wanglab/gogpt-training-data huggingface dataset:
Protein: GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Protein O-fucosyltransferase 2) (S7WCF5)
Organism: Toxoplasma gondii (strain ATCC 50853 / GT1)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates microneme protein MIC2 and may play a role in its stabilization. Probably by regulating protein O-fucosylation, may play a role in tachyzoite adhesion to and/or invasion of host cells; however, POFUT2 involvement in adhesion/invasion is controversial.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30538131}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MHCQLGGQARALIFLMFESCRNSWHVSPWSSVPFLPSPCLFFSFSALPFLHPLSQLIACRGSSATWLFPVSSGTLVLRYALAASPPRGTMRPSTNPRTAEEGRPWLIHATQTGPQTASVLSLFPAVNAGFFSACRQHRGGRPPCLLNHRRLLLGLVSVLTVFLSCLPFTNATVSPAALQDVCYAFGNISRKLSSFLVPSRVTCPRGATPLSGVEAQDSLEHPEIPDFRFLVYDVKNGEGFHLQKEVIYRVALVISLLNARSAQQGRMTDVHTAEKAREDRGHPQASHMLCASSSFSHACSARSTFPFFPMWVLVLPPWCRLAHWHFSEETITAMAENSWLKHVRWGTFFDFQDLGERLPVMEYEDFLTYQLMRPDPWGERRQRKEKQTTPVELDVVLSVRFSSTPSSRSLPFCACLSSRASEIADEQAQRDDVCCNVNDLPGCPQIHAALTPQERQRAPAQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEEAKVSDTWSGVSLWLAGFCETVRALEMWCASLYIADAPRIADLLWRSVAERPPGAIQTVWLKFGENLLVPWPDVLLDAHLLDMLHVHPKLRQIGDLFINKFLSNRDKTETGKGERASTEGGTEGDENLAKHGYIAAHLRRTDFLYLKRSVPLQRAAAYLVSRMKEHGVFKAFICTDGSEDEKRELRDAVRRVGDAASSSPYTVVFFDLPTVRRLMIKTLEASSHVSDDGSFHDLKAVETPGYSGPNHISLLLHPGITALIEVWIAARAAYFIGTKDSRFSQAIRWERHLMGHPLDSSLEVFCVDSSPDQTGGQAQGKCFATKSHDPPEGRSRSELRRKYWPSLDPSSTL
Protein: Transmembrane protein C16orf54 (Q6UWD8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Aspartate beta-hydroxylase domain-containing protein 1
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MPLTPEPPSGRVEGPPAWEAAPWPSLPCGPCIPIMLVLATLAALFILTTAVLAERLFRRALRPDPSHRAPTLVWRPGGELWIEPMGTARERSEDWYGSAVPLLTDRAPEPPTQVGTLEARATAPPAPSAPNSAPSNLGPQTVLEVPARSTFWGPQPWEGRPPATGLVSWAEPEQRPEASVQFGSPQARRQRPGSPDPEWGLQPRVTLEQISAFWKREGRTSVGF
Protein: Anamorsin (Cytokine-induced apoptosis inhibitor 1) (Fe-S cluster assembly protein DRE2 homolog) (Q6FI81)
Organism: Homo sapiens (Human)
Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:16957168, ECO:0000269|PubMed:29848660}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:16957168}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:21700214}.
Interaction partners:
- NADPH-dependent diflavin oxidoreductase 1
- Glutaredoxin-3
- Cytosolic Fe-S cluster assembly factor NUBP1
- BolA-like protein 1
- Cytosolic iron-sulfur assembly component 3
- BolA-like protein 2
- Cytosolic Fe-S cluster assembly factor NUBP2
- Probable cytosolic iron-sulfur protein assembly protein CIAO1
- MMS19 nucleotide excision repair protein homolog
- Cysteine desulfurase
Sequence:
MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMDLIDSDELLDPEDLKKPDPASLRAASCGEGKKRKACKNCTCGLAEELEKEKSREQMSSQPKSACGNCYLGDAFRCASCPYLGMPAFKPGEKVLLSDSNLHDA
Protein: Sorbitol dehydrogenase (SDH) (EC 1.1.1.-) (Polyol dehydrogenase) (Protein tms1) (P36624)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is active with D-sorbitol (D-glucitol) as substrate, leading to the C2-oxidized product D-fructose (By similarity). Suppresses growth arrest induced by a p53 tumor mutant in fission yeast.
Interaction partners:
- Xylulose kinase
- Alcohol dehydrogenase 4
- Multifunctional tryptophan biosynthesis protein
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MAPAEKAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAAKENESLPDYAQRYKQAIIEKYGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVIIGGPDA
Protein: Amyloid beta precursor protein binding family B member 2 (Amyloid-beta (A4) precursor protein-binding family B member 2) (Protein Fe65-like 1) (Q92870)
Organism: Homo sapiens (Human)
Function: Plays a role in the maintenance of lens transparency, and may also play a role in muscle cell strength (By similarity). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning (By similarity). Activates transcription of APP.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14527950}. Golgi apparatus {ECO:0000269|PubMed:14527950}. Early endosome {ECO:0000269|PubMed:14527950}.
Interaction partners:
- Amyloid-beta precursor protein
- Amyloid beta precursor like protein 1
- Amyloid beta precursor like protein 2
- Amyloid beta precursor protein binding family B member 1
- Amyloid-beta A4 precursor protein-binding family A member 2
- Amyloid-beta A4 precursor protein-binding family A member 1
- Epidermal growth factor receptor
Sequence:
MSEVLPADSGVDTLAVFMASSGTTDVTNRNSPATPPNTLNLRSSHNELLNAEIKHTETKNSTPPKCRKKYALTNIQAAMGLSDPAAQPLLGNGSANIKLVKNGENQLRKAAEQGQQDPNKNLSPTAVINITSEKLEGKEPHPQDSSSCEILPSQPRRTKSFLNYYADLETSARELEQNRGNHHGTAEEKSQPVQGQASTIIGNGDLLLQKPNRPQSSPEDGQVATVSSSPETKKDHPKTGAKTDCALHRIQNLAPSDEESSWTTLSQDSASPSSPDETDIWSDHSFQTDPDLPPGWKRVSDIAGTYYWHIPTGTTQWERPVSIPADLQGSRKGSLSSVTPSPTPENEKQPWSDFAVLNGGKINSDIWKDLHAATVNPDPSLKEFEGATLRYASLKLRNAPHPDDDDSCSINSDPEAKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPIVSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERKNAKALACSSLQERANVNLDVPLQVDFPTPKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMGVGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCLVARPPSQKVRPPPPPADSVTRRVTTNVKRGVLSLIDTLKQKRPVTEMP
Protein: Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease) (Pr); Assembly protein (AP) (Capsid assembly protein)] (P24433)
Organism: Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B lymphotropic virus)
Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular location: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.
Interaction partners:
Sequence:
MSKVWVGGFLCVYGEEPSEECLALPRDTVQKELGSGNIPLPLNINHNEKATIGMVRGLFDLEHGLFCVAQIQSQTFMDIIRNIAGKSKLITAGSVIEPLPPDPEIECLSSSFPGLSLSSKVLQDENLDGKPFFHHVSVCGVGRRPGTIAIFGREISWILDRFSCISESEKRQVLEGVNVYSQGFDENLFSADLYDLLADSLDTSYIRKRFPKLQLDKQLCGLSKCTYIKASEPPVEIIVAATKVAGDQVQLTTEPGSELAVETCDVPVVHGNYDAVESATATTAMSNQNLPNTTPLLSSPPFSDCVFLPKDAFFSLLNVTTGQQPKIVPPVSVHPPVTEQYQMLPYSESAAKIAEHESNRYHSPCQAMYPYWQYSPVPQYPAALHGYRQSKTLKKRHFQSDSEDELSFPGDPEYTKKRRRHRVDNDDDKEMAREKNDLRELVDMIGMLRQEISALKHVRAQSPQRHIVPMETLPTIEEKGAASPKPSILNASLAPETVNRSLAGQNESTDLLKLNKKLFVDALNKMDS
Protein: Histidinol-phosphate aminotransferase (HspAT) (EC 2.6.1.9) (Imidazole acetol-phosphate transaminase) (P9WML7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Histidinol dehydrogenase
- Phosphoribosyl isomerase A
- Imidazole glycerol phosphate synthase subunit HisH
- Phosphoribosyl-AMP cyclohydrolase
- Imidazole glycerol phosphate synthase subunit HisF
- Prephenate dehydrogenase
- ATP phosphoribosyltransferase
- Histidinol-phosphatase
- Aromatic amino acid aminotransferase
Sequence:
MTRSGHPVTLDDLPLRADLRGKAPYGAPQLAVPVRLNTNENPHPPTRALVDDVVRSVREAAIDLHRYPDRDAVALRADLAGYLTAQTGIQLGVENIWAANGSNEILQQLLQAFGGPGRSAIGFVPSYSMHPIISDGTHTEWIEASRANDFGLDVDVAVAAVVDRKPDVVFIASPNNPSGQSVSLPDLCKLLDVAPGIAIVDEAYGEFSSQPSAVSLVEEYPSKLVVTRTMSKAFAFAGGRLGYLIATPAVIDAMLLVRLPYHLSSVTQAAARAALRHSDDTLSSVAALIAERERVTTSLNDMGFRVIPSDANFVLFGEFADAPAAWRRYLEAGILIRDVGIPGYLRATTGLAEENDAFLRASARIATDLVPVTRSPVGAP
Protein: Allatostatin-A receptor (BAR) (Q8WPA2)
Organism: Bombyx mori (Silk moth)
Function: Acts as a receptor for A-type allatostatin neuropeptide hormones.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MESTEDEFYTICLNLTAEDPSFGNCNYTTDFENGELLEKVVSRVVPIFFGFIGIVGLVGNALVVLVVAANPGMRSTTNLLIINLAVADLLFVIFCVPFTATDYVMPRWPFGDWWCKVVQYFIVVTAHASVYTLVLMSLDRFMAVVHPIASMSIRTEKNALLAIACIWVVILTTAIPVGICHGEREYSYFNRNHSSCVFLEERGYSKLGFQMSFFLSSYVIPLALISVLYMCMLTRLWKSAPGGRVSAESRRGRKKVTRMVVVVVVVFAVCWCPIQIILLVKALNKYHITYFTVTAQIVSHVLAYMNSCVNPVLYAFLSENFRVAFRKVMYCPPPYNDGFSGRPQATKTTRTGNGNSCHDIV
Protein: Neurocan core protein (Chondroitin sulfate proteoglycan 3) (P55066)
Organism: Mus musculus (Mouse)
Function: May modulate neuronal adhesion and neurite growth during development by binding to neural cell adhesion molecules (NG-CAM and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O14594}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase zeta
- Versican core protein
- Brevican core protein
- Aggrecan core protein
- Neural cell adhesion molecule L1
- Chondroitin sulfate proteoglycan 5
- Decorin
- Glypican-1
- Syndecan-3
- Receptor-type tyrosine-protein phosphatase S
Sequence:
MGAGSVWASGLLLLWLLLLVAGDQDTQDTTATEKGLRMLKSGSGPVRAALAELVALPCFFTLQPRLSSLRDIPRIKWTKVQTASGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYPRHRANATLLLGPLRASDSGLYRCQVVKGIEDEQDLVTLEVTGVVFHYRAARDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRSYGRRDPQELYDVYCFARELGGEVFYVGPARRLTLAGARAQCQRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGFPAPGARFDAYCFRAHHHTAQHGDSEIPSSGDEGEIVSAEGPPGRELKPSLGEQEVIAPDFQEPLMSSGEGEPPDLTWTQAPEETLGSTPGGPTLASWPSSEKWLFTGAPSSMGVSSPSDMGVDMEATTPLGTQVAPTPTMRRGRFKGLNGRHFQQQGPEDQLPEVAEPSAQPPTLGATANHMRPSAATEASESDQSHSPWAILTNEVDEPGAGSLGSRSLPESLMWSPSLISPSVPSTESTPSPKPGAAEAPSVKSAIPHLPRLPSEPPAPSPGPSEALSAVSLQASSADGSPDFPIVAMLRAPKLWLLPRSTLVPNMTPVPLSPASPLPSWVPEEQAVRPVSLGAEDLETPFQTTIAAPVEASHRSPDADSIEIEGTSSMRATKHPISGPWASLDSSNVTMNPVPSDAGILGTESGVLDLPGSPTSGGQATVEKVLATWLPLPGQGLDPGSQSTPMEAHGVAVSMEPTVALEGGATEGPMEATREVVPSTADATWESESRSAISSTHIAVTMARAQGMPTLTSTSSEGHPEPKGQMVAQESLEPLNTLPSHPWSSLVVPMDEVASVSSGEPTGLWDIPSTLIPVSLGLDESVLNVVAESPSVEGFWEEVASGQEDPTDPCENNPCLHGGTCHTNGTVYGCSCDQGYAGENCEIDIDDCLCSPCENGGTCIDEVNGFICLCLPSYGGSLCEKDTEGCDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRAGHLTSVHSPEEHKFINSFGHENSWIGLNDRTVERDFQWTDNTGLQYENWREKQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKGTVLCGPPPAVENASLVGVRKIKYNVHATVRYQCDEGFSQHRVATIRCRNNGKWDRPQIMCIKPRRSHRMRRHHHHPHRHHKPRKEHRKHKRHPAEDWEKDEGDFC
Protein: Inner membrane transport permease YadH (P0AFN6)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized ABC transporter ATP-binding protein YadG
Sequence:
MMHLYWVALKSIWAKEIHRFMRIWVQTLVPPVITMTLYFIIFGNLIGSRIGDMHGFSYMQFIVPGLIMMSVITNAYANVASSFFGAKFQRNIEELLVAPVPTHVIIAGYVGGGVARGLFVGILVTAISLFFVPFQVHSWVFVALTLVLTAVLFSLAGLLNGVFAKTFDDISLVPTFVLTPLTYLGGVFYSLTLLPPFWQGLSHLNPIVYMISGFRYGFLGINDVPLVTTFGVLVVFIVAFYLICWSLIQRGRGLRS
Protein: acid phosphatase (EC 3.1.3.2) (Q8I0P9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH19849p
- Arginine phosphatase
- FAD synthase
- Putative riboflavin kinase
- Low molecular weight phosphotyrosine protein phosphatase 1
- FAD synthase
- Low molecular weight phosphotyrosine protein phosphatase 2
Sequence:
MFSRSRCGSLVTSVARKMWNHPSQRWLILICVICLLSFALANSLHGYANAEGHPVEISATLPGQLKFVHVIYRHGDRTPVDPYPTDPWGDRKFWPTGWGDLTNLGKQEHYDLGKWLRNRYSNLLPPIYSNENIYVQSTDVDRTLMSAQSNLAGLYEPQGEDIWNTDINWQPIPIHTSPEREDPILAAKAPCPAYDYELASLESSPEFKALTEKHRNLFAYLSEKGGRPVKTFIDAQYLNNTLFIENLYNMTLPKWTKMVYGREELTYVSNFAFAISSYTRKLARLKAGPLLKDIFQRFKEKSSGSLKPDRSMWVYSAHDTTVASVLNALKLFELHSPPYTACIMMELRVDETNTPLVSIFYKNTTAEPLPLDIPGCGPSCPLTKLMNIYEDVLPVDWERECKLSTMMMTYEEANLGTATGILILIVIALLFASYGLMIYYRRRNYKLYSSYSQMA
Protein: Phosphatidylinositol-glycan biosynthesis class F protein (PIG-F) (GPI11 homolog) (Q07326)
Organism: Homo sapiens (Human)
Function: Involved in GPI-anchor biosynthesis. It acts through the transfer of ethanolamine phosphate to the third mannose of GPI.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI-anchor transamidase
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI ethanolamine phosphate transferase 2, catalytic subunit
- GPI alpha-1,2-mannosyltransferase 3
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase component GPAA1
- GPI-anchor transamidase component PIGU
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Sequence:
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYLVVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILSTFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERPWQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
Protein: Calcium-activated potassium channel subunit beta-1 (BK channel subunit beta-1) (BKbeta) (BKbeta1) (Hbeta1) (Calcium-activated potassium channel, subfamily M subunit beta-1) (Calcium-activated potassium channel subunit beta) (Charybdotoxin receptor subunit beta-1) (K(VCA)beta-1) (Maxi K channel subunit beta-1) (Slo-beta-1) (Slo-beta) (Q16558)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Calcium-activated potassium channel subunit alpha-1
- Potassium channel subfamily U member 1
- Calcium-activated potassium channel subunit beta-4
- Leucine-rich repeat-containing protein 26
- Small conductance calcium-activated potassium channel protein 1
- Intermediate conductance calcium-activated potassium channel protein 4
- Small conductance calcium-activated potassium channel protein 2
- Small conductance calcium-activated potassium channel protein 3
- Calcium-activated potassium channel subunit beta-2
- cGMP-dependent protein kinase 1
Sequence:
MVKKLVMAQKRGETRALCLGVTMVVCAVITYYILVTTVLPLYQKSVWTQESKCHLIETNIRDQEELKGKKVPQYPCLWVNVSAAGRWAVLYHTEDTRDQNQQCSYIPGSVDNYQTARADVEKVRAKFQEQQVFYCFSAPRGNETSVLFQRLYGPQALLFSLFWPTFLLTGGLLIIAMVKSNQYLSILAAQK
Protein: Fas-activated serine/threonine kinase (FAST kinase) (EC 2.7.11.1) (EC 2.7.11.8) (Q9JIX9)
Organism: Mus musculus (Mouse)
Function: Phosphorylates the splicing regulator TIA1, thereby promoting the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-apoptotic form of the receptor (By similarity). Required for the biogenesis of some mitochondrial-encoded mRNAs, specifically stabilizes ND6 (NADH dehydrogenase complex subunit 6) mRNA, and regulates its levels.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:25704814}. Note=Colocalizes with mitochondrial RNA granules. {ECO:0000269|PubMed:25704814}.
Interaction partners:
- FAST kinase domain-containing protein 2
- NADH-ubiquinone oxidoreductase chain 6
Sequence:
MLRILLSAQTSPARLSGLLLIPPVQPCCLGPSKSGDRPFGGGPVQGLQRLLEQARSPGELLRWLSQNPTKVRAHHYPVALRRLGQLLVSQPRPSPVEQATLQDLSQLIIRNCPSFDVHTIHVCLHLAVLLGFPSDGPLLCALEQERRSRLPPKPPSPHRPAIYGGQRLEVALSCPRFLQYPRQHLIRSLAEARPEELTPHVMVLLAQHLARHRLREPQLLEAIAHFLVVQEAQLNSKVVQKLVLPFGRLNYMPLEQQFMPCLERILAREAGVAPLATVNILMSLCQLQCLPFRALQFVFSPSFINHINGTPPSLIVRRYLSLLDTAVELELPGYQGPRLPQRQRVPIFPQPLITDRARCKYSHKDMVAEGLRQLLGEENYRQNLTVPPGYCTDFLLCVSSSGAVLPMRTQDPFLPYPPRSCQQDQANFNSTTQDPAQRVVLMLRERWHFCRDGRVLLGSRALRERHLGLMGYQLLPLPFEELESQRGLPQLKSYLRQKLQALGFRWGPEGG
Protein: ATP-dependent helicase hrq1 (EC 3.6.4.12) (Homologous to recQ protein 1) (O13983)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Helicase with 3'-5' helicase activity involved in genome stability. Functions in the nucleotide excision repair (NER) pathway and plays a critical role in DNA interstrand cross-link repair. Unwinds relatively long duplex DNA up to 120-bp and requires a long 3'-tail of at least 70 nucleotides for efficient unwinding of duplex DNA (By similarity). Shows both processive helicase and DNA strand annealing activities (By similarity). Affects telomere length by a non-catalytic mechanism, probably through inhibiting telomerase by competing with it for ssDNA binding (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:22064477}.
Interaction partners:
Sequence:
MSQTPIKKEESNDQDDKFEFKKYINEGKLPLKADNPKKKPQLGTIQANQPIPSIFDNLFNLFKVINTTYTFLYLRNSLTITFPLLNSSVKQSLKKELTIGDLSQLREICPQIIELNYKSLASLALEINKNVYTDLNPELYTGSTVSQSSEYVLVIELLETQERSSKRRRREGPTMKANIQRQKLDFNNLKKAIELRNQKFLQGIKEYIKKCQLTELDPTQQLLTQSRKNQPVPPDSPSIPNDSIENCNLNTKACSIEELLNEIASESSYEGQIVQEALHTYPAVEAQYGALSRPLSQELINALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTLKNIRVDTFDGDTPLESRESIIRSANIIFTNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIAEYFGNSQYRFVSCSATIEDPLQHMKKIFGVDNIKLINYTSSPSGSKKFVMWNPPYVDPKHPDDGKKSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELKTKQKGDLLSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVETFPVDQFYLKHPILIHTQPNAELTLDLTNEVLLASHLQCAAYELPINIRSDEKFFGNQIQDICEANLEMVEESYRPHPKYLPFPASQVRIRSVSEDMFTLVDVTNDKNVILELLEPFRVALTAYEGAVYVYQGKTFIIRLLNINKRIITAHQVDVEWSTLQRDFTDVDPVRSLMKKTMHGSTNIYFGAVKATLHVFGYFKVNKQKDILDVVDITDHPVEIDSRGFWIDVPWHIIEVLSLKKINGAASIHAAQHALLSLMPIFISNSGNDIRTECKAGEKEYKEAKSERRRPSRLIFYDNCGDSSGAGLCNKAYEHTDELITMAIERIESCDCKVREGCPGCITSSKFEGGVCSGEVLDKVGALILLKMLLCQHVNLDIYADGPEIDSYHALRTLIPSC
Protein: Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase 5) (Alcohol dehydrogenase class chi chain) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284) (P11766)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Class-III ADH is remarkably ineffective in oxidizing ethanol. Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- S-formylglutathione hydrolase
- Aldehyde dehydrogenase, mitochondrial
- Cytochrome P450 26A1
- Cytochrome P450 2E1
- Aldehyde oxidase
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Lecithin retinol acyltransferase
- Vasopressin-neurophysin 2-copeptin
- All-trans-retinol 13,14-reductase
Sequence:
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI
Protein: Dek, isoform B (LD10094p) (Q8T0D3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Regulator of nonsense transcripts 1 homolog
- Serine/arginine repetitive matrix protein 1
- LD23870p
- Transcription factor AP-2, isoform D
Sequence:
MPSPHEKDANKAAETAAKENAADKVSDVENASVTAGVAKAVGAQPERGSKDAAESPAAVDASASAATDDVADKKAKGDSTAVSNTESDAAAADKKEKSPSPVIKKSNNKDAKKEDNSEKDEENSEDGDEPEDEADEKASDEESEKKKPKLDAEDKIKDATDESKPKSGADKPKKPEPKAKNGKVAKEEDDDEEDEDDEDAEDDDGDENDGLDKNNEVAEDDENVVALAEIDRINENINKTRVDGLQTLHAICFGAQGKNNVVKKNLRSFAGFEFAKDSAEYNKKLEAIKKVDNKGLRSICEILTLDRKGSKNETVLRVLKFLMEPDESLCLEQGDEEEEEDAEDEDLDEDEEDPPSEEDKKRKSGKSSGGAGRGSARNSTGRPRRATAGKKMSAYVDFSSSDDSEQKVAVPKRRRNDDSESGSDYNPSANSDSDGGRGGGAGAAGRKVPSRGGRGRPARKSRRRNSDSEEEEESEVSDADSDVPKRKRGSVGKRGRPAAPASAGRRGRGRGAASRKRKDSDSEDEEVSEDEEEEDVSDFASDQSEEERPKKSKKPITPAKNSKANNKSKPAGKADSRSKKSKKESSEEDDDVDDKDESDEDEPLTKKGKQAFPTDEQIRGYVKEILDKANLEEITMKTVCKQVYAKYPDFDLTDKKDFIKATVKALIAT
Protein: Sjogren's syndrome/scleroderma autoantigen 1 (Autoantigen p27) (G5EEN7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVHKKFVNLTSTRESTWIDRTPHPAARNYLDEMAPINGIRDDDAASIRLRDSFRDEVSKRMGELLLKGQTMLDEYCPTCSGILMEDRALVRRCVTCELFREKSSVIVGEVSLQDEDLNEAVNNKIPTPAAPVNKPAKKAVLQKSAPAKKKEAVPAAAEPSSSDTIESATTAVLQKLEWATDRLNSTEEVARVMDFLSVIQKSAETLKALRI