ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A9KKT9 | MADKRDYYEVLGISKSASDDEIKKAYRKLAKQYHPDANPGDQTAEAKFKEASEAYAVLSDPEKKRQFDQFGHAAFEQGGGGAGGFDFNMGDMGDIFGDIFGDIFGGGRRSRASNGPMNGANLRTAIRITFEEAVFGCEKELELSLKDECETCHGSGAKPGSSAETCHKCNGKGQVTFTQQSLFGMVRNVQTCPDCRGTGKIIKEKCPDCYGSGYISRKKKIQVSVPAGIDNGQSIRIRGKGEPGTNGGERGDLLVEVNVSRHPIFQRQDYDIYSTAPMTFTQAALGGDVRISTVDGDVLYEVKPGTQTDTKVRLRGKGVP... | 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... |
Q2S030 | MPRDYYDILGVDEDASDKEIKKAYRKKAMEYHPDRNPDDPEAEQKFKEASEAYEVLSDPEKRQRYDQFGHDGVDSGAGGGRRGRGRGFHDIEDIFDAFSDIFGGAPGGGRGRGRSERGRGRPGSDLRVSLSLTLEEIAEGTEKNLRLQKYLECESCDGTGAEGGMGGQNFSMCPKCDGTGEIRQVSRSVFGQVVNVQPCPRCEGEGRIIDNLCDDCGGEGRVQGEESISINVPPGVMEGNYLTLGDAGNAGLRGGPSGDLRIEIEEEPHEHFERDGLDIYYDLHLSFPEAALGTEVDVPTLEGEARLEVDPGVQAGKILR... | 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... |
Q9YGI5 | MARLVLELLAAALLLRVAATLRISAFNIRTFGDSKMSNQTVAGFIVSILVQYDITLVQEVRDADLSSVKKLVSQLNSASSYPYSFLSSIPLGRNSYKEQYVFIYRSDIVSVLESYYYDDGCESCGTDIFSREPFIVKFSSPTTQLDEFVIVPLHAEPSSAPAEINALTDVYTDVINKWETNNIFFMGDFNADCSYVTAEQWPSIRLRSLSSCEWLIPDSADTTVTSTDCAYDRIVACGSALRQAVEYGSATVNNFQETLRIQNKDALAISDHFPVEVTLKAR | Cofactor: Divalent metal cations. Prefers Ca(2+) or Mg(2+).
Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs . Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell ... |
Q96KC8 | MTAPCSQPAQLPGRRQLGLVPFPPPPPRTPLLWLLLLLLAAVAPARGWESGDLELFDLVEEVQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLSRKKREKKKKTGSKSVDVSKLGASEKNERLLMKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETRLKEKEDALTRTELETLQKQKKVKKPKPEFPVYTPLETTYIQSYDHGTSIEEIEEQMDDWLENRN... | Function: May modulate protein synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63883
Sequence Length: 554
Subcellular Location: Endoplasmic reticulum membrane
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Q61712 | MWVPGFGSARLPQRRRSGLESSSVRPLWLLLLFLLAAVRPVRAWESGDLELFDLVEEVQLNFYEFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDVLINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLGRKKRERKKKTGSKSVDAAKLGASEKNERLLIKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETKLKEKEDALARIEIETLQKQKKVKVKKPKPEFPVYMPLENTYIQSYDHGTSIEEIEEQMDDWLENRKRT... | Function: May modulate protein synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63870
Sequence Length: 552
Subcellular Location: Endoplasmic reticulum membrane
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Q99543 | MLLLPSAADGRGTAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASASFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAKEKQRQAELEAA... | Function: Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates... |
Q91YW3 | MVAPGSVGSRLGAVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTKVIALKMDFTAARLQRGHLLLKQGKLDEAEDDFKKVLKSNPSEQEEKEAESQLVKADEMQRLRSQALDAFDGADYTAAITFLDKILEVCVWDAELRELRAECFIKEGEPRKAISDLKAASKLKSDNTEAFYKISTLYYQLGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIESAEELIRDGRYTDATSKYESVMKTEPSVAEYTVRSKERICHCFSKDE... | Function: Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid st... |
Q9R0T3 | MVAPGSVRSRLGAVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTRVIELKMDFTAARLQRGHLLLKQGRLAEAEDDFKKVLKSNPSENEEKEAQSQLVKADEMQRLRAQALDAFDSADYTAAITFLDEILEVCVWDAELRELRAECFIKEGEPRKAISDLKAASKLKNDNTEAFYKISILYYQLGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIGSAEELIRDGRYTDATSKYESVMKAEPSVAEYTVRSKERICHCFSKDE... | Function: Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (By similarity).
Sequ... |
P56709 | MRYLELAQLYQKLEKTTMKLIKTRLVADFLKKVPDDHLEFIPYLILGEVFPEWDERELGVGEKLLIKAVAMATGIDAKEIEESVKDTGDLGESIALAVKKKKQKSFFSQPLTIKRVYQTLVKVAETTGEGSQDKKVKYLADLFMDAEPLEAKYLARTILGTMRTGVAEGLLRDAIAMAFHVKVELVERAYMLTSDFGYVAKIAKLEGNEGLAKVQVQLGKPIKPMLAQQAASIRDALLEMGGEAEFEIKYDGARVQVHKDGSKIIVYSRRLENVTRAIPEIVEALKEAIIPEKAIVEGELVAIGENGRPLPFQYVLRRFR... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 63773
Sequence Length: 561
EC: 6.5.1... |
Q0SG75 | MLFSQIVATSRDVGATRSRKVKVGALREVLIQLEPAEVEPVVAWLSGELRQGRIGIGWRTLGDIPATPADVPAVTVSDLDGTVTAVAGISGSGSAARRRKLLADLFARTTADERDFLLRLLTGDLRQGALEGVMTDAIAAAADLPVEPVRRAFMLSGRLPATAVAAFDGGVDALTAFRLEVGRPVRPMLASPAESLTDAWTELGGDVSVEYKLDGARIQVHRNGDDVHVFTRTLREITGSVPELVELVAGLPCTSAVFDGETLALTDSGRPRPFQETMSRFGAESARDLLLHPYFFDCLHLDGVDLLDAPLEERLAALER... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 54393
Sequence Length: 503
EC: 6.5.1... |
Q980T8 | MEFKVIAEYFDKLEKISSRLQLTALLADLLSKSDKTIIDKVVYIIQGKLWPDFLGYPELGIGEKFLIKAISIATNTDENSVENLYKTIGDLGEVARRLKSKQQSTGILGFLGTTSKESLTVDEVYSTLSKVALTTGEGSRDLKIRLLAGLLKKADPLEAKFLVRFVEGRLRVGIGDATVLDAMAIAFGGGQSASEIIERAYNLRADLGNIAKIIVEKGIEALKTLKPQVGIPIRPMLAERLSNPEEILKKMGGNAIVDYKYDGERAQIHKKEDKIFIFSRRLENITSQYPDVVDYVSKYIEGKEFIIEGEIVAIDPESGE... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Interaction with PCNA enhances ligase activity. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to cou... |
A9GU24 | MLVSDLVATSERVAALSRRVEKIGALAALLRRFSPAEVQIGVDWLTGRLRQGRLGLGPSVFAEARRASPSVAQPALTLGDADAVFTEIARASGPGAGGERRAALAGLFARATDLERDFFARLLAGELRQERLEPVMVDAVARAARVPPASLRRAVMLAGDAAEVVKAALLEGALGLQRFSLQLLRPVQPMLAQSADDVVTALSELRAMALEWKLDGVRVQAHKAGDEVRVFSRGLGPVTKAVPEIVEIVRALPVRSVVLDGEALAFRPDGAPHPFQVTMRRFGRAHDAAALRAELPLRALFFDVLHLDGEDLLDRPGSER... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 57294
Sequence Length: 533
EC: 6.5.1... |
Q9FCB1 | MLLARLAQVSREVAATSARSRKTVLLAELFREAEAADVPVVIPYLAGRLPQGRIGVGWKVLSRRVPPADAPTLTVRDVDARLTRLGAVSGAGSQAERTRLVGELMGAATEDEQRFLIGLLTGEVRQGALDAAAVEGLAAATDAPPADVRRAVMLAGSLQTVAEALLADGPGALDRFRLTVGQPVLPMLAHSASSVAEAVGKLGAAAVEEKLDGIRVQVHRDGGTVRIYTRTLDDITDRLPEVTEAALALPGERFILDGEAISLDADGRPRSFQETAGRVGSRTDVATAARAVPVSAVFFDVLSVDGRDLLDLPLTERHAE... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 54696
Sequence Length: 512
EC: 6.5.1... |
B1W5J2 | MLLAELAQVSLEVAATSARSRKTALLAGLFRNAGPEDVPVVIPYLAGRLPQGRIGVGWRSLGEPVEPACDPTLTVTGVDAELTALAATSGPGSQARRRERLRTLFAAATADEQRFLRALLTGEVRQGALDAVAADALAHAAGAPPADVRRAVMLAGSLQDVATVLLADGPGALADFRLTVGRPVQPMLARSAASVGEALDKLGPCAVEEKLDGIRVQVHRDGERIRAYTRTLDDITDRLPELVSAVAALHARRFVLDGELIALGEDGRPRPFQETASRVGSRRDVAGAAAHVPVVPVFFDALRVDGEDLLDRPFADRHAA... | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 54767
Sequence Length: 511
EC: 6.5.1... |
B9KG17 | MTYQEYLEKVKLAKEWMRAYYEDDEPLASDEEYDKLIRELKEFEALYKDKISKDSPTQNIAPTIQSEFHKITHSAKMWSMEDVFDEAELRAWAKRAKCEFDFFIEPKFDGASLNLTYENGKLISGATRGDGEIGEDITLNVKEISNIPKIIPYKDKIEIRGEVVILKEDFEKINEKRAKDGLSLFANPRNGASGSLRQLDTSITKERNLKFYPWGVGENSLKFSKHSEVMEFIRSLGFLKDDFVYCVKTLDEVLEKYHELLEKRDQKPMMMDGMVVRVDDLKKCQELGYTVKFPKFMAAFKFPALEKTTTLLGVNLQVGR... | 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... |
Q3AD38 | MDKEAVKKRIEELRALLHYHNYRYYVLDQPEISDAEYDRMLRELISLEQQYPEFITPDSPSQRVGGEVAKEFREVAHLKPMYSLDNAFGPEDLKEFDRRVRSLLPGQEVEYEVELKIDGLAISLVYENGVLVRGATRGNGTTGEDITANVKTIKAIPLKLRNPIPLLEVRGEAYMPKESFARLNEQREERGEPLFANPRNAAAGSLRQLDPKVTAERDLSAFMYAIGEVQGYEPKTQAELMEWLSELGFKVNPYREVFNNIDDVINYCQSWHEKRFSLPYVIDGLVIKVNSLAQQEALGFTAKSPRWAIAYKFPAEIAET... | 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... |
B0T1N5 | MSQIAVADLTEAQAAEELERLADDLAAHDLRYHQQDAPTISDAEYDALKRRNLDIEDRFPHLVRDNSPSMRVGAARAEQFSPVEHGVPMLSLDNAFSNDEATEFDARIRRFLRLTNEPVFYTAEPKIDGLSASLRYEKGVLVQGATRGDGRMGEDVTANLRTIADIPHRLRGGDPQGGGWPDVIEIRGEVYVELEAFAAFNAAALEAGQRTYANPRNFAAGSLRQIDPKISAQRPLRFFAYAWGLTSEGFAATQWEALGKLRDWGFVTTAPPAERVQDAQGLLDIYAKFEVERPKLAFDIDGVVYKVDDLEQQRRLGFVS... | 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... |
B3PGQ8 | MSNLSLFDDVSAEIAQLREQIRYHNYRYYALDEPQIPDAEYDRLMQRLRELEAQYPASVTPDSPTQRVGAAPLSAFQTVEHQIPMLSLDNAFEEADVIAFNQRILDRLKSTENIEYACELKLDGLAVSLLYRDGVLVRGATRGDGSKGEDITQNLRTIASVPLKLLGEGYPAVLEVRGEVYMPKAGFNALNEKARSTGEKLFVNPRNAAAGALRQLDSRITASRPLEMCAYSVGLVEGGELPGTHTGILAALKSWGFLTNKETATASTIADCIAFYQSIQARRDSLAYDIDGIVFKVNARELQESLGFISRAPRWAIAYK... | 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... |
A9WCA1 | MSHTTVADRINELRSLIRRYDYHYYVLDDPIVSDAEYDALMTELRALEAAHPELITPDSPTQRVSGTPASQFAKVQHPQPMLSLGNAFTKADLLAWRDRVLRLLGPDAIVAYVVEPKIDGLAVALTYRDGRLVQGATRGDGEVGEDVTANLRTIGSIPLTLQATSTPQDDDLPTTLPTTIEVRGEVYMRTADFETLNDRLAAAGEKIFANPRNAAAGSLRQKDPTITAARPLRFFAYGVGVVEGISLSSQWQTLRYLRALGFPVNQDVRRFTDFAEVLAYCEAWMAKRDDLPYEADGVVIKIDDFAQQRELGVVGRDPRW... | 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... |
Q0RDH8 | MNAPPGSGDAAASALEAASQAEASEVEASEAEAASAVEAASAVGAGGAVQPAVAASVADRARAAELARELDEHAYRYYVLDSPTVSDAEYDRLMRELTALEEHHPELRTPDSPTQKVAGSYSTLFTPVEHLERLLSLDNVFDDDEFHLWAARAARETEVDGWLCELKIDGLAVDLVYEEGRLVRAATRGDGRTGEDITPNIRTLASVPTRLRGASVPELLEVRGEVFFPTEKFAELNASLVAGGGKPFANPRNAAAGSLRQKDPRVTATRPLDMIVHGLGAQRGFDAASQSAAYARFAEFGLPVSTHFEVLASVGDVLAF... | 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... |
Q2J6U3 | MSATAGTADESGVASAAASADERARAASLARELDEHAYRYYVLDSPTISDAEYDRLMAELAALEERHPDLRTPDSPTQKVAGSYSTLFTPVEHLERMLSLENVFDDDEFHQWAARVARESEVDAWLCELKIDGLAVDLVYEDGYLVRAATRGDGRTGEDITPNIRTLASVPVRLRGPRVPGLLEVRGEVFFPTAKFAELNAGLVAVGGKPFANPRNAAAGSLRQKDPRVTATRPLEMIVHGLGAQRGFEVTSQSAAYARFAELGLPVATHFEVLATVPGVLDYVHRWGDARHDVVHEIDGVVVKVDSFALQRRLGSTSKS... | 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... |
B0TY02 | MTPSDFISIDYKTLTKAQLKSYIDDLAEYLGEQSYLYHTIDKPVITDSDYDKLFRLLQDLVDDNPQLKPSNSVLDRVGGEILAGFETIKHKKKMTSLANVFSLEELRDFYDKIEYDIELECEPKMDGLAISIFYKNGKFDYAVTRGDGIQGEKVSENVKTIRNVPLKLNTSNPPEELEVRGEIILDKQSFLSLNEYMQTHENKTFANPRNAAAGSIRMLDSKVVAKRPLKLYSYGIGYFSKDFVHPETQFELMNLLQSFGFTISDNMFLAKNFSEVEVYHHKMSHQRADLAYDIDGLVFKVNNIKLQDTIGYTARGPKWA... | 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... |
Q8RI94 | MEIKKRIEELKNNQTGLTFYSSQELNDLEKIVKLREDLNKYRDSYYNDNKSLISDYEFDILLKELESLEEKYPQYKEISSPTTSVGASLKENKFKKVEHLHPMLSLANSYNIGEIVEFIERIKKKIPKEQELKYCLEVKLDGLSISLTYRQGKLVRAVTRGDGFIGEDVTENILEIASIVKTLPQAIDMEIRGEVVLPLASFEKLNNERLEKGEELFANPRNAASGTLRQLDSKIVKDRGLDAYFYFLVEADKLGLKSHSESIKFLESMGIKTTGIFELLETSKDIEKRINYWEKERESLPYETDGLVIKVDEINLWDEI... | 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... |
C1A6H2 | MTASSGTPPHQTVERARELREQLGTAQHEYYVLDRPTLSDQEYDRLFRELQGIEAEYPTLCTEDSPTRRVGAPVQSAFSPHRHLVRMLSLDNAFDLSELEDFEQSLKRVVGDAIHTSGYTVELKIDGAAVALTYREGVLVTAATRGDGTDGEDVTANVRTIRGVPLRLHGDNHPPLMEVRGEVYLPFAGFERMNEARVAAGEPVYVNPRNAAAGSMRQLDSANTAARPLRFFGYAAVLPDGSAPARSQWELLEQLSAWGVPVAPHRQRCHTIQEAEAWATVVEHETRATLGFAIDGGVVKVNDMALQDELGIRADRTPRW... | 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... |
O87703 | MDRQQAERRAAELRELLNRYGYEYYVLDRPSVPDAEYDRLMQELIAIEEQYPELKTSDSPTQRIGGPPLEAFRKVAHRVPMMSLANAFGEGDLRDFDRRVRQEVGEAAYVCELKIDGLAVSVRYEDGYFVQGATRGDGTTGEDITENLKTIRSLPLRLKEPVSLEARGEAFMPKASFLRLNEERKARGEELFANPRNAAAGSLRQLDPKVAASRQLDLFVYGLADAEALGIASHSEALDYLQALGFKVNPERRRCANIDEVIAFVSEWHDKRPQLPYEIDGIVIKVDSFAQQRALGATAKSPRWAIAYKFPAEEVVTTLI... | 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... |
Q74ER9 | MDKQTAADRVAALRTELERHNRLYYAEDRPEITDAEYDLLFRELVDLETRFPDLAAPDSPTQRVGGAPLDKFEQVTHRIPMLSLENAFTDVEIADFDDRVKRFLGLHGDVEIDYVCEPKMDGLAVELVYERGILTVGSTRGDGVVGENVTHNLKTVRGIPLRLRCEQPPELLEVRGEVYLPLAAFQRLNAQREEEGEPPFANPRNAAAGSIRQLDSRITARRPLAIFCYAPGEVRGASFAAQTEFLDRIGEWGLPVNPLIRPVKGVAEILAYYREMTERRDSLPYEIDGVVVKVDSFALQRELGEKSRSPRWAVAVKFPP... | 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... |
B2J3P0 | MTQIKPEVKRTEELRQLLQQASYAYYVLDTPIMEDSVYDQLYRELQQLEIQYPELTAPDSPTQRVGERPATQFTSVRHNIPLYSLENAFNIDELQGWDQRWRRQVPKIDSVEYVTELKIDGSALALTYQDGILVRGTTRGDGVMGEDITQNVRTIRSIPLRLNFEGLEILERVEVRGEAFLPLEVFKQINEERQKAGEQLFANPRNAAAGTLRQLDSRIVAKRRLAFFGYTLHIPGRDDTSIANTQWEALELLEKMGFQVNPNHKLCASIAEVAKYYEYWDTERLNLPYMTDGVVVKLNSFKLQEQLGFTQKFPRWAIAL... | 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... |
Q2G7J5 | MTTSALTEAEAANELMRLARQIAKHNRLYHAEDSPEITDAEYDALVRRNAELEAAFPHLIRPDSPSAQIGHEIAASPLGKVQHEVRMMSLDNAFTDEEVEEFVARVRRFLALPEDAEVVMTAEDKIDGLSCSLRYENGRLVRAATRGDGQVGEDVTANVAHIPDIPQELKAAGLFDIPAVFEIRGEVYMAKDDFLALNARQAEAGEKIFANPRNGAAGSLRQKDASVTASRPLRFLAHGWGAASEVPAATQFEMMRKIADWGVPVSPLLVRCSSAAEMVAHYRDIGEKRASLPYDIDGVVYKVDRLDWQDRLGFVAKAPR... | 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... |
Q8CXK6 | MNKEQVSKKIESLIELLNQYGYEYYVLDNPTVPDAEYDQKLRELQQLEQDFPDLVMENSPTQRVGGAPLASFQKVTHNVPMLSLGNAFNEQDLRDFARRASNGTDQPISFVCELKIDGLAISLTYENGKFVRGATRGDGTIGEDITSNLKTIRSIPLSIKEQGTLEVRGEAYMPHKSFLALNELREKNEEEPFANPRNAAAGSLRQLDPKIAAKRNLDIFLYGVGEWENSDLTSHSEHLTRLKELGFKTNKEWKKCNTIDEVIEYVNYWTEHRNDLSYEIDGIVIKVDSLDQQEELGFTAKSPRWAIAYKFPAEEAMTTL... | 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... |
Q30ZK6 | MDRRGAPVKQDSAKVEQRMEELRTLLEYHGHRYYVMDEPEISDAEYDALFRELVRLEEEHPEHIHPGSPTHKVGGQILDGLKPREHSLRMYSLDNAFGIEEFREFVERVVRLEPDAPLEFWVDPKMDGLAMELVYENGVFLLAVTRGDGSMGEDVTHTMRTVRNVRMRLNPEIEAPVRLEVRGEVIITRADFEALNARQQQKGGKLFANPRNAAAGSVRQLDSSVAAARPLRFMAYGVGQVVWADGRQRWRTQYDIMRGLQELGFAVPSQGRLCAAPADVEAAFTELSAARHELPFEIDGVVAKLNDLDLQEALGFTARA... | 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... |
A6LA55 | MVEAKIKALRDELERHNYNYYVLSAPTISDFEFDKMMKELQELEAAHPEFADPDSPTRRVGSDLSKEFEQVVHKYPMLSLGNTYSEDEIRDFYDRTVRSLNEPFEIVAELKYDGTSISLTYEKGRLTRAVTRGDGTRGDDVTANIKTIRSVPLRLRGSDFPEEFEIRGEVLLPWAEFDRLNKEREEQEEPLFANPRNAASGTLKQQNPAIVASRKLDAYFYYLLGENLPAEGHYENLQAARAWGFKIPDVIRKCQSLQDIFDYIAYWDVERKNLPVATDGIVLKVNSLRQQRNLGFTSKSPRWAIAYKFQAERAETRLNS... | 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... |
Q6MAB5 | MITQKDYEKLCHEIWHHNKLYYIEHQPIISDEEFDALLKKLEEIERSHPEWITEFSPSQRVNESLTSGFKTVAHRTPMLSLANTYSKEEIEDFIKRLQKLVGKRQVEFSVELKMDGIAITAIYEQGIFKRGITRGNGKRGDDITTNMRMIENLPLQLSGENLPDFLEIRGEVFMPRQVFLQLNEQKLQDGEVLWANPRNAAAGSLKLLDPKMVAERRLAVVFYGLAEDSSASIKKQAEVPSFFRSIGLPALEHHAYCQNIEQIWKFAEEIRSLRTILPYDIDGIVIKLNDFKDQKRLGVTGKSPRWAIAYKFAAEQAKTR... | 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... |
Q9CKA9 | MTDSIKLEIEQLRQTLRYHEYQYHVLDNPQIPDAEYDRLFHRLKTLEQQYPQWFSPDSPTQRVGAKPLSAFAQVQHEMPMLSLDNAFSDEELHAFVKRIQDRLVFSPKLLEFCCEPKLDGLAVSILYVDGKLTQAATRGDGSTGEDITLNIRTVRNIPLQLLMENPPTRLEVRGEVFMSQAGFEVLNEKALARGEKTFANPRNAAAGSLRQLDPRITSQRPLLLNAYSIGVAEGIDLPDTHFERLQWLKSIGIPVNNEIQLCEGTENVLNFYRAIMQKRSTLGYDIDGTVIKVNDIALQEELGFISKAPRWAIAYKFPAQ... | 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... |
A4VKN0 | MPSAQTAAERIAELRSEIDAHNYRYYVLDEPSVPDAEYDRLFNELKALEAEHPELVTPESPTQRVGGAALAAFGQVRHEVPMLSLGNAFEEQDLLDFDRRVREGLDLPAGDLFGDGAVVEYSCEPKLDGLAVSLLYENGHLVRGATRGDGSTGEDISANVRTVRNIPLKLHGSGWPAVLEVRGEIYMPKAGFEALNARQLESGGKPFANPRNAAAGSLRQLDSKITASRPLELCAYGVGRSDGELPDTHIGILQALKGWGLPISRELKLAKGVAECRAYYDAIGAKRDALPYEIDGVVFKVNAVEQQRELGFRAREPRWA... | 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... |
C1DW63 | MYSEETQRKLIEKTREFLNLDIKSIDRKKAESIIEDLREVIRFHDWRYYVLAQPVISDYEYDKLFKLLKDIESKYPDLITPDSPTQRVPSEITKVFPQVKHLTPMLSLDNSYNEADLRDFDRRVRELTGLEKIEYAVEPKFDGAGISLIYEKDLFKRGATRGDGEVGEDITNNLKVIKSIPLSAKFSSYGIDKVEIRGEVLIRKDIFKRINEQRLEEGLPLFANPRNAAAGSIRLQDPKEVAKRGLEAFVYQITYAEKDGKNLLGTVLKKHSDNIKMLHLLGFKTPYEVLKVCNGIDEVIDYCREWERKRDNYPYEIDGM... | 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... |
Q30QV9 | MKKEQYIKAVELLNLYSYHYYVLDDAITTDEVYDKLYHEVLEYEESHKEDILKNSPTQRVGDTVSEGFSKAPHLSRMWSLEDVFDSDGLQKWLIKTYKLDSNISFYCEPKYDGASLNLIYENGELSQAITRGDGEVGELITQNVKTIRSVPLSIEHKEKIEIRGEVVIFKDEFEKINQTRLKDGEALFANPRNAAAGSLRQLDSSITASRNLVFLPYGVGENFLEHKLLSQKMEYIYSLGFKKPPFCATCKDFNEIEAVYQEMSRNRDSYPMMLDGMVVKVDEIAAQIDMGYTVKNPRFSVAYKFPAVEKITTIKEIILQ... | 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... |
Q67KI8 | MDRSWAERRIPELIETIRHHEYLYYVKNEPEISDAAFDELMQELKQLEEAFPDLRRPDSPTQRVGGATAPDFAKVPHQPPMYSLDNAFSEADLRDFDRRVREGLGGEPVSYVCELKIDGLSISLRYEDGLFVQGATRGDGETGEDVTENLRTIGSIPLRLDGTEAPVPPRLIVRGEVYMTKQVLEELNAALAAEGKPLLQNPRNAAAGGLRQKDPRKTRERRLDAFLYQVVDAEALGIADHWSALQRLQAWRFKVNPHRHLAHTIDEVLDWVAGWQARRHELPYEIDGLVIKVNDLAQQRRLGFTSKFPRWAIAYKFPAE... | 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... |
Q2LTN8 | MMDAESARKNIEDLKARIEYHNRRYYQLDDPEISDAEYDSLLQELIALEKQFPQWLTEDSPSRRIGAAPLSKFAPAVHLSPMLSLANAFSEEEILEFDRRLKRFLDSSERLSFVVEPKIDGVAVNLIYSSGVLTTGATRGDGAKGEDVTQNIRTLHTIPLKIQNGSDERLPEQIEIRGEIYMETAAFRKLNERRLAAGEPPFANPRNAAAGSLRQLDASITARRPLKMFCYAVGIVRGRAFTYHHDVLHALKKWGFSVNPFIRQVEGIEKCIEFYRELQDLRNELPYEIDGMVIKVDDLSLQTRLGAVSRSPRWAVACKF... | 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... |
Q31RL0 | MTASQTGPTTTAIAQRASELRQLLQQASYAYYVLDQPVMEDAVYDRLYRELQDLEQQHPSLITPDSPTQRVGEQPATGFESVQHRIPLYSLENAFDAEELRSWDQRWRKLAPDVPADAGYVCELKIDGAAIALSYENGLLVRGATRGDGTRGEEITANLRTIKSIPLRLQTDQPPEWLEVRGEAFLSLTRFKQLNTEREKHGEALFANPRNAAAGTLRQLDPRIVAERQLDFFAYSIQGPNDWANLDQAASLDCLQSLGFRVEPHRQTCPTLAEVEQYFSDWDARRRDLPYLTDGVVVKLQSRRLQDELGFTQKFPRWAI... | 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... |
A0LI67 | MPDREKAHARIEALREEIRHHNYLYYVLDRPEISDEAYDGLFRELVRLEESYPALITPDSPTQRVGAAPAEKFLPFPHTIPMLSLENAMSEAEVFEFARRVRKILGDRGDVDFMAEPKMDGLAVELVYENGELTGAGTRGDGYVGEDVTRNAKTIRAIPLKLYAGAGGASPPARIAVRGEVYMDRKDFAALNRSREQAGEPLFANPRNAAAGSLRQLDPSVTAARSLKAFFYGVGEVSGYRFKTQAQTLEQLRRWGLPVNPLSRVCPSIEDAVSFYNEIAAGRDALPFEIDGVVVKVNSIEWQEMLGEKSRSPRWAIAYK... | 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... |
Q2JW63 | MDPKLEQRARELRALLQKASIAYYVHDAPILEDSVYDRLYRELQELERAYPELITPDSPTQRVGEKPAEQFPTVSHRIPLYSLENAFNLEELKEWQERLWRVLGRTPEEGELEYVCELKIDGAALALTYVDGLLQRGATRGDGQSGEDITPNIRAIPSIPLRLATAAPPPVLEVRGEAYLPIAEFERINRERCSAGDPPFANPRNCAAGTLRQLDSRVVAARKLSFFAYALHWPEGWPSGDPPQTQWECLQRLKDLGLPVNPLSQVCRGLEEVVQFYERWRQAQLPYACDGVVVKLNSLRLQEEAGFTQKFPRWAIALKY... | 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... |
Q92874 | MGGPRALLAALWALEAAGTAALRIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQYKEMYLFVYRKDAVSVVDTYLYPDPEDVFSREPFVVKFSAPGTGERAPPLPSRRALTPPPLPAAAQNLVLIPLHAAPHQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVACGARLRRSLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTLKFHR | Function: Divalent cation-dependent acid DNA endonuclease involved in the breakdown of the nucleus during corneocyte formation of epidermal keratinocytes. May play an immune role by eliminating harmful DNA released into the extracellular environment by damaged epidermal cells.
Sequence Mass (Da): 32853
Sequence Length:... |
Q13609 | MSRELAPLLLLLLSIHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRGITYNYVISSRLGRNTYKEQYAFLYKEKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVKKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAYKLTEEEALDVSDHFPVEFKLQSSRAFTNSKKSVTLRKKTKSKRS | Function: Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA . Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and ... |
O74354 | MRTTLRLHIIKDGEQDNQFMILFDPSSSISLLKEKVQETYKSLYPFESNINIRNIKNEESYDIPNEYLVGEIFPTNSKVIVESFSSPLKKLDGTMINFKEKNIQHDLDGVENDFATVQSASNGVHAINGKRTHPDESENPRKLPKKNFVEAIDANSPGFVYRPTSIRDRAYSISSNHDNESTLTEGIALKEIESPDKDRKADGIVNLSVTQEEDDNHQSFNSSLTPSQPTTYNRANFFSINDASSDSSSDAPLRTLSSPSRLRMKDNDRKYLVEHSPAALIKESETIDGIDDKSLRSSTREVSVESPNEDSVNDDSSSDV... | Function: Negatively regulates the septation initiation network (SIN) pathway, independently of the cdc14 phosphatase clp1. May also have a role in silencing rDNA transcription. Required for maintaining the exclusive nucleolus localization of nuc1.
PTM: Phosphorylated by clp1.
Sequence Mass (Da): 65977
Sequence Length:... |
P47120 | MSTNFEKHFQENVDECTLEQLRDILVNKSGKTVLANRFRALFNLKTVAEEFATKPEEAKKAIEYIAESFVNDKSELLKHEVAYVLGQTKNLDAAPTLRHVMLDQNQEPMVRHEAAEALGALGDKDSLDDLNKAAKEDPHVAVRETCELAINRINWTHGGAKDKENLQQSLYSSIDPAPPLPLEKDATIPELQALLNDPKQPLFQRYRAMFRLRDIGTDEAILALATGFSAESSLFKHEIAYVFGQIGSPAAVPSLIEVLGRKEEAPMVRHEAAEALGAIASPEVVDVLKSYLNDEVDVVRESCIVALDMYDYENSNELEY... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Catalytic Activity: [eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A... |
Q70KF0 | MGGRMRALQFHGGHKAQIIDTPRPEAPPGWAVVKVHYCCLCGSDLWLYRGKWHGNRYPIVPGHEWAGVVDSAPEGYESWVGRPVTGDLIVGCQGCGPCRDGLPVMCENLIEIGFTVDGGCAGYVAVPITNLYLLPEGMDLAAASQTEPLAVALHAVDRINLRPAERVAVLGAGGIGQLILQSARATGATVTLATDLVAERRKIAEESGAAAAVHPSELPELTSYADKVDVVFEASGDPESVVRALDLVRPGGRVCLVGYQVGAEHALETARLPLSYASLVGVMGPGGKYREAVDLLANGAIDTQPILTDIVTLDDYAPAI... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI).
Catalytic Activity: 2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy-scyllo-inosose + H(+) + NADPH
Sequence Mass (Da): 3... |
Q53U21 | MKALVFEAPERAVLTHRDIPAPAPGEALVRVAYNSVCGSDLSFYKGVWHGFTYPVVPGHEWSGSVVDVNGPRGADLVGRNVVGDLTCSCGTCAHCAAGTPTLCEDLGELGFTRDGACAEYMTVPVANLRPLPDTLPLRTACQVEPLAVALNAVDRLGVTPGEKVAVMGAGGIGLLLVQAVRLRGGTVTAVAEPVPERRAAALALGVPAAVGGDPGALVELTRSDPAAVPDVVLEASGYPTAVQEAVEAVRPGGRVGLVGYRIEEAAVMAPHHIVLKVLTVRASMGPGTRFEEAVDVLASGAVDVDALLSHEFALDDYAKA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI).
Catalytic Activity: 2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy-scyllo-inosose + H(+) + NADPH
Sequence Mass (Da): 3... |
Q9S5E2 | MTTKQICFADRCFNFAFGEHVLESVESYIPRDEFDQYIMISDSGVPDSIVHYAAEYFGKLAPVHILRFQGGEEYKTLSTVTNLQERAIALGANRRTAIVAVGGGLTGNVAGVAAGMMFRGIALIHVPTTFLAASDSVLSIKQAVNLTSGKNLVGFYYPPRFVFADTRILSESPPRQVKAGMCELVKNMLILENDNKEFTEDDLNSANVYSPKQLETFINFCISAKMSVLSEDIYEKKKGLIFEYGHTIGHAIELAEQGGITHGEAIAVGMIYAAKIANRMNLMPEHDVSAHYWLLNKIGALQDIPLKSDPDSIFHYLIHD... | Cofactor: Binds 1 Co(2+) ion per subunit.
Function: Catalyzes the intramolecular carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).
Catalytic Activity: D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate
Sequence Mass (Da): 40747
Sequence Length: 368
Pathway: Metabolic intermediat... |
Q53U19 | MQTTRIAMEDASFPYRLGTDCAEDVVARLAALEASSYLVVADTTVAELYGAALTAHIDKEAGPSHLLTHEVGEVHKTLATVSALAEQALGRGADRRSVVVALGGGVTGNIAGLMASLLFRGIRLVHVPTTVVAMLDSVLSLKQAVNTTFGKNLAGTFYQPVEVLADTAALRTLPPREIRSGMGEVVKNALAIRPAMLDRLAGALRPDTRYDDETMRWIIAESLAAKADVTSGDKHERRSGLVLEYGHTAGHAIEHASRGAVAHGAGVAVGMTLAAEVSRRLGHADAGLVALHRELVAAAGVEPAVPDHVDTALVKNWLAY... | Cofactor: Binds 1 Co(2+) ion per subunit.
Function: Catalyzes the intramolecular carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).
Catalytic Activity: D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate
Sequence Mass (Da): 43960
Sequence Length: 430
Pathway: Metabolic intermediat... |
Q99704 | MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSGGGRGSSRRLDCKVIRLAECVSVAPVTVETPPEPGATAFRLDTAQRSHLLAADAPSSAAWVQTLCRNAFPKGSWTLAPTDNPPKLSALEMLENSLYSPTWEGSQFWVTVQRTEAAERCGLHGSYVLRVEAERLTLLTVGAQSQILEPLLSWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTAQGNDIFQAVETAIHRQKAQGKAGQGHDVLRADSHEGEVAEGKLPSPPGPQELLDSPPALYAEPLDSLRIAPCPSQDSLYSDPLD... | Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding sit... |
P97465 | MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSRGGRGGSRRLDCKMIRLAECVSVVPVTVESPPEPGAVAFRLDTAQRSHLLAADAVSSTAWVQTLCRTAFPKGGWALAQTENQPKFSALEMLENSLYSPTWEGSQFWVTSQKTEASERCGLQGSYILRVEAEKLTLLTLGAQSQILEPLLFWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTSQGNDIFQAVEAAIQQQKAQGKVGQAQDILRTDSHDGETEGKTVPPPVPQDPLGSPPALYAEPLDSLRIPPGPSQDSVYSDPLGS... | Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding sit... |
Q0P4G7 | MQANIFPFYPQPRTSFKFDTKIIEIIIICIVTACTFIIILPGIRGKSRSIWLFRILTSLFIGAVILAVNFTSDWETGIVTATTVYKSFSHSMLNASIGLWIGLKGVNITLIGNPVYQLNETINYNEEFAWESANQFDKNYKDGLERGLPYPILYVAEKFTINSPCGLFQQYCISTYYSSEIMWVAFGSWILYNVLFSMPVILYGICMMFVTAICMLVSLISFASVRQAPVCNIHFGNAVLKTHFGVSYWLSLVTGLFCLIVSLVLLFLYKTQPKVIRLIFSYGEEEDLSDKSENEEEHSSALSLNEML | Function: Possible role in maturation and transport from the endoplasmic reticulum to the plasma membrane of functional dual oxidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34937
Sequence Length: 308
Subcellular Location: Membrane
|
Q1HG44 | MTLWNGVLPFYPQPRHAAGFSVPLLIVILVFLALAASFLLILPGIRGHSRWFWLVRVLLSLFIGAEIVAVHFSAEWFVGTVNTNTSYKAFSAARVTARVRLLVGLEGINITLTGTPVHQLNETIDYNEQFTWRLKENYAAEYANALEKGLPDPVLYLAEKFTPSSPCGLYHQYHLAGHYASATLWVAFCFWLLSNVLLSTPAPLYGGLALLTTGAFALFGVFALASISSVPLCPLRLGSSALTTQYGAAFWVTLATGVLCLFLGGAVVSLQYVRPSALRTLLDQSAKDCSQERGGSPLILGDPLHKQAALPDLKCITTNL | Function: Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34787
Sequence Length: 320
Subcellular Location: Endopl... |
Q9D311 | MTAWDGVLPFYPQPRHAASFSVPLLIVILVFLSLAASFLFILPGIRGHSRWFWLVRVLLSLFIGAEIVAVHFSGDWFVGRVWTNTSYKAFSPSRVQVHVGLHVGLAGVNITLRGTPRQQLNETIDYNERFTWRLNEDYTKEYVHALEKGLPDPVLYLAEKFTPSSPCGLYHQYHLAGHYAAATLWVAFCFWIIANALLSMPAPLYGGLALLTTGAFTLFGVFAFASISSVPLCHFRLGSAVLTPYYGASFWLTLATGILSLLLGGAVVILHYTRPSALRSFLDLSVKDCSNQAKGNSPLTLNNPQHEQLKSPDLNITTLL | Function: Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis (By similarity).
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35427
Sequence Length: 320
Subcellular ... |
P97224 | MERVTIIGIIFAILVVGWILATGQWAYGNVVGPLVNHSKIPLLKITYVSAYENAKGTYLILNITDCCGPDAYPASAPIMEIYNSTWHVFLYSYNISNDTVKVIQAPWNENKKDYTNWYSGFVVILGSEAQFQLQLPFHLSPGTYHIKLYTPAVSSKVLAKQTATFTIS | Function: TQO plays a role in sulfur oxidation and is proposed to couple sulfur oxidation to dioxygen reduction; caldariellaquinone or sulfolobus quinone seem to serve to transfer electrons to the electron transport chain terminal oxidase formed by DoxBCE.
PTM: The N-terminus is blocked.
Location Topology: Single-pass ... |
Q59971 | MSGEAPRVAVDPFSCPMMTMQRKPEVHDAFREAGPVVEVNAPAGGPAWVITDDALAREVLADPRFVKDPDLAPTAWRGVDDGLDIPVPELRPFTLIAVDGEDHRRLRRIHAPAFNPRRLAERTDRIAAIADRLLTELADSSDRSGEPAELIGGFAYHFPLLVICELLGVPVTDPAMAREAVGVLKALGLGGPQSAGGDGTDPAGDVPDTSALESLLLEAVHAARRKDTRTMTRVLYERAQAEFGSVSDDQLVYMITGLIFAGHDTTGSFLGFLLAEVLAGRLAADADGDAISRFVEEALRHHPPVPYTLWRFAATEVVIR... | Function: Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, DoxA catalyzes the C-13 hydroxylation of 13-deoxycarminomycin and ... |
P97207 | MSGKQSEEFKRTEKMTRMEYLFPVRFAVGWMFLDGGLRKAVLKPAKLDPNSASFVGGKLVNFLPHAGPFKGLLLMTLENRSLDVTFLTVFSYIEIIAGLFIIIGLLTRLAALGALAMSVGFAPAYWLGSTCEDEWQIGALLTAGSVTLMLTAAGRVWGLDYFLYKKLGDRPIANVPILKWIKLW | Function: TQO plays a role in sulfur oxidation and is proposed to couple sulfur oxidation to dioxygen reduction; caldariellaquinone or sulfolobus quinone seem to serve to transfer electrons to the electron transport chain terminal oxidase formed by DoxBCE.
Catalytic Activity: 6-decylubiquinone + 2 thiosulfate = 6-decyl... |
Q9UKG1 | MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGG... | Function: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism . Regulates signaling pathway leading to cell proliferation through interaction wi... |
Q8K3H0 | MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPISQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNGQLEEFLANIGTSVQNVRREMDGDVETMQQTIEDLEVASDPLYLPDPDPTKFPINRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGG... | Function: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism (By similarity) . Regulates signaling pathway leading to cell proliferation throug... |
Q8NEU8 | MPAVDKLLLEEALQDSPQTRSLLSVFEEDAGTLTDYTNQLLQAMQRVYGAQNEMCLATQQLSKQLLAYEKQNFALGKGDEEVISTLHYFSKVVDELNLLHTELAKQLADTMVLPIIQFREKDLTEVSTLKDLFGLASNEHDLSMAKYSRLPKKKENEKVKTEVGKEVAAARRKQHLSSLQYYCALNALQYRKQMAMMEPMIGFAHGQINFFKKGAEMFSKRMDSFLSSVADMVQSIQVELEAEAEKMRVSQQELLSVDESVYTPDSDVAAPQINRNLIQKAGYLNLRNKTGLVTTTWERLYFFTQGGNLMCQPRGAVAGG... | Function: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism . Regulates signaling pathway leading to cell proliferation through interaction wi... |
P0CN21 | MSDAFSTPADHALSHPELEAILENAQAGPSSIGDGAEGMSIEEAFEVDETVRRVLEGDYKTIGLQFPDELLPSSVSVYRAIQTRIAHTGAQAYVLADSTYGNCCPDVLSCLHLPADFLVHYGHACLTPTDALPVHYVFPRQKLDVKQAVESLLAASKNELDGDGRKGIVVVWDVSYDWLANDIRDTFSQDSTIQISFASIQKPTLASQKGLKDVKGKTPALRSVEPPQGLEMNDCVLWYIGEEGRSCMNLQMTHANNPLFIYSPSSQSVSPLHRTTSRLLSRRLFALHQALSADVFGLIVSNIGLASSKPLLAQLREDLK... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a ... |
A4QN59 | MTDAFSSSSEAVLQRSVTSTHSFHPSGDLLLLYQTPETCRFITSNHFKKVALQFPDELLPDAVRVSAEIEDKTKAKTYILGDTSYGSCCVDEVAAEHVGADCIVHYGSSCLSPCRRLPLLYVFGKRPIDVHQCASSFKELYPNLQSHIIVLFDVTYSHAIDDLRTLLCDVYPNVVVSRLKTDHSCGAELIQDSCVDLQSNDDGVIFKFGRQFRIKEGQTVNDYSIFYIGQEGLTLTNFMMSWNNCVFSSFNPETSTGRVESVQINKALMKRYYAIERAKDASVVGILVGTLGVANYLIIIEQLKDTIQRAGKKSYMFAMG... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph1 and ... |
Q6BMF6 | MTTEGLVVPALSTQQDDSTFEFDKVCSKTVVRSHLGLPNDATDDQVIKRIREYYNISEICNFLKQKVEGHELDMIPKYKHVTLQFPDSLICDSASIVHELQRELGLMPRTEDSSEVKCSADSCCKTGKVESPLSQKLWILADTSYSSCCIDEVAAGHVNSDLVIHFGDACLNVVESLPAAYVFGKPSLKLDSVITQFKEIYANRDSKILIMADAPHTQSLNQLYNILKPEYPNLAYADLYLNPSSNASIIGYDPCPSQSSILNVLNRTIIGLDNGDIDTDIDTILLEHDLFHIEVPAVPRLLQLTTRFQSVTTFEPKSGL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a ... |
B0G132 | MSAAPPPSIYTESFSTSSNNTTESESINVEETRENILSGFSFEEYFQVSESISVIIKNNFKKIALQLPDYLLWASSELSNKIQNSVPLEYGIKVFILGDTSYGSCCVDEVTSSHLKSDFIIHYGHSCLSPSSKIPVQYVFGKKKNFNVDKFSIELNKLVESKKEENFVIFYDLLYHHNRDSIENLYKNNDNIIVTNINNFNNIYLNNSFKNNKLNETQNCNNNYNNDCCGSDNNNNNNDSGCCGGNNNNNNNNSGCCQSQSQQQQQQNDCCQQKLNNEINNENDNNNEELISGRKIEFKNEKDIKKFNFIWIGEESLTLT... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph1 and ... |
Q4I5M4 | MASELSSAPVLSTPDDHILEVPAADSIPTSTLSDDALRTTYEIVRTADEIRAGGWKRIGLQFPDFMLVDAPRVVEALSKEINTHDQEEAKPERRIYVLADSSYSACCVDEIAAEHVSADVVVHYGRTCLSPTSHLPAIYVYTTHDLDYEVTINEIKKEFSDKTVKLVIMADLTYQNHVDKVVSLLKEQGYNDAVSTEVTRDPAALIPNRKILSDETHDDEHWKAYSIIHISDPPSALLLALYTRFASLHVLSTPSPALENPTMRTAGLLRRRFAKVLALASAGVIGILVNTLSVANYLSSINTLRERIARADKKSYTIVV... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a ... |
Q9BQC3 | MESMFSSPAEAALQRETGVPGLLTPLPDLDGVYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEETTGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACLSPPARPLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALEALATLLRPRYLDLLVSSPAFPQPVGSLSPEPMPLERFGRRFPLAPGRRLEEYGAFYVGGSKASPDPDLDPDLSRLLLGWAPGQPFSSCCPDTGKTQDEGARAGRLRARRRYLVERARDARVVGLLAGTLGVAQHREALAHLRNLTQAAGKRSYVLALG... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 . DPH1 and DPH2 transfer a... |
Q57907 | MLFKTIFYQKLQKKVTTLFNLETERVIREIENLNKNNPKVIFQAPEGLKLKVEKEIEKIKQYFKQKNINIEIYLWGNTCFGACDLIDNHVKNLNVDLIIHYGHEKLSYANPEIKTLFIPAYHIFNKDEEEKILNDIKNFIEKHKSGGKKVAIATTIQYKKLLKDFNPSIILGCRGEVKEGDVILFVGTGRFHPLMIAYKYQKEVFIYNPLSKCFDKISEEEINKFIKKRILAISKLLLNKPKKVGVVLSTKKGQCRKRVFDEIIKLLEENDVNYLPILVDNISPDILFYDVDCYIIVACPRIVLDDYILYKKPIYTPEEF... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imi... |
Q9CR25 | MESTFSSPAEAALQREAGVPGQFTPPEDLDRVYELERVTKFVCDLGCQRVTLQFPDQLLGDAGAVAARLEEVTGAKMFILGDTAYGSCCVDVLGAEQAGAQALVHFGPACLSPPASQLPITFVLGQRPVALELCAKAFEAQNPDPTAPVVLLSEPACAHALEPLAMLLLPKYQDLLISRPALPLPVGSPSSQPESLERFGRCFPLNPGRRLEEYGAFYVGASQASSDSSLDPDLSRLLLGWTPGRPFFSCCPDTGQTQDQGAKAGRLRARRLYLIERARDARVVGLLAGTLGVARHREALAHLRKLTEAAGKRSYVLAVG... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 . DPH1 and DPH2 transfer a... |
A7SKJ3 | MEVETTAKSYDVPASAFSESAVIDTHLDVPSTKTESIERMVEVYEIERSVQVITSSGFNKVALQFPDSLLADSASVARLIEQRASCKAFILADTSYGRHPPLPANKTFLKLYNVRICFKLLAFLHFSSCCVDEIAAEHADAELIIHYGQACLSQTKRLPVLYVFGKNPINVIECSQHFRQLYPDTGIRVLVFYDVVYNHCIGALDEALSPLYPNMTISTIAPEGLPSEPTSQQSSRNPQASDVEGMEVNQCNRRFGRDFTLAANSSISDYQIFYIGEQSLTLRNLMMTYNKCQFSTYDPITNESRRETLNVNKALMKRYH... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph1 and ... |
Q7S5C0 | MAGELNAAPVLSTPEDHLFEYAVVPTDDQTKAKSDDELRDIYEITRTAKEVGEGGWRRIGLQFPDHMLCDAPRVVQLLEAELASLPQPTVPTSTADLQSTATACPEPSTTNNGQCGRNVQQNGTGCGCGKQAPAPVESQPKARRVYVLADTSYSACCVDEIAAEHVNADVVVHYGRSCLSPTSRLPVIYVFTKHILDRDAALVKFEKEYPDKEAKVVLMADVTYQVHVPSLLSELQSGGYVNLLATEIVHNPMGRIPNRKVVDAQGKEVEISHGSETSTGLDLRDYSIFHISQPPTALLLALCSRVKNLYIFQTSSDSSS... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph-1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph-1 and dph-2 transfer... |
O58832 | MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFLHGEINYGACDPADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFEVSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAIDPYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRIVKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRKPVLTPKEVEILLGLREEYEF... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imi... |
Q10206 | MSFELSAPVPLSDNSEAILEKEIGETVKIEGDLVEVYEINRTVDFIKSGNYNSVALQFPDEHLADSGKVASILTNLVEANVQILADTNYGSCCVDEVAAEHMSADAIVHYGRACLSPTSRLPVLYVFGRLPINLHKLEKCLTIPLDQNILLVSDTRWYYAQDSILKSLKTLGYQNVYESHLKERIEPNLEEASTSYTIPGRTYSLPKSLSLQDMTLLYIGPDSPTLSSILMSHYSLVNQFLSFDPLSNKIVEESSFTGAKLRRRYALVQRCRDAGVIGIVIGTLGVHRYLHVLNQLRKMILNAGKKPYMLAVGKLNPAKL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a ... |
Q6DE00 | MAAALFSSNGEEAIGRNIDIGQVDIQSSPEKDLGEFYEIEKTVEFIQRNAAQKVALQFPDDLLLDSVKVARKLEEATGAKTYILGDTSYGSCCVDEVAAEHVKANVLVHYGRACLSPCCRLPVSYVFGRKAVNMDLCAEAFLSHYRDTESHVVVLSDVVYDHALGELAKRIRSAYPNVIFSKLTSCGETASPDEIVKFGRRFSPDLRLWPESYGIFYVGGEGSTLNNLMLTWPRCSFFSFNPFTGEGRTEGLHVNRALMIRFYLIERARDAHVFGILVGTLGVSDYLSALKHLKNIIHLAGKKSYMFSVGKLNPAKLANF... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph1 and ... |
Q6CGE7 | MSQAPVLSTEPEFETVAPLVRETPSNDYLNKYYCLPQLTEYLNSHEYKSIALQFPANDVADSALVVRLLKQTVDPSISLFILADTNYSPCCVDVVGANHIKADLVVHFGSACLNPVTMPVVYVFCNPEIDVKVMVDQLTEQIKDAEQPNILLDSDSKYYPEMPTMFKALREAFPDKIIVRSFIPNPQETLGLSEEETKPDAEEGYLYRRTHDDLDPQETMLIYVGTPSSSLALHYSTRFGATAYFNPVSGQAETPKTAIMKRYRYMNMARAAQTIGILINSLSMSETKEMSKKLQKAIAESGKKSYTFVVGKPNVAKLAN... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a ... |
P32461 | MEVAPALSTTQSDVAFQKVETHEIDRSSYLGPCYNSDELMQLISAYYNVEPLVGYLEQHPEYQNVTLQFPDDLIKDSSLIVRLLQSKFPHGKIKFWVLADTAYSACCVDEVAAEHVHAEVVVHFGDACLNAIQNLPVVYSFGTPFLDLALVVENFQRAFPDLSSKICLMANAPFSKHLSQLYNILKGDLHYTNIIYSQVNTSAVEEKFVTILDTFHVPEDVDQVGVFEKNSVLFGQHDKADNISPEDYHLFHLTTPQDPRLLYLSTVFQSVHIFDPALPGMVTGPFPSLMRRYKYMHVARTAGCIGILVNTLSLRNTRET... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 . DPH1 and DPH2 transfer a... |
P74933 | MQEKKTLYLLDAYGLIYRSYHAFARAPLINDSGANVSAVYGFFRSLHTLLCHYRPRYFVAVFDSLTPTFRHVQYPAYKAKRDKTSAELYAQIPLIEEILCALGITVLRHDGFEADDLIATLAKRVAAEHCHVVIISSDKDVLQLVCDTVQVLRLDIDHKWTCCDAAYVQQRWTVMPTQLLDLFSLMGDSSDNVPGVRGIGPKTAAHLLHCFGTLDGIYRHTYSLKEALRTKIVCGKKDAFFSRSLIELRDDVPCVFSLEDSCCIPLDVTSAARIFVREGLHALAQQYRACVQEIDTEATNDTLQMTESSVLTSGRCANEC... | Function: In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 112217
Sequence Length: 997
EC: 2.7.7.7
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A0A0A8JA06 | MINGLIQPKGSVSKETNKNSIALSLGLKFSEVEYLSTEILIDTYIVVFDPISEMVFYVGNAKGNPQTWNLNSDGNLILTTDFSTYTLLKIGLSNPDTSLKIGYQRKKINDSLSSIESVAGYMNSNFVSIMEFQHLITSKPNLNDMETWDWSPALDAAISYVQSYIPQTAVNSQMYGVMPIVFPPGVFQYSTEMKFTKYLNSTGSLSTCYTLIGSGMTSTVLQPITQGQNAFTATQCKINLINIGFRSGASYQTGAVLGSSTAWLPVVHSNWRCVGFSGFARGVVANLLFDSTFEDIFIQNISNMQSTSDVSYGFTFEVYT... | Function: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K35-type polysaccharides of Klebsiella pneumoniae capsule .
PTM: Proteolytic cleavage and release of the chaper... |
P21189 | MAQAGFILTRHWRDTPQGTEVSFWLATDNGPLQVTLAPQESVAFIPADQVPRAQHILQGEQGFRLTPLALKDFHRQPVYGLYCRAHRQLMNYEKRLREGGVTVYEADVRPPERYLMERFITSPVWVEGDMHNGTIVNARLKPHPDYRPPLKWVSIDIETTRHGELYCIGLEGCGQRIVYMLGPENGDASSLDFELEYVASRPQLLEKLNAWFANYDPDVIIGWNVVQFDLRMLQKHAERYRLPLRLGRDNSELEWREHGFKNGVFFAQAKGRLIIDGIEALKSAFWNFSSFSLETVAQELLGEGKSIDNPWDRMDEIDRR... | Function: Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 90053
Sequence Length: 783
EC: 2.7.7.7
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Q67QM6 | MRTDLWVIHLDMDAFFASIEQRDNPRLRGKPVIVGGSPNSRGVVSTCSYEARRFGVRSAMPSREALRLCPQAVFIRPNHAKYAAVGRQVRAIMRRFTDVIEPLSIDEAFLDVSGQDAVRVARELKEAIRAELHLTGSAGVSYCKFLAKLASDMQKPDGLTVITWERAQELLPTLPVRKLWGVGPASEQALHALGIYTCGDLLAYDPDTLRKHFGKRADELILLARGIDPRPVVPYREAKSIGEENTFPVDQTDREYLSRLLERYADNLAEELRRQGLYARTVTVKIKWNVFVEGGPKGGDFLQITRSQTLPMPTNDARTI... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q07635 | MGRTQPSYTMAVNRELEKLERIIERLHSPILSLLLERVKEKVRYTQSASYDELVDPYNLVYFALIWALAEECEKMEEYVLDAYPIKGGVKLFLSNFKEKTIRTTFPVYTITDNPDIVLQHPEVRYYEKEKWKTLDGKEVKVYRFEVESLDAYYYMRKRLNVVNETPTVLSQTLYRLGIKPFRRFRSSDDEFPKVTIARVVPLDWYGESLKGKVFEVKINNEVRRFYEKPEVEVDIAECLGEACNYVKSNVKIRIEKKRSPVSAKGLIEWSFISLTPIHEIAYATIGKVLTINEAWVAFKRRIIIPKVVPRVEKLRRLEDI... | Function: This polymerase is devoid of exonuclease activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 73535
Sequence Length: 626
EC: 2.7.7.7
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P0DTK4 | MSYLQPPLFTTVSSDWVAPDLSTLPSWEGAKRVAIDCETRDPDLRKLGPGAGRRPNSYITGISFAIEDGPGGYLPIRHEGGGNLPLEGVLAYLRAQAKVFTGDLVGANLPYDLDFLAGDGIEFERVRYFRDIQIADPLICELHDSYSMQAIAERWGFHGKDEALLRAAAVDYGIDPKKDMWMLPAKFVGKYAEEDTRLPLNILRRQEREIDEQDLWGVYNLESKLLPILTGLRRRGVRIDCDRLDMIERWALEKETEALAQVRSITGHRIAVGDVWKPEVIAPALEHIGIKLNKTSQGKPNIDKELLGSIDHPVADLLER... | Function: DNA polymerase that replicates the viral genomic DNA (Probable). Also incorporates 5-hydroxymethyl-2'-deoxyuridine (5-hmdU) instead of dTMP into DNA during replication, as an early step in the pathway of thymidine hypermodifications of the viral genome . As a final result of the pathway of hypermodification, ... |
Q6DRD3 | SKRKAPQESLNEGITDFLVELANYERNVNRAIHKYNAYRKAASVIAKYPQKIKSGTEAKKLDGVGAKIAEKIDEFLTTGKLRKLEKIRNDDTSSSINFLTRVTGIGPAAARKFFDEGVRNLEDLKKIEHKLNHHQQIGLKYFEEFEKRIPRSEMQKMEALILKELDIVDPEYIGTICGSYRRGAESSGDIDILLTHPDFTSQSEKQPKLLHAVVDHLESIGFITDTLSKGDTKFMGVCQLQKEKEEEEEESLHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRTHALEKGFTLNEYTIRPLGVTGVAGEPLLVDSEKDI... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribo... |
Q8N608 | MNQTASVSHHIKCQPSKTIKELGSNSPPQRNWKGIAIALLVILVVCSLITMSVILLTPDELTNSSETRLSLEDLFRKDFVLHDPEARWINDTDVVYKSENGHVIKLNIETNATTLLLENTTFVTFKASRHSVSPDLKYVLLAYDVKQIFHYSYTASYVIYNIHTREVWELNPPEVEDSVLQYAAWGVQGQQLIYIFENNIYYQPDIKSSSLRLTSSGKEEIIFNGIADWLYEEELLHSHIAHWWSPDGERLAFLMINDSLVPTMVIPRFTGALYPKGKQYPYPKAGQVNPTIKLYVVNLYGPTHTLELMPPDSFKSREYY... | Function: Promotes cell surface expression of the potassium channel KCND2 . Modulates the activity and gating characteristics of the potassium channel KCND2 . Has no dipeptidyl aminopeptidase activity .
PTM: N-glycosylation is important for cell surface expression, specially at Asn-257, which is crucial.
Location Topol... |
B2RID1 | MKKRLLLPLFAALCLSQIAHADEGMWLMQQLGRKYAQMKERGLKMKEYDLYNPNGTSLKDAVVLFDGGCTGEVVSDRGLVLTNHHCGYDMIQAHSTLEHNYLENGFWAMREADELPNKDISVVFIDKIEDVTDYVKKELKAIKDPNSMDYLSPKYLQKLADKKAGKNFSAKNPGLSVEIKAFYGGNLYLMFTKKTYTDVRLVGAPPSSIGKFGADTDNWIWPRHTGDFSIFRIYADKNGNPAPYSEDNVPLKPKRFFNISLGGVQENDYAMIMGFPGTTHRYFTASEVDEWKSIDNDIRIRMRDIRQGVMLREMLADPQI... | Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as ... |
Q9UUA6 | MEAVGKHVKLFWNVYSDYAVLIAISLSYFVFDVLMLPFTRQFSLEDITISHPFALHEQVPTKYLGIICVFFPALVLYGFGKLRNNSLLFWKSLMGLLYSTMVCGLCVSLLKNAVGRPRPDFLARCQPFESTPKTGLVDVLSCSVPWSDKVLQDGFRSFPSGHTSFSFAGLGFLAIFLAGQLKMFRNKTSSWKVVVPLVPLSIASWIGLSRSQDYRHHKEDIAVGALFGFAIAYVVYRQLFPPLDHHNADILYVQAELDEGYTNVHSAGNSSATNAEQMV | Function: Catalyzes the dephosphorylation of diacylglycerol phosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG).
Catalytic Activity: a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate
Location Topology: Multi-pass m... |
Q05521 | MNRVSFIKTPFNIGAKWRLEDVFLLIIMILLNYPVYYQQPFERQFYINDLTISHPYATTERVNNNMLFVYSFVVPSLTILIIGSILADRRHLIFILYTSLLGLSLAWFSTSFFTNFIKNWIGRLRPDFLDRCQPVEGLPLDTLFTAKDVCTTKNHERLLDGFRTTPSGHSSESFAGLGYLYFWLCGQLLTESPLMPLWRKMVAFLPLLGAALIALSRTQDYRHHFVDVILGSMLGYIMAHFFYRRIFPPIDDPLPFKPLMDDSDVTLEEAVTHQRIPDEELHPLSDEGM | Function: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with LPP1, regulates intracellular DGPP and PA levels, which are phospholipid molecules believed to play a signaling role in stress response. ... |
Q9UHL4 | MGSAPWAPVLLLALGLRGLQAGARRAPDPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGNEGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTELLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPHLVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQIKDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSE... | Function: Plays an important role in the degradation of some oligopeptides.
PTM: N-glycosylated.
Catalytic Activity: Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.
Sequence Mass (Da): 54341
Sequence Length: 492
Subcellular... |
Q9ET22 | MNFHPCYPVDHGVPSWILVLLLSLGLCNLQARADRVLDPDFHENYFEQYMDHFNFESFGNKTFGQRFLVSDKFWKMGEGPIFFYTGNEGDIWSFANNSGFMVELAAQQEALLVFAEHRYYGKSLPFGVQSTQRGYTQLLTVEQALADFAVLLQALRQDLGVHDAPTIAFGGSYGGMLSAYMRMKYPHLVAGALAASAPVVAVAGLGDSYQFFRDVTADFYGQSPKCAQAVRDAFQQIKDLFLQGAYDTISQNFGTCQSLSSPKDLTQLFGFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCQRLLNEGQRIMGLRALA... | Function: Plays an important role in the degradation of some oligopeptides.
Catalytic Activity: Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.
Sequence Mass (Da): 56254
Sequence Length: 506
Subcellular Location: Lysosome
E... |
P83681 | FANLVEKTTYFSDKGEFEGFVAMVNKNVTLGNVIPASYKLQVYKTYDATHEGLIQSFVENGTEEVPLDGXEXX | Cofactor: Binds 1 zinc ion per subunit.
Function: Degrades neuropeptide proctolin (RYLPT) by cleavage between Tyr and Leu residues.
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Location Topology:... |
Q557H1 | MSVPSSVIENHLVPKEIPVYRLNARESFNLLTEKEQLYAHHISVACWWGSKICLGQTSIESGPIFNLFQNLFSIQNLKSTVVPNIVSEEEYSDLLSYAATFYGNMGNYLSFGDSKFIPRISKEKLQLIINKVNDNKVNEYWGKCSELMYSLDKQVRELGIDGNGISTYYSPNITKVEIEKVQKFMDSKSISPYNTRLFKVSENNYNLLIASASTSTPTVSHQFDGYTINIVYGDWNKNLTKVVDNLKLALPYAANENQTNMLKKYIDSFYSGSIDDHKDSQRWWIKDISPAVETNIGFIESYRDPYGVRGEWEGFVSMVN... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Sequence Mass (Da): 78274
Sequence Length: 691
Subcellular Location: Cytoplasm
EC: 3.4.14.4
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Q9VHR8 | MFWLRGLQRSRQQLNRLCHFRSRLNYGTSPSIRSVQPSISRSLGFCSSLVRYSCSTNLPQPAEMASKTAHFVLPNTQPIADLDCKSAFENLTEKEKLYAHHFSQASWDGGLIALIQSSPEAPLIFSLLHRIFLAEKIPVLRAKALEAGVSADDFTAFLVYACGVFANAGNYKGMGDSKIVPNLSEKQFETIVKASAAYSDEPRVGKIFEKVKNLIYALESRNEILGFAPDGITTYWSDNCTKEDSEIVNAWLTSKRIEPYMCRTFKIVENGQTVYDVKLGSVAESTQDGITLPLEEYNGNKFRVTRGDYQKLLQRVNQHL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Degrades neuropeptide proctolin (RYLPT) by cleavage between Tyr and Leu residues.
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Location Topology:... |
Q08FX8 | MEAAIEFDEIVKKLLNIYINDICTMGEKRLLNNYEKSILDRIYKSCEYIKKNYELDFNSMYNQININDITTSDIKSKIIESLLIDSRPSVKLATLSFISLIAEKWGEKNRTKIMEILSNEIVEKISNNGKDFIDFIDRDDDDIVDDYVLITNYLKITIFGAILGITAYYICKYLLKSIF | Function: Plays a role in the inhibition of host apoptosis by sequestering and inactivating several proapoptotic BCL-2 proteins, including BAK1 and BAX. Prevents the conformational activation of both of them.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20874
Sequence Length: 179
Subcellular Loca... |
P34413 | MAKKPKNSPEKSKYSSDTSSSLYSQTWLASVVIIGLLVGYINYQHVYTLFENDKHFSHLADFEREMAYRTEMGLYYSYYKTIINAPSFLEGVQEITHDTVTEHGHEINTLNRFNLYPEVILAFLYRPFRAFAKSANWQIELCWQVNRGELRPVESCEGIGNPHYFYITGVFIVAGTVASSIFYLGVLVSDSIFGGFLSVLCFAFNHGEATRVQWTPPLRESFAFPFIIGHIAILTFVIKYKKSGHSMILLLTSMAVPALLFWQFTQFAFFTQICSIFLAFSLDLIPFSTAKTVIHSHIISFLIGFLLLFGNEMMITALYF... | Function: C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins such as unc-5 and mig-21. Mediates the attachment of alpha-mannose in C-C linkage to the C2 of the indole ring of tryptophan. C-mannosylation takes place in the endoplasmic reticulum and frequently found in thrombosp... |
Q9VWR8 | MREPNLYVILSHALIGCGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQRFYVLPELVTAYFFHVVRSGFNPMVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYGVISYLMFHSFVAKIYERPLARENFAFPFIFLQMFYLCICIGRIIHRQRHTSRMFMIFAMSLFTACALLSWQFSTFIFTTQILIMMTSWNASALPTALVNAFVLDYSLSHLLGHALAFVMSHGNSQLLLTWQLSISLFLFLITMVRQLRHVRSRRLGHAQDLLNGD... | Function: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101097
Sequence Length: 872
Subcellular Location: Membrane
EC: 2.4.1.-
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P61168 | MDPLNLSWYDDDLERQNWSRPFNGSEGKPDRPHYNYYAMLLTLLIFIIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMIAIVWVLSFTISCPLLFGLNNTDQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRKRRKRVNTKRSSRAFRANLKTPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRMDAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSNPD... | Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 .
PTM: Palmitoylated. Palmitoylation which is required for proper localizat... |
Q5IS72 | MAPLSQLSGHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYMVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGV... | Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation (By similarity).
PTM: Phosphorylated by GRK4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44237
Sequence Length: 400
Subcellular Location: Cell membrane
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P19020 | MAPLSQISTHLNSTCGAENSTGVNRARPHAYYALSYCALILAIIFGNGLVCAAVLRERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPSICSISNPDFVIYSSVVSFYVPFGVTVLVYARIYIVLRQRQRKRILTRQNSQCISIRPGFPQQSSCLRLHPIRQFSIRARFLSDATGQMEHIEDKQYPQKCQDPLLSHLQPPSPGQTHGGLKRYYSICQDTALRHPSLEGGA... | Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation (By similarity).
PTM: Phosphorylated by GRK4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49516
Sequence Length: 446
Subcellular Location: Cell membrane
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P21917 | MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVATERALQTPTNSFIVSLAAADLLLALLVLPLFVYSEVQGGAWLLSPRLCDALMAMDVMLCTASIFNLCAISVDRFVAVAVPLRYNRQGGSRRQLLLIGATWLLSAAVAAPVLCGLNDVRGRDPAVCRLEDRDYVVYSSVCSFFLPCPLMLLLYWATFRGLQRWEVARRAKLHGRAPRRPSGPGPPSPTPPAPRLPQDPCGPDCAPPAPGLPRGPCGPDCAPAAPSLPQDPCGPDCAPPAPGLPPDPCGSNCAPPDAVRAAA... | Function: Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs . Agonist binding triggers signaling via... |
Q6TLJ0 | MGNRSAADADGLLAGRGPGTGGGAGSPGAAAALVGGVLLIGAVLAGNALVCVSVAAERALQTPTNYFIVSLAAADLLLALLVLPLFVYSEVQGGVWQFSPGLCDALMAMDVMLCTASIFNLCAISADRFVAVAVPLSYNRQSGGGRQLLLIGATWLLSAAVAAPVLCGLNDARGRDPAVCRLEDRDYVVYSSVCSFFLPCPVMLLLYWATFRGLRRWEAARRTKLHGRRPRRPSGPGPPPPEAVETPEAPEAIPTPDATLAEPALPASEERRAKITGRERKAMRVLPVVVGAFLVCWTPFFVVHITGALCPACAVPPRLV... | Function: Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs. Agonist binding triggers signaling via ... |
P30729 | MGNSSATGDGGLLAGRGPESLGTGTGLGGAGAAALVGGVLLIGMVLAGNSLVCVSVASERILQTPTNYFIVSLAAADLLLAVLVLPLFVYSEVQGGVWLLSPRLCDTLMAMDVMLCTASIFNLCAISVDRFVAVTVPLRYNQQGQCQLLLIAATWLLSAAVAAPVVCGLNDVPGRDPTVCCLEDRDYVVYSSICSFFLPCPLMLLLYWATFRGLRRWEAARHTKLHSRAPRRPSGPGPPVSDPTQGPLFSDCPPPSPSLRTSPTVSSRPESDLSQSPCSPGCLLPDAALAQPPAPSSRRKRGAKITGRERKAMRVLPVVV... | Function: Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs (By similarity). Agonist binding trigger... |
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