ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5ACZ2 | MVSLQQLTISILLLFTASVQSLDINVDDKDSICSAAKYVVQGIWNYYEGLKYGGTVGMFAPPNYWWNAGEAFGGLVDFYTYCQSDNSTLEKLIYNGMYHQAGENYNYIPSNQSMTEGNDDQGVWGMAIMEAVERNFTEPESHSWLEMVQAVFNTMNARWDADNCGGGLRWQIFTWNSGYDYKNSISNGCLFHLAARLARYTGNSSVYVDTAEKVWKWMEDVGFLTEEDNGDVRIYDGAKITNNCSSVTDLRWSYTYGVFMAGCAYLYNFTGDDVWLTRTNEIVQASLSYFFANKIMQETTCQPQNKCNNDQRSFRCLFSR... | Function: Required for normal synthesis of the cell wall and alkaline pH-induced hypha formation.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mann... |
Q05031 | MIVNISAKMILSICFTFLSFFKATHAMDLDTTSKTSICDATALIQGGMLDYYEGTRYGGTVGMFQSPYYWWHAGEAFGGMLENWFLCENDTYQELLYDALLAQTGSNYDYIPSNQTMVEGNDDQGIWGITVMGAVERNFTDPGDGKPGWLAMVQAVFNTMYSRWDSEHCGGGLRWQIFTWNSGYNYKNTVSNACLFQIAARLGRYTGNTTYLEVAEQVFDWLVDVGYVVLNDTANVFDGAEIDTNCTDITKIEWTYNHGIVLGGLAYMYNATNGTGEWETSLTKILNGAKSYFFKDSIMYESACQDYGTCNTDQRTFKSI... | Function: Required for normal synthesis of the cell wall.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Catalytic Activity: Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Sequence Mass (Da): 50541
Sequence Length: 458
Subcellular Location: Cell membrane
EC: 3.2.1.101
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Q5AFI4 | MEKLSINNNNNNRRYQSRRFDGITIIRIVVLVFIVTVSTYFVNSYTCNQPHHNHSTRPSHYLPINGTHGLMNNDDSLHNKGAIGHYNTTVSLERRADENNSTTNGLFPSTSSSTFIFTPSSSSSSTFQQSRSSPQTTSTSSFVATTSSFQQETSQTSIPDTTTDFSFSSFSEAPTTSTTSSTSEFSSTPQETSNTVTSTSSTSTSSSSSPTSSPATTSASQHVTTFSSVDNGKTIVVTRTSVISSSPTASNSNNNKNNDNGGGLSHTNRIVVGVVVGVGGSILIGLLAVLFYLRKRNNRDYEGGWTFWRKNEKLGSDEFF... | Function: Cell-surface associated glycoprotein that acts as a plasma membrane receptor-type protein which senses the presence of matrix. Binds to calmodulin in response to environmental conditions and initiates a signaling cascade that activates CEK1, thus promoting invasive filamentation. Involved in the maintenance o... |
P37530 | MNTAPFIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSDHFLKKGQPVIADYHIYKNVIFAERTLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQLISDYEVAIKQLQEADPELTVLTVDGDSKDFVLNKSDFERIAAHVKELIV | Function: Plays an essential role in generating the deoxyribonucleotide precursors dGTP for DNA metabolism. Highly specific toward deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity is observed with guanosine. UTP is slightly more efficient as phosphate donor than CTP, ATP and GTP.
Catalytic Activity... |
Q54UT2 | MFRRSLMFMISNNKNTNMVSSINTTNKVNNFSKIIILEGNISAGKTYLSSKLGDLLGYKVFLEPTATNPYLSLFYKEPSKYALIMQKWLLNQRYNTFLNALQYSLENEQGVILDRSVYSDWVFAENCRSEGLISAEGFKEYNSIRDRFLSNIPIPNVTLFLDVDPKQCLQRIQNRKRDCEQSIPLSYLSGLDNCYKKFLIEMKSKGSNVIILDWNNFGDINLVLNEINNDNFNNFNNSNNSKFNDVNYKKQQLISDIENEKNNLKEMKFFLNENNNNNNQEKIKS | Function: Purine-specific deoxyribonucleoside kinase that phosphorylates preferentially deoxyguanosine, as part of the deoxyribonucleotide salvage pathway.
Catalytic Activity: 2'-deoxyguanosine + ATP = ADP + dGMP + H(+)
Sequence Mass (Da): 33193
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 2.7.1.113
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Q8NCG7 | MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDL... | Function: Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production . ... |
Q6BF16 | MQWQTKLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEQSIPAIVDAYGDKALIGAGTVLKPEQVDALARMGCQLIVTPNIHSEVIRRAVGYGMTVCPGCATATEAFTALEAGAQALKIFPSSAFGPQYIKALKAVLPSDIAVFAVGGVTPENLAQWIDAGCAGAGLGSDLYRAGQSVERTAQQAAAFVKAYREAVQ | Function: Involved in the degradation of galactose via the DeLey-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophil... |
Q92RN8 | MDRIPLPPMERPLIAILRGLKPEEAEGVVGALIETGFTAIEIPLNSPDPFRSIETAVKMAPAGCLIGAGTVLTTAQVERLADVGGRLMVSPNVEPAVIRLAATKGMVTMPGVFTPTEALAAAAAGASGLKFFPASVLGPSGITAIRAVLPGDLEIAAVGGVSEVNFADYAAIGIRSFGLGSSLYKPGMSAGDVRQRAIATLAAYDAVYGGQQ | Function: Involved in the degradation of galactose via the DeLey-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate (By similarity).
Catalytic Activity: 2-dehydro-3-deoxy-6-phospho-D-galactonate = ... |
P09788 | MSEQNNAVLPKGVTQGEFNKAVQKFRALLGDDNVLVESDQLVPYNKIMMPVENAAHAPSAAVTATTVEQVQGVVKICNEHKIPIWTISTGRNFGYGSAAPVQRGQVILDLKKMNKIIKIDPEMCYALVEPGVTFGQMYDYIQENNLPVMLSFSAPSAIAGPVGNTMDRGVGYTPYGEHFMMQCGMEVVLANGDVYRTGMGGVPGSNTWQIFKWGYGPTLDGMFTQANYGICTKMGFWLMPKPPVFKPFEVIFEDEADIVEIVDALRPLRMSNTIPNSVVIASTLWEAGSAHLTRAQYTTEPGHTPDSVIKQMQKDTGMGA... | Cofactor: Binds 1 FAD covalently per subunit.
Function: Catalyzes the azurin dependent hydroxylation of the methyl group of 4-methylphenol to form 4-hydroxybenzaldehyde.
Catalytic Activity: 4-methylphenol + H2O + 4 oxidized [azurin] = 4-hydroxybenzaldehyde + 4 H(+) + 4 reduced [azurin]
Sequence Mass (Da): 57945
Sequenc... |
Q2FYJ2 | MLVAVVKELKQGEGRVACTPENVRKLTDAGHKVIVEKNAGIGSGFSNDMYEKEGAKIVTHEQAWEADLVIKVKEPHESEYQYFKKNQIIWGFLHLASSKEIVEKMQEVGVTAISGETIIKNGKAELLAPMSAIAGQRSAIMGAYYSEAQHGGQGTLVTGVHENVDIPGSTYVIFGGGVAATNAANVALGLNAKVIIIELNDDRIKYLEDMYAEKDVTVVKSTPENLAEQIKKADVFISTILISGAKPPKLVTREMVKSMKKGSVLIDIAIDQGGTIETIRPTTISDPVYEEEGVIHYGVPNQPGAVPRTSTMALAQGNID... | Function: May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer.
Catalytic Activity: H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate
Sequence Mass (Da): 40225
Sequence Length: 372
Pathway: Amino-acid degradation; L-alanine degradation via dehydrogenase pat... |
Q2THW0 | MPSGSMSGGVSGPTSPPHPTVPSRPLRPSRYVPVSAATAFLVGSTTLFFCFTCPWLSEQFSVAVPIYNGVMFMFVLANFCMATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIRGIQVRMKWCSTCRFYRPPRCSHCSVCDNCVEDFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFGFGLLFILYHTQQLDRVHSAVTMAVMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTNGCLRNVSHVLCSSQAPRYLGRKRKAQTVSVQPPFLRPQLTEAQLAAKVLDNGIQGDLHRSKSSLEMMES... | Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Ma... |
E7FBS9 | MPVGLSVGGALGDPSPSRPFRPSRYVPVSAATAFLVGATTLFLCFTCPWLSEKFSSFIPLYNVVVFLFTLANFCMATFMDPGVFPRAEEDEDKEDDFRAPLYKTVEVRGIQVRMKWCSTCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTVHIMDVFGFSLLYILHHTKQLDLVQSGVTMAVMCVAGLFFVPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTHGCFKNIAHVLCSSQAPRYLGRLRKPQSVQVQPPFLRPPLSEAQLAAKVLDNGIQQSKSSLEIMESQSTDADPPPP... | Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Ma... |
Q9UBM7 | MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTL... | Function: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADP... |
Q5UQI4 | MNSYQTNTATSWGRNHIPTLLDNLTTAAMFMFCPFIILVFYLITYGEYLGSIGDFYLDIINGDWQTIWSNIPSFKINVLGACLLWIVFQLILSKLPDTIHRFVPHYVGGIKAGHITPAGNLVYYNINGLQAFIITHVLVIMSCYYGLFSPTIIMDNWGSIFWSVNIIGYLITFLAYFKALTFSSHPSDNKFTGKLFYDIVMGIEFNPEIFGTDLKLFFNGRPGIIAWNLINLSCAMKQYENFGYVSNSMILVIILQLIYIVDFFYNENWYVHTVDIAHDHFGWMLAWGDTVWLPFGYTLQAGYLMNNPIDLSTGFFNLVF... | Function: Production of cholesterol by reduction of C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC).
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51692
Sequence Length: 447
Pathway: Steroid... |
Q6P4M0 | MGERRRANASRGDKKVANGEKPHVGQWGRAWEVDYFSLAAVLFLLAFAPLIVYYFVMSCDQYQCALTAPVLDLYWGKAQLSDIWDKTPALTWGAAKIYIVWVSFQVFLYMLVPDILHKFVPGYEGGVQEGARTPAGLINKYQVNGLQAWTITHLLWFANAYHFHWFSPTIIIDNWVPLLWCANLLGYSVATFALLKAYFFPTNAHDCKFTGNFFYDYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSYAAKQQELYGQVTNSMILVNVLQAIYVVDFFWNESWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQG... | Function: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADP... |
Q86SQ9 | MSWIKEGELSLWERFCANIIKAGPMPKHIAFIMDGNRRYAKKCQVERQEGHSQGFNKLAETLRWCLNLGILEVTVYAFSIENFKRSKSEVDGLMDLARQKFSRLMEEKEKLQKHGVCIRVLGDLHLLPLDLQELIAQAVQATKNYNKCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPSDISESLLDKCLYTNRSPHPDILIRTSGEVRLSDFLLWQTSHSCLVFQPVLWPEYTFWNLFEAILQFQMNHSVLQKARDMYAEERKRQQLERDQATVTEQLLREGLQASGDAQLRRTRLHKLSARREERVQGFLQALELK... | Cofactor: Binds 1 magnesium ion per subunit.
Function: With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyropho... |
F1QLP1 | MEDFAVSFWIYIGVMSIFVGGAVKKFLAFNIGAMPSVVVWLGATLLVERLCALCMPAVLARLVLCVCCWLYFTWATPKPSLPVEDKAVFITGCDSGFGNATAKKLDAMGFEVFATVLNLEGEGAKHLRKVCSSRLTLLQVDITQPQQVQQALLDTKAKLGIRDLWGLVNNAGWCVNIGDAELSLMSNYRGCMEVNFFGTVTVTRTFLPLLRQSKGRIVTISSPSGEHPFPCLASYGASKAALNLFINTLRHELDPWGVKVSTILPSAYKTGQSSNAEYWEKQYKSLLQGLSPNLLEEYGEEYLLETKELFQNYAKTANED... | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) . Cortisol is the primary glucocorticoid in teleosts and is released to increase glucose bioav... |
P80365 | MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPGAIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELSPVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVALLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYIEHLHGQFLHSLRLAMSDLTP... | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) . Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active gluco... |
P51976 | MERWPWPSGGAWLLVAARALIQLLRADLRLGRPLLAALALLAALDWLCQSLLPPSAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDAMGFTVLATVLEMNGPGALELRACCSPRLKLLQMDLTKPADISRALEFTKAHTTSTGLWGLVNNAGHNDVVADVELSPVATFRNCMEVNFFGALELTKGLLPLLHHSRGRIVTLGSPAGEMPYPCLAAYGTSKAAMALLMDAFSCELLPWGVKVSVIQPGCFKTESVSNVSHWEQRKQLLLANLPGELRQAYGEDYIEHLHREFLHSLRLALPDLSP... | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as corticosterone, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as 11-dehydrocorticosterone, in the presence of NAD(+) . Functions as a dehydrogenase (oxidase), thereby decreasing the concentr... |
P50233 | MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALVVLAGAGWIALSRLARPPRLPVATRAVLITGCDTGFGKETAKKLDAMGFTVLATVLDLNGPGALELRARCSPRLKLLQMDLTKPEDISRVLEITKAHTASTGLWGLVNNAGLNMVVADVELSPVVTFRECMEVNFFGALELTKGLLPLLRHSRGRIVTVGSPAGDMPYPCLAAYGTSKAAIALLMDTFSCELLPWGIKVSIIQPGCFKTEAVTNVNLWEKRKQLLLANLPRELLQAYGEDYIEHLHGQFLNSLRMALPDLSP... | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as corticosterone, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as 11-dehydrocorticosterone, in the presence of NAD(+) . Functions as a dehydrogenase (oxidase), thereby decreasing the concentr... |
Q59660 | MRYITPRKAAEGLGSAHEGTQHHWAMTVSAVALTVLTPLFMIVVARAIGLSQEQLLAYFGRPFPALITALFVIVGMVHFIKGTRIMIDDYFQGGTRKAAIIFSVIFGWAVIAAAVYALARMGLGAIVVL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13934
Sequence Length: 129
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
A5GZW8 | MATLWRLSVLCGARGGGALVLRTSVVRPAHVSAFLQDRHTPGWCGVQHIHLSPSHQASSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGIGQVVTDYVRGDALQKVAKAGLLALSAFTFAGLCYFNYHDVGICKAVAMLWKL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17005
Sequence Le... |
P80479 | MYKTLLAQVFFHSIAKKKLYFFWLPRLFSLLLVPGFLFDIEILFLFHPIILLHASLGLSVIIEDYIHIETIKFQYLSLIKLLLVLLINLNILYLL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11265
Sequence Length: 95
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitoch... |
P80482 | MTEKLLHFIRTKSGSMHWWLQRFLAILLAPIILYLLFDVAIYIGQQSDPTVMMFLNRIFNHNSIFIFITSVILIWHVRGGMEVIIEDYVHGEKTRIVSIFLIRVIAIEIMEYLYKCSIIF | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14222
Sequence Length: 120
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitoc... |
P41086 | MIYDFKAEIIKAKNSSFSKSGSHHWLLQRVTGVILALCSFWLIYFMFTNKNNDINIIMWEFKKPFNIVILLITVTISLYHSVLGMRVVIEDYINCHKLRNTLIIIVKLFCILTIVSFVVAIFYSG | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14555
Sequence Length: 125
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
Q9P7X0 | MLQTRLGLGALRQGRLLFAVKSFSTTSVAKIFPPPPQTIKGTVNDAAVFPHHSKLHGSYHWDFERIIAIAMVPQVMIPLFTGTSHPLMDAALACTLITHAHLGFESCVIDYFPARRFKKLSPLMHWILRGCTVLTLIGVYEFNTNDIGLTEGIKKLWKS | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17744
Sequence Le... |
Q08717 | MAETEKMKYGSLNRFAQAVTGLFLLFFLGVHLYVAHIDFGHPVAFFSSVINQLHNPWWLAFFLIFVYIITYHGINGLNHIVADTSISEKAKRNIGIALMVIYVITIIYGTILALLVARMTVPT | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13874
Sequence Length: 123
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
Q6P355 | MATLLRVSSLCRANRASAFKSLLIRPVPCLTQDHHMVQTSQIHTSPNHHAGSKAASMHWTSERALSVALLGLLPAAYLYPGAAMDYSLAAALTLHGHWGLGQVVTDYVHGDAKIKMANTSLFALSALTFAGLCYFNYHDVGICKAVSMLWSL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16424
Sequence Le... |
P37298 | MMLPRSMKFMTGRRIFHTATVRAFQSTAKKSLTIPFLPVLPQKPGGVRGTPNDAYVPPPENKLEGSYHWYMEKIFALSVVPLATTAMLTTGPLSTAADSFFSVMLLGYCYMEFNSCITDYISERVYGVWHKYAMYMLGLGSAVSLFGIYKLETENDGVVGLVKSLWDSSEKDNSQKIEAKK | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1... |
P17874 | XEEFDYDLVIIGAG | Function: Soluble hydrogenase catalyzes both production and consumption of hydrogen from suitable artificial electron donors or acceptors. This subunit (50 kDa) is required for hydrogen production with reduced methyl-viologen.
Sequence Mass (Da): 1552
Sequence Length: 14
Subcellular Location: Cytoplasm
EC: 1.12.-.-
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Q8Q051 | MHHNVFTNTPTIPIDVKDRSVSELMDGMLRTGFQGRKLAESVQAWSNMLKEKDTTVLMGLSGAMVPAGMRRVISYLIRERMIDCLVSTGANLFHDSHEALGRKHYVGSHLANDEKLFEHGVDRIYDVFAVEEEFRNADNLIADFAEEIGEISCSSREFMYLLGKELVRRGAAEDSIVVSAYRHNVPIFVPALSDSSIGIGLTIARRRGLKLEIDQIKDVDEITQIVEKSGHTGVVYVGGGVPKNFIQQTEVIASILGMDVPGHEYAIQYTSDSPHWGGLSGCTFDEAVSWGKVAAQAKKVQVFVDATIALPIVAHALHEK... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
Q38BX0 | MAELAKSAVLVSSCTDDLLGDAKQVVVGPNQEDLHSAEAVLNRYSTVGFQASNLARAFSICEMMLTPQSPSPSLMPTEGDQASESPVMVQPTLFVGVTANLFGTGCREAIRFLCTECVPLPNGVEPATPLDDMAGISCDGTGALKPSPCDSRALIHVLVVSGGAMEHDIRRACESYKLSRDGAEEEGEQFHHPVERDRSRSKGTDCHFGNVRYNSSGVASRNLFSCVMRCLVKRLAEAQRKEKANREAAPIPEAYYDVCSWAITPSTLWYMAGLWMADIFTEALQETGEVTDEKVASEEGLKRAKSTVLYWAARNGVPIF... | Cofactor: The binding sites for NAD(+) are contained in the regulatory subunit DHSp.
Function: In association with the non-catalytic regulatory subunit DHSp, catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a sp... |
Q6EWQ6 | MEGPQEREVPAAALAAVLKHSSALPFETAQVRGYDFNRGVDYRALLEAFSTTGFQATNFGRAVQQVNAMIEKKLEPLSEDEDQHADLTQSRRPLTGCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDFIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNDNYCKFEDWLMPILDQMVLEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVLSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLKLINTQAIFAKRTGMIILGGGMVKHHIANANLMRNGADYAVYINTAQEFDGSDSGAR... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translation... |
Q6BJH5 | MSGSDKLPGLASDAVLKQSIPVPDSFVEIKGIDYSKDSAYNMKAVDLIESMKNMGFQASSVSQACEIINGMRSWRGKHIDSLPEHERTGEFDDEGYQKSTIFMGYTSNLISSGLRDTLRFLVQHKMVSAIVSSAGGIEEDLIKVLAPTYMGEFSLPGKGLRDQGMNRIGNLLVPNDNYCKFEEWIVPILDKCLEEQEEGMKKMGSDGLNADSPACWTPSKLINRLGKEINDESSVLYWAHKNDIPVFCPALTDGSIGDMLFFHTFKASPQQIRLDIVADIRKLNSMSMAASNAGMILLGGGLIKHHICNACLMRNGADYA... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
Q9AXQ8 | MEDANHDSVASAHSAAFKKSENLEGKSVKIEGYDFNQGVNYSKLLQSFASNGFQASNLGDAIEVVNHMLDWSLADEAPVDDCSEEERDPKFRESVKCKVFLGFTSNLISSGVRDTIRYLVQHHMVDVIVTTTGGIEEDLIKGRSIKCLAPTFKGDFALPGAQLRSKGLNRIGNLLVPNDNYCKFEDWIIPILDKMLEEQISEKILWTPSKLIGRLGREINDESSYLYWAFKNNIPVFCPGLTDGSLGDMLYFHSFRNPGLIVDVVQDIRAVNGEAVHAAPRKTGMIILGGGLPKHHICNANMMRNGADYAVFINTAEEFD... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. Also able to produce homospermidine from putre... |
Q54MQ7 | MSTNTTTTNATPELAKESVFFQSNHEDLKNRPKVRGYDFNEGVDFSKLFETYKTIGYQASAVGEAIDEINRMISWRLVDEPLKEGEDDDEERKVTRCKIFLGYTSNLVSSGVREIIRYLVQHSMVDVIVSTAGGVEEDFIKCLAPTYMGEFHLEGEKLRRKGLNRIGNLLVPNDNYCKFEDWIMPILDQMVEEQKTKGTVWTPSRVINRLGKEINHEDSIYYWAWKNDIPVYSPALTDGSIGDMMYFHSYNTPGLVLDIISDIRAINNHAVYSKKSGMIILGGGVIKHHICNANLFRNGADYSVFVNTGNEFDGSDSGAR... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translation... |
Q9VSF4 | MSTEPSVAKDAVLKRSEALAENTPQVSGYDFNEGLDYSKLFESYVNTGFQATNLGLAIREINRMLDCRDQPLEADQIDSHETDDFIRRRSKCTVFLGYTSNLVSSGLRETIRFLAEHRMIDCIVTTAGGVEEDFIKCLAPTFMGSFELSGRDLRERGINRIGNLLVPNDNYCKFEDWVMPLLDEMLEEQKSQGTIWSPSKIIHRLGERIGDPSSIYYWAAKNQIPVFCPALTDGSLGDMMYFHSFRQPGLVVDILSDLRRLNTMAVKAVNSGMIIVGGGVIKHHICNANLMRNGADYSVFINTASEFDGSDSGARPDEAI... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
Q8SQN2 | MDRPQNVKDLARKVKDNLSFSREVRGMDFEKEWDFMAIMRSFETMGFQGSNLYRAVEEIERMKNSKIFFGCTSNIISSGLRDVIATLVKRRHVHVLVITGGGIEEDIIKAFKPTFCADFRLDGAELRDNGLNRIGNLVIPSENYEHLESWLNNIVNDITEGYTAERPRILTPSSFIRILGERIDDESSILYWAAKNDIPVYSPAVVDGSLGDILSFHPRRKMLKLDIVEDVYRINCETIFCGETAAIILGCGVVKHHILNANLFKNGLEHCVLINNAQEFDGSDAGASLDEAVSWGKVKPGTRGVKVFGDATILFPLLVG... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
B0R5L2 | MTGDDADETHENVVPGSDEDLDTPDVRGYDFSGEFDFFELLDSYATTGFQASHLADAVDITREMREDDATIYLTLTSNIVSSGLREVVAHLVRENYVDVIITTSGSLTEDIIKTAKPFKMGEWDVDEAALREEGINRLGNIFVPSDRYVWLEEYLYDFFEEFFADQKVRTPTAFARELGATLDDEDSILKNAADNDIPVFCPALTDAEIGNFLYYYRQGYDSEVGIEILDDYDALIEEGLLADTTGLICVGAGVPKHHAIMTNLFRGGADYAVYISTGMEGDGSLSGAPPEEAVSWGKIKDEDAEPNYALIEAEATLVFP... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
P49366 | MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGAR... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue . This is the first step of the post-translatio... |
O60074 | MSNLEASLFQLKFAAKSLNKQSLKAAKEERAEREKVKKAITKGNSEIARIYASNAIRKQQESLNLLKLSSRIDAVSSRLQTAVTMRAVSGNMAGVVRGMDRAMKTMNLEMISQVMDKFEAQFDDVNVQTGYMNKAMGSVTAVDTPQEDVDLLMQTVADEAGLEFNQNMNNNLSVPAASVPTPAAPVEDDNLQERLRALRS | Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole (By similarity).
Location Topo... |
P69771 | MSRNSAAGLENTLFQLKFTSKQLQKQANKASKEEKQETNKLKRALNENEDISRIYASNAIRKKNERLQLLKLASRVDSVASRVQTAVTMRQVSASMGQVCKGMDKALQNMNLQQITMIMDKFEQQFEDLDTSVNVYEDMGVNSDAMLVDNDKVDELMSKVADENGMELKQSAKLDNVPEIKAKEVNVDDEKEDKLAQRLRALRG | Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripheral... |
O14177 | MGLTSWLFGGGKSPQEQLRAHQRSLGRAERELDRERTKLDQRERALIQEIKGSAKAGNTGAARIQARDLMRLRNSRKKMMNAKTQLQAISLRLQTMRTSEQMMQSMRGATRLLTGMNKSMNIPAMARITQQFERENEIMEQRQEMIDENMDDALEEDDEEEADELVNKVLDEIGVDLSQGLPDAATQIGTVPELKTEDNLQARLDELAKR | Function: Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo ... |
P36108 | MSLFEWVFGKNVTPQERLKKNQRALERTQRELEREKRKLELQDKKLVSEIKKSAKNGQVAAAKVQAKDLVRTRNYIQKFDNMKAQLQAISLRIQAVRSSDQMTRSMSEATGLLAGMNRTMNLPQLQRISMEFEKQSDLMGQRQEFMDEAIDNVMGDEVDEDEEADEIVNKVLDEIGVDLNSQLQSTPQNLVSNAPIAETAMGIPEPIGAGSEFHGNPDDDLQARLNTLKKQT | Function: Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo ... |
A7MAQ2 | MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI | Function: Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities . Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc an... |
Q9LXV3 | MASLALSGSCSLAFPLKSRSLSLPRPPSSSLNLTKPLRSLDSRFSLLKSPLPVSLRRRSSTLVKASSTVASASSSPTPPLVPAPVPWQGAAIKPLLASIATGLILWFVPVPEGVTRNAWQLLAIFLATIVGIITQPLPLGAVALMGLGASVLTKTLTFAAAFSAFGDPIPWLIALAFFFARGFIKTGLGNRVAYQFVRLFGSSSLGLGYSLVFSEALLAPAIPSVSARAGGIFLPLVKSLCVACGSNVGDGTEHRLGSWLMLTCFQTSVISSSMFLTAMAANPLSANLAFNTIKQTIGWTDWAKAAIVPGLVSLIVVPFL... | Function: 2-oxoglutarate/malate translocator involved with DIT2-1 in primary ammonia assimilation and in the re-assimilation of ammonia generated by the photorespiratory pathway. Imports 2-oxoglutarate into plastids as precursor for ammonia assimilation. 2-oxoglutarate is converted to glutamate, the end product of ammo... |
Q90839 | MRRGEGPAPRRRWLLLLAVLAALCCAAAGSGGRRRAASLGEMLREVEALMEDTQHKLRNAVQEMEAEEEGAKKLSEVNFENLPPTYHNESNTETRIGNKTVQTHQEIDKVTDNRTGSTIFSETIITSIKGGENKRNHECIIDEDCETGKYCQFSTFEYKCQPCKTQHTHCSRDVECCGDQLCVWGECRKATSRGENGTICENQHDCNPGTCCAFQKELLFPVCTPLPEEGEPCHDPSNRLLNLITWELEPDGVLERCPCASGLICQPQSSHSTTSVCELSSNETRKNEKEDPLNMDEMPFISLIPRDILSDYEESSVIQE... | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero... |
Q9UBP4 | MQRLGATLLCLLLAAAVPTAPAPAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAAKASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVGDEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHCTKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLITWELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVGSFMEEVRQE... | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero... |
Q9QUN9 | MQRLGGILLCTLLAAAVPTAPAPSPTVTWTPAEPGPALNYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAAKTSSEVNLASLPPNYHNETSTETRVGNNTVHVHQEVHKITNNQSGQVVFSETVITSVGDEEGKRSHECIIDEDCGPTRYCQFSSFKYTCQPCRDQQMLCTRDSECCGDQLCAWGHCTQKATKGGNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPTSQLLDLITWELEPEGALDRCPCASGLLCQPHSHSLVYMCKPAFVGSHDHSEESQLPREAPDEYEDVGFIGEVRQE... | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero... |
Q9UBT3 | MVAAVLLGLSWLCSPLGALVLDFNNIRSSADLHGARKGSQCLSDTDCNTRKFCLQPRDEKPFCATCRGLRRRCQRDAMCCPGTLCVNDVCTTMEDATPILERQLDEQDGTHAEGTTGHPVQENQPKRKPSIKKSQGRKGQEGESCLRTFDCGPGLCCARHFWTKICKPVLLEGQVCSRRGHKDTAQAPEIFQRCDCGPGLLCRSQLTSNRQHARLRVCQKIEKL | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero... |
Q9UK85 | MGEASPPAPARRHLLVLLLLLSTLVIPSAAAPIHDADAQESSLGLTGLQSLLQGFSRLFLKGNLLRGIDSLFSAPMDFRGLPGNYHKEENQEHQLGNNTLSSHLQIDKMTDNKTGEVLISENVVASIQPAEGSFEGDLKVPRMEEKEALVPIQKATDSFHTELHPRVAFWIIKLPRRRSHQDALEGGHWLSEKRHRLQAIRDGLRKGTHKDVLEEGTESSSHSRLSPRKTHLLYILRPSRQL | Function: Involved in fertilization by facilitating sperm penetration of the zona pellucida. May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells. Is not essential either for development or fertility.
PTM: N-glycosylated during spermatogenes... |
Q9QZL9 | MCRLRVLLLLLPLAFVSSSALPIHDVDSQQNTSGFLGLQRLLQSFSRLFLKNDLLRDLDNFFSSPMDFRDLPRNFHQEENQEHRMGNHTLSSHLQIDKVTDNQTGEVLISEKVEASIEPERNPEGDWKVPKVEAKEPPVPVQKVTDSLHPEPRQVAFWIMKMPRRRTQPDVQDGGRWLIEKRHRMQAIRDGLRGGAREDSLEDGVHIPQHAKLPVRKTHFLYILRPSQQL | Function: Involved in fertilization by facilitating sperm penetration of the zona pellucida . May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells . Is not essential either for development or fertility .
PTM: N-glycosylated during spermatoge... |
P0CH43 | DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPVTTNCAKEGEVCGWGSKCCHGLDCPLAFIPYCEKYRGRND | Function: Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents . It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein-protein interface and insertin... |
A1ZAY1 | MAFLCPVRMRRDKKKATNASIERDLPAVGVLGMGRITGSSSIETLVRVGIEKEHGLSPDSKMVVLHDFTPCVDDELEVKRGQLVNILYRENDWVYVIGQDSRQEGFIPFSYCAPCNTQLADLAVKKKLPREQCPEQPIEENIPLLGTDNKLDVLCDETLNPGSANSIENTLLVEPECTPFVKEPSGRCIVLYTFIARDENDLSVERGEFVTVLNREDPDWFWIMRSDGQEGFVPASFIYPADSVRVLQQQKATLNAMETILQQGQQGQQSQQQQQPQLGLGTDDLRYHGTELVMLYDYKAQAPDDLYLSVRRGDWIYADL... | Function: Required for the apical cell cortex localization, total cellular level and full activity of dachs.
PTM: Palmitoylated by app.
Sequence Mass (Da): 40131
Sequence Length: 355
Subcellular Location: Cytoplasm
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O01700 | MTSTTMVTTLDLVTPTSEEQPGPAPESSDFSTVVLSPDGSELVTQSAPNTPIQHREQANAEFGQKEGSPDPKNMVAATGNASKPSLNSFYADGLGQLRNGLFSCFQPVFGYFGTKTTVEIEKSEDELWEIPFDAISELEWLGSGSQGAVFRGQLENRTVAVKKVNQLKETEIKHLRHLRHQNIIEFLGVCSKSPCYCIVMEYCSKGQLCTVLKSRNTITRELFAQWVKEIADGMHYLHQNKVIHRDLKSPNILISAEDSIKICDFGTSHMQKKMDSTMMSFCGTVSWMAPEMIKKQPCNEKVDVYSFGVVLWEMLTRETP... | Function: Component of a MAP kinase pathway that functions presynaptically to regulate synaptic architecture and presynaptic differentiation . Phosphorylates and activates mkk-4 . Has a role in axonal regrowth following injury and synaptogenesis . Plays a role in modulating polymerization of neuronal microtubules . Als... |
Q09163 | MIATGALLRVLLLLLAFGHSTYGAECDPPCDPQYGFCEADNVCRCHVGWEGPLCDKCVTAPGCVNGVCKEPWQCICKDGWDGKFCEIDVRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGQASHASCLCPPGFSGNFCEIVAATNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCQNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGASPVQVTHLPSGYGLTYRLTPGVHELPVQQPEQHILKVSMKELNKSTPLLTEGQAICFTILGVLTSLVV... | Function: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation.
PTM: N- and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41320
Sequence Length: 385
Subcellular Location: Membrane
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O70534 | MIATGALLRVLLLLLAFGHSTYGAECDPACDPQHGFCEADNVCRCEPGWEGPLCEKCVTSPGCVNGLCEEPWQCVCKEGWDGKFCEIDIRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGRASHASCLCPPGFSGNFCEIVTNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCLNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGTSPVQVTHLPSGYGLTYRLTPGVHELPVQQPEHHILKVSMKELNKSAPLLTEGQAICFTILGVLTSLVVLG... | Function: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41149
Sequence Length: 383
Subcellular Location: Membrane
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A4FV93 | MPSGCRCLHLVCLLCILGAPVKPARGNDCSSLCDLAHGCCAPDGSCRCDPGWEGLHCERCVRMPGCQHGTCHQPWQCICHTGWAGKFCDKDEHICTTQSPCRNGGQCVYDGGGDYHCVCPPGFHGRDCERKAGPCEQAGSPCRNGGQCQDDQGFALNFTCRCLAGFMGARCEVNVDDCLMRPCANGATCLDGINRFSCLCPEGFTGRFCTINLDDCASRPCQRGARCRDRVHDFDCLCPSGYGGKTCELVLPVPGPAATADSPPGPTLAVLVPATGPIPHSAGAGLLRISVKEVVRRQEAGLGEPSLVAVVVFGAVTAAL... | Function: Regulates adipogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40507
Sequence Length: 383
Subcellular Location: Membrane
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Q8K1E3 | MPSGCRCLNLVCLLCILGATSQPARADDCSSHCDLAHGCCAPDGSCRCDPGWEGLHCERCVRMPGCQHGTCHQPWQCICHSGWAGKFCDKDEHICTSQSPCQNGGQCVYDGGGEYHCVCLPGFHGRGCERKAGPCEQAGFPCRNGGQCQDNQGFALNFTCRCLAGFMGAHCEVNVDDCLMRPCANGATCIDGINRFSCLCPEGFAGRFCTINLDDCASRPCQRGARCRDRVHDFDCLCPSGYGGKTCELVLPAPEPASVGTPQMPTSAVVVPATGPAPHSAGAGLLRISVKEVVRRQESGLGESSLVALVVFGSLTAALV... | Function: Regulates adipogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40404
Sequence Length: 382
Subcellular Location: Membrane
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Q61483 | MGRRSALALAVVSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGSGPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGAGIDPAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLTTQRHLTVGEEWSQDLHSSGRTDLRYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGDRGEKMCDPGWKGQYCTDPICLPGCDDQHGYCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCRNGATCTNTGQGSYTCSCRPGYT... | Function: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner . Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination... |
Q9NYJ7 | MVSPRMSGLLSQTVILALIFLPQTRPAGVFELQIHSFGPGPGPGAPRSPCSARLPCRLFFRVCLKPGLSEEAAESPCALGAALSARGPVYTEQPGAPAPDLPLPDGLLQVPFRDAWPGTFSFIIETWREELGDQIGGPAWSLLARVAGRRRLAAGGPWARDIQRAGAWELRFSYRARCEPPAVGTACTRLCRPRSAPSRCGPGLRPCAPLEDECEAPLVCRAGCSPEHGFCEQPGECRCLEGWTGPLCTVPVSTSSCLSPRGPSSATTGCLVPGPGPCDGNPCANGGSCSETPRSFECTCPRGFYGLRCEVSGVTCADGP... | Function: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degrad... |
O88516 | MVSLQVSPLSQTLILAFLLPQALPAGVFELQIHSFGPGPGLGTPRSPCNARGPCRLFFRVCLKPGVSQEATESLCALGAALSTSVPVYTEHPGESAAALPLPDGLVRVPFRDAWPGTFSLVIETWREQLGEHAGGPAWNLLARVVGRRRLAAGGPWARDVQRTGTWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPSVCRPGCSPEHGYCEEPDECRCLEGWTGPLCTVPVSTSSCLNSRVPGPASTGCLLPGPGPCDGNPCANGGSCSETSGSFECACPRGFYGLRCEVSGVTCADGPCF... | Function: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm.
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation.
Location ... |
Q4FP21 | MKNFSIAKSRRLRSTPYTSRIEKQGVTAYTIYNHMLLPAAFGSIEDSYKHLKEHVQIWDVAAERQVEISGKDSAELVQLMTCRDLSKSKIGRCYYCPIIDENGNLVNDPVVLKLDENKWWISIADSDVIFFAKGLASGHKFDVKIVEPVVDIMAIQGPKSFALMEKVFGKKITELKFFGFDYFDFEGTKHLIARSGWSKQGGYEVYVENTQSGQKLYDHLFEVGKEFNVGPGCPNLIERIESALLSYGNDFDNNDNPFECGFDQYVSLDSDINFLGKEKLKEIKLKGPQKKLRGVKIDIKEISLTGSKNIYDENNNVIGE... | Function: Major contributor to the demethylation of dimethylsulfonioproprionate (DMSP). Demethylates DMSP to methyl-mercaptopropionate (MMPA).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + S,S-dimethyl-beta-propiothetin = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3-(methylsulfanyl)propanoate + H(+)
Sequence Mass (... |
Q5LS57 | MASIFPSRRVRRTPFSAGVEAAGVKGYTVYNHMLLPTVFDSLQADCAHLKEHVQVWDVACERQVSIQGPDALRLMKLISPRDMDRMADDQCYYVPTVDHRGGMLNDPVAVKLAADHYWLSLADGDLLQFGLGIAIARGFDVEIVEPDVSPLAVQGPRADDLMARVFGEAVRDIRFFRYKRLAFQGVELVVARSGWSKQGGFEIYVEGSELGMPLWNALFAAGADLNVRAGCPNNIERVESGLLSYGNDMTRENTPYECGLGKFCNSPEDYIGKAALAEQAKNGPARQIRALVIGGEIPPCQDAWPLLADGRQVGQVGSAI... | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating demethylation of dimethylsulfonioproprionate (DMSP) to methyl-mercaptopropionate (MMPA). The intracellular concentration of DMSP is estimated to be 70 mM.
C... |
Q0QLE1 | MKAKGSVFRYGDNVDTDVIIPARFLNTSDPLELAAHCMEDIDADFSSKVNAGDIIVADDNFGCGSSREHAPISIKASGVSCVIANSFARIFYRNAINIGLPILECPEAVAVIEAGDEVEVDFDSGVITDVTKGQSFQGQAFPEFMQTLIAAGGLVNYINATEK | Catalytic Activity: (2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O
Sequence Mass (Da): 17369
Sequence Length: 163
Pathway: Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 7/8.
EC: 4.2.1.85
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Q5LRT0 | MLGQMMYQPLLISSLIDHAARYHGEAQIWSVSTEGGVEETNWAGIADNARRLGSVLTDAGLAPQSRVATLAWNNRRHLEIYYGVSGAGFVLHTINPRLFPEQLVYILNHAEDRILFFDATFLPLVEGIRPHLTTVERLVLMGPRDEAAAARIEGLEFYDEFVATGDAGFDWPDLDERTASSLCYTSGTTGNPKGVLYSHRSTVLHSFGSNTRDCIGFSARDVVMPVVPMFHVNAWGTPYACAMSGSCMVLPGPDLHGEALVGLIDRYRVTIALGVPTIWQGLLATARAKGSTLESLTRTVIGGAACPPSMIAEFRDRYGV... | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA) . It is also active with short-chain-fat... |
Q5LLW7 | MTYQAPVRDIMFAIEHLSQWPQVEALQTYSEIELDDARAALEEFGRFCGEMIAPLSTIGDTEGARLENGRVVLPEGYKTAYDQFVDMGWQSLSHPAEHGGMGLPKVVGAAATEIVNSADMSFGLCPLLTNGAIDALSITGSDAQKAFYLDKLITGRWSGTMNLTEPQAGSDLSRVRCTAVPQDDGTYAISGTKIFITFGEHDLSENIVHLVLARTPDAPEGVRGLSLFVVPKLLAGEGGETSQRNTLGCVSLEHKLGVRASPTAVMEYDNATGYLVGEENSGLRYMFIMMTSARYAVGVQGVAIAERAYQHALSYARDRI... | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl-CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).
Catalytic Activity: 3-(methylsulfanyl)propanoyl-CoA + H(+)... |
Q5LLW6 | MTQDVTSGYSNLDLDLRDNGVCVVTLNRPDKRNALDVATIEELVTFFSTAHRKGVRAVVLTGAGDHFCAGLDLVEHWKADRSADDFMHVCLRWHEAFNKMEYGGVPIIAALRGAVVGGGLELASAAHLRVMDQSTYFALPEGQRGIFTGGGATIRVSDMIGKYRMIDMILTGRVYQGQEAADLGLAQYITEGSSFDKAMELADKIASNLPLTNFAICSAISHMQNMSGLDAAYAEAFVGGIVNTQPAARERLEAFANKTAARVRPNS | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by catalyzing both the hydration and the hydrolysis of 3-(methylthio)acryloyl-CoA (MTA-CoA) to acetaldehyde, CO2, MeSH, and CoA .
Catalytic Activity: 3-(methylsulfanyl)a... |
Q97UL5 | MLKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDDQLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFKKIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNELLELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDGEDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRSAETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRHSNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFDAGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPK... | Function: Catalyzes the decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to IPP, a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Catalytic Activity: (R)-5-diphosphomevalonate + ATP = ADP... |
Q9LCC1 | MTEASESCVRDPSNYRDRSADWYAFYDERRRKEIIDIIDEHPEIVEEHAANPFGYRKHPSPYLQRVHNYFRMQPTFGKYYIYSEREWDAYRIATIREFGELPELGDERFKTEEEAMHAVFLRRIEDVRAELA | Function: Hydrolyzes N,N-dimethylformamide, and to a lesser extent N,N-dimethylacetamide and N,N-diethylacetamide. Has no activity against the substituted amides N-methylformamide, N-ethylformamide, N-ethylformamide and N-methylacetamide or the unsubstituted amides formamide, nicotinamide, acetoamide, benzamide, acetam... |
Q3INE3 | MQDTAKYLVHADITADGVVERSDVVGAVFGQTEGLLGDELDLRELQDASKVGRIDVEIDSENGQSFGRITIATSLDRVETAILGGALETIDRVGPCRSAIEVRKIEDVRSAKRREVVERAKSLLDGAFDESMRSSRDLVEEVRESVRVEDITDYEGLPAGPAVADSDAIVVVEGRADVLTLLQYGIKNAVAVEGTNVPEAVASLTETRTVTAFLDNDRGGELIRKELGQVGDIDYVATPPDGKCVEDLARHEVMSALREKVPYGRFKQAASDDADPEAAEQRTGEAAGATAADSEPAATDGIGGVTTDAEGKPVSSPESP... | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 52822
Sequence Length: 509
EC: 2.7.7.101
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P57029 | MIPSDFIDELLAKTDIVDIIDEQVPLKKGGANYMACCPFHKEKTPSFSVSPTKQFYHCFSCGAHGSAIGFVMEHQGLSFPEAVQFLADRVGMVVPKVHGQNDNPEVRAERKKKQQTLEETTAAAADFYAQQLKFNPAAKAYLDKRGLSAEVIAHYGLGYAPDGWQPLTQVFQPYPNTALVDTGMVIDNEGRHYDRFRHRIMFPIRNPRGQVIGFGGRVLDDSKPKYLNSPDTPLFDKGKNLYGLYEGRAAVKEAGRILVVEGYMDVVALAQFGVGYGVAALGTATTAEHVKILMRQADSIYFCFDGDSAGRKAAWRALEN... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 65915
Sequence Length: 590
Domain: Contain... |
Q6L1F0 | MNVDPNITKYMIKAKIVTDGVVEKPDVVGAIFGQTEGLLGDELDLRDLQKSGKIGRIEVEIDTKKGRTEGYVLIPSGLDQVESSILAAALETIDRIGPCKAKVEIESIEDVRINKRDRVIKRAEELYRKMGENGKSLSESIVQTVREEVEKKEIISYGEEHLPAGPAIADSDSIIVVEGRNDVLNLLRYGIKNTIAVQGTSVPKTVKELSKSRTVTLFVDGDHGGDLIIKEMLQVADVDFIARAPPGTEVEELTYKQIIKALKYKTPVEQYLETHGMIEELKEWSSRNTKELEERQGNELKNERPEKINENEESEKNVEL... | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction betwee... |
Q9I5W0 | MAGLIPQSFIDDLLNRTDIVEVVSSRIQLKKTGKNYSACCPFHKEKTPSFTVSPDKQFYYCFGCGAGGNALGFVMDHDQLEFPQAVEELAKRAGMDVPREERGGRGHTPRQPTDSPLYPLLSAAAEFYKQALKSHPARKAAVNYLKGRGLTGEIARDFGLGFAPPGWDNLLKHLGGDNLQLKAMLDAGLLVENSDTGKRYDRFRDRVMFPIRDSRGRIIAFGGRVLGDDKPKYLNSPETPVFHKGQELYGLYEARQKNRDLDEIMVVEGYMDVIALAQQGIRNAVATLGTATSEEHIKRLFRLVPSILFCFDGDQAGRKA... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 74176
Sequence Length: 664
Domain: Contain... |
Q8ZVU9 | MGALTIVAKYMIVAQIEVNGSVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVDIFEKNGKTKAKIHIPSNLDRYETALVAALIESIERVGPYPAAVKVVEIRDLREEKRKKIIEKAKELVKLIEEEILPDTKEIIEKLKEDVAKAEIIEYGPERLPAGPDVDKSDSIIIVEGRADVVNLVKHGYRNVIALEGISRGVPQTIIELSKKKNVTVFIDGDKGGELVLRELLKVAHVDYIARAPPGKEVEQLTAKEIAKALRNKITLEEWLAQQKAAGEKAETPQQPPPQQPVPQQEVREEAQKPAFPFDITKKIDE... | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction betwee... |
P30103 | MRVTQEFYEFLRNRINISDVVRQKLALTRKSSNYVGLCPFHQEKTPSFTVSDSKRFFYCFGCKASGDVIKFTSNISGLSYNESAIKLANDYGIEIPKLTVKQKEFYEESDNILNILELANKFFRTQLTPEILNYLYKRNITETTIKEFSIGFAPRNNKFEKFFLDKKIDITKLGQAGLIGKCKNGKIYNLFSNRITIPIRNIYNKIVGFGGRVLGNELPKYLNSFETIVFQKSDILYGEHKAISSSYKKNRSILVEGYFDVIALHQAGFNEVVASLGTSVTESHLHKLWRAGDEIILCLDGDNAGIKASIRTINLALPLV... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 68684
Sequence Length: 593
Domain: Contain... |
Q057X7 | MTKQDYYTTLNISNTASQLDIKRAYKKLAIKYHPDRNQGNKTAEEKFKKIKQAYEILSDTKKRNLYDQYGHSAFEQNNNSNNEFHSSFTTSTSDFNDIFGDVFGDIFGSNKKNRKEKGSDLQYNIILTLEEAVKGIKKEIRIPKLDKCQSCYGYGSAYGSKPSTCTSCNGHGQIHMRKGFFSVQQTCSTCRGTGTMIKNPCKICFGQGRIKKSKKLSITIPAGIDTNDQIRLNNEGEAGKYGAKSGDLYIQIKVKKHPIFKRDENNLHCKIPINFVIAGGSIILYSSFRGEITVPTLEGKINLKIPSETQSGKIFRIRGK... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q6AEC0 | MADHYEVLGVERNATPDEIKKAYRRLARELHPDVNPSTEAQERFKLVTHAYDVLSDPQQRQQYDRGGASGFGGGGGADFSGFGDIFETFFGGGGASRGPRSRRERGQDALLRVEVDLDEVVFGAHRDLEVDTAIVCETCDGSCCQPGTAPVPCDICHGTGSIQRSVRSLLGNVMTSSPCGSCRGYGTVIATPCVTCQGQGRVRARRTVPVDIPAGVDTGLRLQMPGSGEAGPAGGPNGDLYLEIKVKHHDVFSRDGDDLLCTLEVSMADAILGAAATIKALDGDIRLELKPGTQSADIVSVKDRGITHLRCSGRGDLRVG... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
P61440 | MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVSGGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRSSGFGGGRRSGPQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCVDCNGSGASKGSSPATCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTIISNPCRSCGGQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGPHGDLYVVTHIKKHELFERQGNDLILVRKISLAQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGM... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
O60884 | MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQY... | Function: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) .
Location Topology: Lipid-anchor
Sequence Mass (Da): 45746
Sequence Length: 412
Subcellular Location: Membrane
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O35824 | MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLFVQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDARQIVVKYPPGKVIEPGCVRVVRGEGMPQY... | Function: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Location Topology: Lipid-anchor
Sequence Mass (Da): 45766
Sequence Length: 412
Subcellular Location: Membrane
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Q96EY1 | MAARCSTRWLLVVVGTPRLPAISGRGARPPREGVVGAWLSRKLSVPAFASSLTSCGPRALLTLRPGVSLTGTKHNPFICTASFHTSAPLAKEDYYQILGVPRNASQKEIKKAYYQLAKKYHPDTNKDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGASGSQHSYWKGGPTVDPEELFRKIFGEFSSSSFGDFQTVFDQPQEYFMELTFNQAAKGVNKEFTVNIMDTCERCNGKGNEPGTKVQHCHYCGGSGMETINTGPFVMRSTCRRCGGRGSIIISPCVVCRGAGQAKQKKRVMIPVPAGVEDGQTVRM... | Function: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contras... |
P25686 | MASYYEILDVPRSASADDIKKAYRRKALQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTGTGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELFDDLGPFSELQNRGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSVSTSTTFVQGRRITTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTSRSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPAGGREAQHRRQGRPKAQHQDPGLGGTQEGARGEATKRSPSPEEKASR... | Function: Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family . In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins . Thereby, may regulate the aggregation and promote ... |
Q8RC42 | MDREEARKRIEELREKINYHNYRYYVLDQPEISDYEYDMLMRELIELEEKYPEFKTPDSPSQRVGGEPLDEFEPFTHIVPMLSLANAFTAEEIKEFDRRVKEAVGEVEYVVEPKIDGLSVELVYENGMFTVGSTRGDGIVGENVTPNLKTIKSIPLRLKDSVNLVVRGEVFMPKASFAKLNEERAERGESLFANPRNAAAGSVRQLDPKVTAKRDLDIFIFNLQRIEGRDFKTHVEALEFLKEQGFKVIPLIKKCTTIEEVIKAIEELGEMKDSLPYDIDGAVIKVNELDKREILGQTAKDYRWAIAFKYPAEMKKTKIV... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
B2GL64 | MSTVNAKGAKPATDANGQSLNPEEPSEALREEYAQLSDRVREARAAYYVHDQPVISDAEYDQLYRSLEEFEALHPELKANDSPTQEVGGEVGAAFSPVKHLEKMYSLEDVFSTDELVAWLERAQKQVAELPGAPEVAWLSEVKIDGLAVNLLYRDGVLVRAATRGDGTTGEDITHNVATIKTIPQRLSGENLPEEVEVRGEVFISSKDFRTLNEAMVEEGRAPFANPRNAAAGSLRQKDPQVTARRPLSMFVHGIGYVRGVDLETQSEAYEILRGWGLPVSPYSRVLSTVAEVLEFIAEFGDKRHALLHEIDGIVVKVDD... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
Q1GBF7 | MAESLEEAKQEVRQLRAQLDQWAKAYYEQDAPVVEDHVYDEKYARLLELEAAYPELKSADSITQRVGGEVNSDLPKVEHPVPMLSMGDVFSKEELAEFDQRVQKAIGHPVAYNVELKIDGLSLSLEYEEGCLKRASTRGNGQVGEDVTKNVKYIKDVPQKLPKAITTEVRGECYMSKEAFAKLNQERDEAGESIFANPRNAAAGSLRQLDPKVTKKRQLSTFIYTWINPPAGIDSQHQAICEMAKLGFHTNENGRRLENLADVYDYIDEFTKKRDSLPYVIDGIVLKVDDLALQADLGNTVKVPRWEIAYKFPPEEEETV... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
A9KPL0 | MQGKKQRITQLTELLDEAARVYEQEDREIMSNFEYDKLYDELKKLEEETGIVLAGSPTRKVGYEILSELPKERHESAMLSLDKTKEVPALIDWLGNKEGILSWKMDGLTIVLTYRNGELVKAVTRGNGEVGEVVTNNAKVFKNLPLTIPYEGELIIRGEAVIRYSDFEMINAQIPDADAKYKNPRNLCSGSVRQLNNAITAKRNVNFFAFALIRMDEMNRFKTMMEQFNWLKELGFDVVEEKLVTAENMAETMEYFESHIITNDFPSDGLVLFFNDIAYGESLGRTSKFPRNGIAFKWRDEIKETTLQEIEWSASRTGLI... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
C1D4R5 | MTDLNPTARAAGLRALLHRYNHEYYVLDAPSVPDAEYDRLFRELEALEAAHPELASADSPTRRVGGAPLAAFASVTHRLPMLSLNNVFSDMQDSDPAGRHAELAAFDQRVRDGLGLDEVEYAVEPKFDGLAVSLVYEHGVLVQGATRGDGETGENVTENLRTVRSIPLRLENAPGDDLFAPAVVPARLEVRGEVLMLKRDFERLNSEQDAAGLKRFANPRNAAAGSLRQLDSRITASRRLTFFAYAVAEADGVSLPATHSATMDWLAGLGLPVSRQRSVVRGLAGLTGAYEAMLAQRAGLPFDIDGVVYKVNRLSEQARL... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
Q4UN15 | MQNIDLISEEEAKKLLEELADKIAAYNHAYYIEDNPLVSDSEYDQLFNTNLKLEQKFPHLVLENSPSKKIGAKITNKFAKITHQIPMLSLSNAFDEQDVRDFVDRIKNFLRLDEFAPIFCEPKIDGLSFSAIYKNGLLTTGATRGDGYVGEDITANIKTIKNFPHKIDNAPEFLEVRGEIYIEKQDFLNLNKEQEEQGRDKFANPRNAAAGSLRQLDASITAQRSLKYFVYSGGVTEQNLASSQEQLLIKLKEFGFSVNEISKLTNSEEEIFTFYEYLKTNRENLPYEIDGVVYKLNDFALQNRMGFIARSPRFATAHKF... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
A5V1U3 | MNNDHLTRRVEALREQIRYHNYRYYVLDEPVISDAEYDALMRELRALEAAHPELVTPDSPTQRVGAPPGEQFAKVQHVVPMLSLANASDEAEVRAWYDRVVRLLGNDARVAFVVEPKIDGLAVTLIYRNGILVRGATRGDGETGEDVTANLRTIPGIPLRLGAFASNPEGQTNGAPVQAVIPPLIEVRGEVYMRIADFLRLNEQLAASGEKVAANPRNAAAGSLRQKDPAITARRPLRFFAYGIGQIEGVQVQTQWETLNLLRTLGFPVNRDARRFERLDDALAYCREWMTRRDELEYEVDGVVIKIDSLAQQAQLGVVG... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
Q1AZ75 | MGAPTLPRIIPPVAEKLAEARQRVEELREQIRYHNRKYYVEDAPEISDAEYDALYRELEELESRFPELVTPDSPTQRVGGEPLEEFEEVRHAVPMLSLQNARRVEELREWDARVRRLLGPEEEGRLRYVTELKIDGLAVSLRYENGRLVRGATRGNGFVGEDVTRQLRTIRSVPDRLDDDPPGVLEPRGEVYIKLKDFEEFNRRRQERGERPFANPRNLAAGSVRQLDPRVTARRPLTIYLYGVGEGYENFESHSEALAALRRYGLRVNPHTVHGDIDSVIEECGRWAKKREALDFQVDGVVVKVDSREQQERLGAVQKA... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
B8I3I1 | MADKIQLMKDKIEILDRAAKAYYQENTEIMSNIEYDKLYDELLELEKETGVVLSNSPSIHVGYELLSNLPKERHEKPMLSLDKTKDVGTLKEWLGTQKGILSWKLDGLTIVLTYQDGHLVKAVTRGTGEEGEVITNNARVFRNLPVTIAYKGTLILRGEAIIRYSDFIKINNEIADVGVKYKNPRNLCSGSVRQLNNKVTSERNVYFFGFSLVKADNVELDNSRASQMNWLKNQGFDIVDFKEVTSSNIEETVQWFSQNIEANDFPSDGLVLTFEDIAYGESLGSTAKFPRDSIAFKWRDEIKETTLLNIEWSPSRTGLI... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleo... |
O31504 | MALIDLEDKIAEIVNREDHSDFLYELLGVYDVPRATITRLKKGNQNLTKRVGEVHLKNKVWFKEAKKGKLFDALIDIEQQVEYLSAKPRYLLVTDYDGVLAKDTKTLEALDVKFEELPQYFDFFLAWKGIEKVEFEKENPADIKAAERFARIYDVLRKENNIIETNRGLDLFLIRLLFCFFAEDTDIFKRNSFTNLIKTLTEEDGSNLNKLFADLFIVLDKNERDDVPSYLKEFPYVNGQLFTEPHTELEFSAKSRKLIIECGELLNWAKINPDIFGSMIQAVASEESRSYLGMHYTSVPNIMKVIKPLFLDKLNQSFLD... | Function: Recognizes the double-stranded sequence 5'-GACGAG-3' and methylates A-5, yielding m6A. m6A methylation functions as a transcriptional modifier, promoting transcription of a number of genes (at least scpA, hbs, rnhC, yumC and zapA). One studied mechanism is via transcriptional repressor ScoC (also called hpr) ... |
P04531 | MKLIFLSGVKRSGKDTTADFIMSNYSAVKYQLAGPIKDALAYAWGVFAANTDYPCLTRKEFEGIDYDRETNLNLTKLEVITIMEQAFCYLNGKSPIKGVFVFDDEGKESVNFVAFNKITDVINNIEDQWSVRRLMQALGTDLIVNNFDRMYWVKLFALDYLDKFNSGYDYYIVPDTRQDHEMDAARAMGATVIHVVRPGQKSNDTHITEAGLPIRDGDLVITNDGSLEELFSKIKNTLKVL | Function: Phosphorylates dGMP, dTMP and 5-hydroxymethyl-dCMP while excluding dCMP and dAMP. The phosphorylation of 5-hydroxymethyl-dCMP represents the first step in the replacement of cytosine by hydroxymethylcytosine in new viral DNA genomes.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'-deoxy... |
Q6QGP4 | MSVLVGLHGEAGSGKDTVAKLIIDWCNDTYPTCLSRRYSFAKPVYELASVILGVTPEFLGERRGKEIDQWFTVTQSQLERARDVWFKYGIDKFEDFSYVWPIFEEKYLNPQQLISENKEDGLYSLFISPRKMLQLVGTELGRQLVHERIWLIILEQSIAKDDPDVAVITDVRFPNEGELLRETNHLDMDSLLVNVVPAEQKFTIKSDHPSESGIPAKYITHELVNKFDGINNLKLEVYNFCDLELEPLVG | Function: Allows the synthesis of deoxyribonucleoside triphosphates necessary for the rapid viral DNA replication . Phosphorylates all four dNMPs .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'-deoxyribonucleoside 5'-diphosphate + ADP
Sequence Mass (Da): 28701
Sequence Length: 250
EC: 2.7.4.13
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Q9UPQ8 | MTRECPSPAPGPGAPLSGSVLAEAAVVFAVVLSIHATVWDRYSWCAVALAVQAFYVQYKWDRLLQQGSAVFQFRMSANSGLLPASMVMPLLGLVMKERCQTAGNPFFERFGIVVAATGMAVALFSSVLALGITRPVPTNTCVILGLAGGVIIYIMKHSLSVGEVIEVLEVLLIFVYLNMILLYLLPRCFTPGEALLVLGGISFVLNQLIKRSLTLVESQGDPVDFFLLVVVVGMVLMGIFFSTLFVFMDSGTWASSIFFHLMTCVLSLGVVLPWLHRLIRRNPLLWLLQFLFQTDTRIYLLAYWSLLATLACLVVLYQNA... | Function: Catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis . Dol-P is a lipid carrier essential for the synthesis of N-linked and O-linked oligosaccharides and for GPI anchors .
Catalytic Activity: CTP + di-trans,poly-cis-dolichol = a dolichyl ... |
P64598 | MKALSPIAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLEVRVNSALSKDEQIKKEARINVTAYQGKVLLVGQSPNAELSARAKQIAMGVDGANEVYNEIRQGQPIGLGEASNDTWITTKVRSQLLTSDLVKSSNVKVTTENGEVFLMGLVTEREAKAAADIASRVSGVKRVTTAFTFIK | Function: Plays an important role in maintaining outer membrane integrity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20028
Sequence Length: 191
Subcellular Location: Cell outer membrane
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P45301 | MTLSPLKKLAILLGATIFLQGCVAAVIGGGAVAAKVATDPRTTGTQIDDETLEFKVENAVEKDAQIKAEGRVNAVSYNGRVLLIGQVPNSDVKDTATALAKGVEGVNEVYNELTVSPKISFAQISKDSWLTTQVKSKMFVDGRVKATDVKVISENGEVFLLGNVTQSQANAAADIASKISGVKKVIKVFKYLD | Function: Plays an important role in maintaining outer membrane integrity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20414
Sequence Length: 193
Subcellular Location: Cell outer membrane
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Q7CPQ6 | MKAFSPLAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLELRVSSALSKDEQIKKETRINVTAYQGKVLLVGQSPNSELSARAKQIAMGVEGTTEVYNEIRQGQPIGLGTASNDTWITTKVRSQLLTSDQVKSSNVKVTTENGEVFLLGLVTEREGKAAADIASRVSGVKRVTTAFTYIK | Function: Plays an important role in maintaining outer membrane integrity . Contributes to virulence .
Location Topology: Lipid-anchor
Sequence Mass (Da): 20097
Sequence Length: 191
Subcellular Location: Cell outer membrane
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A0A0N9HTA1 | MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDY... | Function: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family . Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein .
Catalytic Activity: (-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-h... |
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