYLRQFHGETVVIKYGGHAMKDEALKKAFALNVALLKLVGINPVIVHGGGPQIGKMLEQLNIQSHFREGLRVTDDATMDVVEMVLVGKVNKEIVNQMNLAGAKAVGLSGKDGMLIRARKMEMVISKEAQAPEIIDLGKVGEVMGVNTTLLRSLERDGFVPVIAPVGVDDNGETYNINADAVAGAVAAALKAKRLLLLTDVAGILDHDKKLIRSVNMREAVNLFSDGTLTGGMIPKVKCCLEALEEGVEKAMIIDGRTENCILLELLTDKGVGTEIVSDRAAQAACNCVLR | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 33080
Sequence Length: 308
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
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