wanglab/gogpt-training-data huggingface dataset:
Protein: PcrV (Virulence-associated V antigen) (O30527)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MEVRNLNAARELFLDELLAASAAPASAEQEELLALLRSERIVLAHAGQPLSEAQVLKALAWLLAANPSAPPGQGLEVLREVLQARRQPGAQWDLREFLVSAYFSLHGRLDEDVIGVYKDVLQTQDGKRKALLDELKALTAELKVYSVIQSQINAALSAKQGIRIDAGGIDLVDPTLYGYAVGDPRWKDSPEYALLSNLDTFSGKLSIKDFLSGSPKQSGELKGLSDEYPFEKDNNPVGNFATTVSDRSRPLNDKVNEKTTLLNDTSSRYNSAVEALNRFIQKYDSVLRDILSAI
Protein: Aquaporin TIP2-1 (Tonoplast intrinsic protein 2-1) (ZmTIP2-1) (ZmTIP2;1) (Q9ATL9)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Tonoplast.
Interaction partners:
- RNA helicase
Sequence:
MVKLAFGSVGDSFSATSIKAYVAEFIATLLFVFAGVGSAIAYGQLTNGGALDPAGLVAIAIAHALALFVGVSVAANISGGHLNPAVTFGLAVGGHITILTGVFYWVAQLLGATVACLLLGFVTHGKAIPTHAVAGISELEGVVFEVVITFALVYTVYATAADPKKGSLGTIAPIAIGFIVGANILAAGPFSGGSMNPARSFGPAVAAGDFAGNWVYWVGPLVGGGLAGLVYGDVFIGGSYQQVADQDYA
Protein: Polymerase delta-interacting protein 2 (Q91VA6)
Organism: Mus musculus (Mouse)
Function: Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites. May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9Y2S7}. Nucleus {ECO:0000250|UniProtKB:Q9Y2S7}. Note=Mainly localizes to the mitochondrial matrix; a small fraction localizes in the nucleus. {ECO:0000250|UniProtKB:Q9Y2S7}.
Interaction partners:
- Cytochrome b-245 light chain
- NADPH oxidase 4
- Neutrophil cytosol factor 2
- Neutrophil cytosol factor 1
- DNA-directed primase/polymerase protein
- NADPH oxidase 2
Sequence:
MAGCVARRALAVGSRWWSRSLATTRGSRPLCAVGGAGGLPPVATATTRRHLSSRNRAEGKVLETVGVFEVPKQNGKYETGQLFLHSVFGYRGVVLFPWQARLYDRDVASATPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW
Protein: Polyamine aminopropyltransferase 2 (1,3-diaminopropane aminopropyltransferase) (EC 2.5.1.23) (Sym-norspermidine synthase) (A2BJU2)
Organism: Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)
Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to 1,3-diaminopropane to yield sym-norspermidine (bis(3-aminopropyl)amine). It can also synthesize thermospermine from spermidine with a very low activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Arginine decarboxylase proenzyme
- Agmatinase
- S-methyl-5'-thioadenosine phosphorylase
- Polyamine aminopropyltransferase 1
- Cytosine deaminase
- S-methyl-5-thioadenosine phosphorylase
Sequence:
MAQRLPWRFVAEWTSEGEMVLREVKRIYAAGATRYQEYMIAELAGIGKALVLDGKVQSSILDEHWYHEALVHPILLAHQCPRKVLVIGGGEGATVREVLRHSCVEHVTMVDIDEELVELAKKHLAEWHQGAFSSDKLELVIGDGRRYVENCHRKYDAIILDLVDPMEGGPAARLYTLEFYRAVKGCLRPGGAVVTQATSPTLSPRVYAVIRNTLAKVFTIVRPYVSYVRSYNGLWGFVAASDTVDPAKLSAKEVDELIAARIRGQLRFYDGETHEWMFRLPLPVRQVLSETRDYATDEKPVYVPV
Protein: DNA topoisomerase type IB small subunit (EC 5.99.1.2) (Q38EP5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA topoisomerase I
- DNA topoisomerase 2
- Tyrosyl-DNA Phosphodiesterase
- SUMO-conjugating enzyme UBC9
- Small ubiquitin protein, putative
- DNA topoisomerase 2
Sequence:
MSSANSEVRNGGSSSVAAAQPRAASPAKIPVKVPYSLAKVPMPRLVPAKMPAPKRAAESEAQHRGNREDSDDALLESSAPSKKPKKEESKKAPLVETESSSSSEYSSSDSDDTDASDSESEGSKTSTVSDSSDISDDEESVSEDNLTFFELAERSGLMNDIKNKVNSGEGEQEEEEEVHIDGKPPRPKFLRSFPRDIEAEIGKHEKRLKDVENMLKMKQDNKTVSLGTSKVNYIDPRIVCSWANENNVPISRLFSATLQKKFPWALKARDFTF
Protein: LRR receptor-like serine/threonine-protein kinase RGI5 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 5) (Protein RGF1 INSENSITIVE 5) (C0LGF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with RGI1, RGI2, RGI3 and RGI4, acts as receptor of RGF1, a peptide hormone that maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT). Links RGF1 signal with its downstream components.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Probable LRR receptor-like serine/threonine-protein kinase At1g14390
Sequence:
MERERSNFFFLFLFCSWVSMAQPTLSLSSDGQALLSLKRPSPSLFSSWDPQDQTPCSWYGITCSADNRVISVSIPDTFLNLSSIPDLSSLSSLQFLNLSSTNLSGPIPPSFGKLTHLRLLDLSSNSLSGPIPSELGRLSTLQFLILNANKLSGSIPSQISNLFALQVLCLQDNLLNGSIPSSFGSLVSLQQFRLGGNTNLGGPIPAQLGFLKNLTTLGFAASGLSGSIPSTFGNLVNLQTLALYDTEISGTIPPQLGLCSELRNLYLHMNKLTGSIPKELGKLQKITSLLLWGNSLSGVIPPEISNCSSLVVFDVSANDLTGDIPGDLGKLVWLEQLQLSDNMFTGQIPWELSNCSSLIALQLDKNKLSGSIPSQIGNLKSLQSFFLWENSISGTIPSSFGNCTDLVALDLSRNKLTGRIPEELFSLKRLSKLLLLGNSLSGGLPKSVAKCQSLVRLRVGENQLSGQIPKEIGELQNLVFLDLYMNHFSGGLPYEISNITVLELLDVHNNYITGDIPAQLGNLVNLEQLDLSRNSFTGNIPLSFGNLSYLNKLILNNNLLTGQIPKSIKNLQKLTLLDLSYNSLSGEIPQELGQVTSLTINLDLSYNTFTGNIPETFSDLTQLQSLDLSSNSLHGDIKVLGSLTSLASLNISCNNFSGPIPSTPFFKTISTTSYLQNTNLCHSLDGITCSSHTGQNNGVKSPKIVALTAVILASITIAILAAWLLILRNNHLYKTSQNSSSSPSTAEDFSYPWTFIPFQKLGITVNNIVTSLTDENVIGKGCSGIVYKAEIPNGDIVAVKKLWKTKDNNEEGESTIDSFAAEIQILGNIRHRNIVKLLGYCSNKSVKLLLYNYFPNGNLQQLLQGNRNLDWETRYKIAIGAAQGLAYLHHDCVPAILHRDVKCNNILLDSKYEAILADFGLAKLMMNSPNYHNAMSRVAGSYGYIAPEYGYTMNITEKSDVYSYGVVLLEILSGRSAVEPQIGDGLHIVEWVKKKMGTFEPALSVLDVKLQGLPDQIVQEMLQTLGIAMFCVNPSPVERPTMKEVVTLLMEVKCSPEEWGKTSQPLIKPSSS
Protein: MPL proto-oncogene, thrombopoietin receptor (A0A2R8YE13)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XWISLVTALHLVLGLSAVLGLLLLRWQFPAHYSSQDIVQAPYDDKRGSAKSAPASKHFSLFYPVHQPFQTGFLHKRLRHALWPSLPDLHRVLGQYLRDTAALSPPKATVSDTCEEVEPSLLEILPKSSERTPLPLCSSQAQMDYRRLQPSCLGTMPLSVCPPMAESGSCCTTHIANH
Protein: Volume-regulated anion channel subunit LRRC8D (Leucine-rich repeat-containing protein 5) (Leucine-rich repeat-containing protein 8D) (Q5U308)
Organism: Rattus norvegicus (Rat)
Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (By similarity). Plays a redundant role in the efflux of amino acids, such as aspartate, in response to osmotic stress (By similarity). Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition. Also acts as a regulator of glucose-sensing in pancreatic beta cells: VRAC currents, generated in response to hypotonicity- or glucose-induced beta cell swelling, depolarize cells, thereby causing electrical excitation, leading to increase glucose sensitivity and insulin secretion (By similarity). VRAC channels containing LRRC8D inhibit transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28833202}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L1W4}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7L1W4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L1W4}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000250|UniProtKB:Q7L1W4}.
Interaction partners:
- Volume-regulated anion channel subunit LRRC8A
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L2
Sequence:
MFTLAEVASLNDIQPTYRILKPWWDVFMDYLAVVMLMVAIFAGTMQLTKDQVVCLPVLPSPANSKAHTPPGNADVTTEVPKMETATPQDQNGQTTNDIAFGTSAVTPDIPLQATYSHAESTFPSQETKKEKRDPTGRKTNLDFQQYVFINQMCYHLALPWYSKYFPYLALIHTIILMVSSNFWFKYPKTCSKVEHFVSILGKCFESPWTTKALSETACEDSEENKQRITGAQTLPKHVSTSSDEGSPSASTPMINKTGFKFSAEKPVIEVPSMTILDKKDGEQAKALFEKVRKFRAHVEDSDLIYKLYVVQTLIKTAKFIFILCYTANFVNAISFEHVCKPKVEHLTGYEVFECTHNMAYMLKKLLISYISIICVYGFICLYTLFWLFRIPLKEYSFEKVREESSFSDIPDVKNDFAFLLHMVDQYDQLYSKRFGVFLSEVSENKLREISLNHEWTFEKLRQHVSRNAQDKQELHLFMLSGVPDAVFDLTDLDVLKLELIPEAKIPAKISQMTNLQELHLCHCPAKVEQTAFSFLRDHLRCLHVKFTDVAEIPAWVYLLKNLRELYLIGNLNSENNKMIGLESLRELRHLKILHVKSNLTKVPSNITDVAPHLTKLVIHNDGTKLLVLNSLKKMMNVAELELQNCELERIPHAIFSLSNLQELDLKSNSIRTIEEIISFQHLKRLTCLKLWHNKIVAIPPSITHVKNLESLYFSNNKLESLPVAVFSLQKLRCLDVSYNNISTIPIEIGLLQNLQHLHITGNKVDVLPKQLFKCVKLRTLNLGQNCIASLPEKISQLSQLTQLELKGNCLDRLPAQLGQCRMLKKSGLVVEDQLFDTLPLEVKEALNQDVNVPFANGI
Protein: Neurexin-3-beta (E9P874)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVFLEHLRGGTPRGTTTVSPILCLMNWNDEQCRQQLKSYIPKFASNFDAPRHVPQPPSSPSYDYEGDEDEEKKEEKDHGIADRSMNDVSGETTGFFSPVLPTVANFPTTRQTEPETTRRPLSPSKMTPSLPSPTTTTLPVFFLSQITDGDESEDEFDGSGDDLFGGDGVGITAATQPSVKRTTSISVVTKVLTTTSEPSSTHRSTVLPRPYASVKEAAEQNPDYLGASIWNQVDTLPEPMVTGPAWRTNKSLTTTATTEASSTKSNRKTTTTTTTSATTTIRIQQRPNYDIDNEVTALITSSLAPQKTRPKSTPHFTVYPVRPTTPMGDTITTTMQAATVTDFPRTPLIMCSSLAVIIAIAAVVFFVFKCRQNPPNSEHYTMAMKSQSGYTAIAPELSPPMNHDRSNDSCTQPLLAKPHINGNGYEPLKGAVIANGNGATATMMRNGNGNGVAKKKDFKEWYV
Protein: Beta-glucosidase 32 (AtBGLU32) (EC 3.2.1.21) (Q9FLU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Proline-rich receptor-like protein kinase PERK3
- Heavy metal-associated isoprenylated plant protein 4
- Peroxidase 32
- NAC domain containing protein 38
- Peroxidase 22
- Protein indeterminate-domain 6
Sequence:
MAIKLIALVITICVASWDSAQGRSLRFSTTPLNRYSFPPHFDFGVASSAYQYEGAVEEGGRSPSIWDNFTHAFPERTNMDNGDVAVDFYHRYKDDIKLIKEMNMDSFRFSLSWSRILPSGKLSDGVNKEGVQFYKNLIDELIKNGIKPFVTIYHWDIPQALDDEYGSFLSPRIIDDFRNFARFCFQEFGDKVSMWTTFNEPYVYSVSGYDAGNKAIGRCSKWVNSLCIAGDSGTEPYLVSHNLLLAHAAAVEEFRKCDKISQDAKIGIVLSPYWFEPYDIDSESDKEAVERALVFNIGWHLSPLVFGDYPETIKTTAGNRLPSFTKEQSMMLQNSFDFIGINYYTARFVAHDLHVDLSRPRFTTDQHLQYKLTNRSGDHISSESDGTKILWSYPEGLRKLLNYIKNKYNNPTIYITENGFDDYENGSVTREEIIEDTKRIEYHQNHLQQLQKAITEDGCNVKGYFTWSLLDNFEWEHGYAVRFGLYYVDYKNGLSRHAKNSAKWFKHFLQRSGKPMPLDLFKSVKNWWSAIPMI
Protein: Non-lysosomal glucosylceramidase (NLGase) (EC 3.2.1.45) (E7F5W0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- N-acylsphingosine amidohydrolase
- Acid ceramidase
- Galactocerebrosidase
- UDP-glucose ceramide glucosyltransferase.
- Glucosylceramidase
- Neutral ceramidase
- Beta-galactosidase.
- Alkaline ceramidase
- UDP glycosyltransferase 8
- Ceramide kinase
Sequence:
MDLNDSKSLAELMSRYASSETGFGVPKDGWRICLAHEFKEKRKPFQAKDVSLSNMLEHVSLGVRYLKWWYRKTQVEKKAPFIDMFRAVPLRQIYGVPLGGIGGGSITRGWRGEFCRWQLNPGMYHYKTVIANQFTVCLRRDGQTVYQQVLSTERPSTLQGWNWGYCGEHAFYHGLFPRAWTVYNLPGQNVTLTCRQVSPVIPHDYKDSSLPVAVFVWDIENKNDYALDISIMFTMVNGSGQKDDKSGGHWNEPFHLEKEGESVSGVLLHHQTPANPYTLCIAARQKSGQEISHQTAFSPKGTCSAVWCDLMTDGRLDSPTNSSPPTEKGEEVAAALVVSCSVSANSRNSVDFSLAWDMPKITFGSKERTYVRRYTRYYGTKGDAAPSISHYALTHYSKWEESIEEWQRPILQDRSLPAWYKSALFNELYFVVDGGTIWVELPEDADISGGLRPEDGGLPAQPEVVKDFGRFAYLEGQEYRMYNTYDVHFYASFALIMLWPKLALSLQYDIAGSVVQHDPMERLNLMNGRYSPVKTRGVVPHDIGDPDDEPWVRVNAYLIHDTADWKDLNLKFVLQVYRDYHLTQDQQYLKDMWPVCQTVMENELKFDKDGDGLIENSGYADQTYDGWKVTGPSAYCGGLWLASVCMMCKMARVLNCESVYQRYRDILERGSAAFDKLLWNGKYYNYDSSGRSLSNSVMSDQCAGHWFLRASGLGDDEYQAFPKEKICSALKSVFDLNVMSFAGGQMGAVNGMRPEGVPDRSSVQSDEVWVGVVYGLAATMIHEGMVEEGLRTAEGCYRAVWERMGMAFQTPEAYCEKGIYRSLAYMRPLSIWAMQLALNNRPNHDTTTDKT
Protein: NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (Q38F81)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NEDD8-activating enzyme E1 regulatory subunit
- Ubiquitin, putative
- Ubiquitin-conjugating enzyme E2, putative
- Polyubiquitin, putative
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-like modifier-activating enzyme 5
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- Cullin 1, putative
Sequence:
MSCNPLRTAFTLQNPGLQRVVQRAPPIFANGYSSDSITWDSVRVLLVGAGGIGCEVLHSLALSGFADITVIDMDTVELSNLSRQFLFREADIGRSKAEVAAAAVECRCPGVRVRALFGRIEDQSDEFYRQFHAVILAVDSVAARRWVNQKVAEVAEWETFDMVDGGCYENIAARPIARRMRRIAYAMPLIDTGTEGYEGCCRVVLLRSVNPTPCIECDLSLYPSRRTVPLCTLENIPRLPEHCVLYVKFKLWEELRPHESPDADNPEHIAWMTVMAQRRKEAFGIEGPDIDDAFTLGVVKNVVPAVGFTNALVAAQAVLELVKLLTGVAFPVQCFSYYNGSTKCGLTSYVTDLIPNPTCSVCGPRPLLILSAEMTPLNVLLAIKTQVGMPPSVEDISHLDVTLRVRFAAGEVYLMYKSNNPLRTNVVATTIEEAFATSGYAAAFVEWCNSDAVVFTLECSGADIHIS
Protein: Fanconi-associated nuclease 1 homolog (PaFAN1) (pFAN1) (EC 3.1.4.1) (Q9I2N0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. Also has endonuclease activity toward 5'-flaps.
Interaction partners:
- Helicase ATP-binding domain-containing protein
- YebG family protein
- Uncharacterized protein
Sequence:
MHEQYQAPLPVNSPALPEPFYYLHNFRAVLAWIGERYADLLDDQERAFIAAFAELPEASQALLVRMVMRKGTLFREGKLAYAEIGDTRAAVQPLLALGWVDAQPTLELAQLFGLLKKDELSQLFRDHLGRANLRKDALLERLQPLFPEARRLAEWQADFAEPVYELRCMALCDRLRLMYFGNLWQDWSEFVLADLGIYRYESVEFSADSRGFRLRADVDAYLHLFDCRQRFDLGEPLEELLAGLPGEPYANPWLEGRRVKLLFQFAQHCEKQRDFDLAQRLYRQSSHPGARLRAIRSLERGERFAEAHALAREASCAPESDAERQGLARLLPRLQGKLGLPRQARAAAPEIDRLDLCLAFPSEPCSVEWAVREHLEEPGCAVHYVENGLINSLFGLLCWEAIFAAIPGAFFHPFHSAPADLHSADFRQRRAALFEACLGRLEDGSYRDAIRCRYRDKFGLQSPFVYWELLGEELLEQALDCLPAAHLRAWFERLLEDIPGNRAGLPDLIQFWPAQRRYRMVEVKGPGDRLQDNQLRWLQFCREREMPVAVCYVRWHVDD
Protein: Fibroblast growth factor 15 (FGF-15) (O35622)
Organism: Mus musculus (Mouse)
Function: Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression.
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor 4
- Beta-klotho
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Klotho
- Fibroblast growth factor receptor 3
- Fibroblast growth factor 4
- Bile acid receptor
- Cytochrome P450 7A1
- Vascular endothelial growth factor receptor 2
Sequence:
MARKWNGRAVARALVLATLWLAVSGRPLAQQSQSVSDEDPLFLYGWGKITRLQYLYSAGPYVSNCFLRIRSDGSVDCEEDQNERNLLEFRAVALKTIAIKDVSSVRYLCMSADGKIYGLIRYSEEDCTFREEMDCLGYNQYRSMKHHLHIIFIQAKPREQLQDQKPSNFIPVFHRSFFETGDQLRSKMFSLPLESDSMDPFRMVEDVDHLVKSPSFQK
Protein: Presequence translocase associated motor 16 (A0A8I5ZMD9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
Interaction partners:
Sequence:
MIIVMGVQVVGRAFARALRQEFAASQAAADARGRAGHQSAAASNLSGLSLQEAQQILNISKLSPEEVQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERLDEELRIQAQEDREKGQTPKT
Protein: Medium-chain acyl-CoA ligase ACSF2, mitochondrial (EC 6.2.1.2) (Q9VMR6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein bL21m
Sequence:
MNSKLQTISRYMLRQKCAFNSMRSISTSMPSLISHKHHIGKDPLVYRTIGQQLELSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEISDADTGKIRSEKFPHLRSVIIDSNDSLKGALRFDDFLDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKETELKAARL
Protein: 12S rRNA N(4)-cytidine methyltransferase METTL15 (12S rRNA m4C methyltransferase) (EC 2.1.1.-) (Methyltransferase 5 domain-containing protein 1) (Methyltransferase-like protein 15) (A6NJ78)
Organism: Homo sapiens (Human)
Function: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA. Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}.
Interaction partners:
- Putative ribosome-binding factor A
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS11m
Sequence:
MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLRPGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSVRQQVMKTSQLGSDHENTEEVSMRRAPLMWELIHKKVLSPQDQDVQDNPRGRSAKLRAAIKL
Protein: Aldehyde dehydrogenase, mitochondrial (EC 1.2.1.3) (AHD-M1) (ALDH class 2) (ALDH-E2) (ALDHI) (P47738)
Organism: Mus musculus (Mouse)
Function: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Amine oxidase [copper-containing] 3
- Aldehyde oxidase 3
- Aldehyde oxidase 1
- Aldehyde oxidase 4
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Acetyl-coenzyme A synthetase, cytoplasmic
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Aldehyde oxidase 2
Sequence:
MLRAALTTVRRGPRLSRLLSAAATSAVPAPNHQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Protein: Heat shock protein 110 (Q05036)
Organism: Caenorhabditis elegans
Interaction partners:
- DnaJ homolog subfamily B member 13
- Stress-induced-phosphoprotein 1
- BAG domain-containing protein
- BAG family molecular chaperone regulator 1
- DNaJ domain
- Heat shock protein 90
- DNaJ domain
- Heat shock protein hsp-6
- Heat shock protein hsp-1
- J domain-containing protein
Sequence:
MSVLGFDIGNLNCYIGVARQGGIEVITNDYSLHATPACVSFGPKDRSMGVAARQAVTTNIKNTVINFKHLIGRKFSDPVAQRFIPFIPCKVVKLPNDDIGVQVSYLGEPHTFTPEQVLAALLTKLRTIVESQLSDVKKVSDCVLAVPSYFTDVQRRAVLSAIQYAGLNSLRIVNETTAIALAYGIYKQDLPEEDAKSRNVVFLDIGHSSTQASLVAFNRGKLQMVNTSYDLESGGIWFDALIREHFRKEFKTKYGIDAATSPRPWLRLLDECERVKKQMSANQTPIPLNIECFMEDKDVTGKMQRQEFEDLAAPIFNRIKQVLINLFADGVSIKPEEIDEIEIVGGSSRIPMIREIVKDLFGKEPKTTMNQDEAVARGAAMQCAILSPTFRVREFAIKDTQPYRIRLSWNSTGENGGENDVFSPRDEVPFSKLVSLLRSGPFNVEAHYAQPNVVPHNQVHIGSWKVNGARPGADGGNQKVKVKVRVNPDGIFTIASATMYEPRIVEEVPAEAMEVDGDAKTEAPAEPLEPVKKTKLVPVDLEVIESIPVSYDVQKFHNLELQMQESDAREKAKADAKNSLEEYVYEMRDKVSDQYAEFITPAAADEFRSVLTSTEDWLYDEGEDAERDVYEKRLSELKAVGTPVVERYRESETRKPAFDSFDQSIMRVRKAYEDYANGGPTYAHLDSKEMEKVINAIEDKKKWLDEARHKQETRSKTDAPVVFTEEILQNKNVFENVVNPILNKKKPAAPAPPKKEEPQPAAGDQPQSQPGEMDVD
Protein: Carbohydrate sulfotransferase 3 (EC 2.8.2.17) (EC 2.8.2.21) (Chondroitin 6-O-sulfotransferase 1) (C6ST-1) (Chondroitin 6-sulfotransferase) (C6ST) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0) (GST-0) (O88199)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan. Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Carbohydrate sulfotransferase 7
- Carbohydrate sulfotransferase 12
- Carbohydrate sulfotransferase 11
Sequence:
MEKGLALPQDFRDLVHSLKIRGRYVLFLAFVVIVFIFIEKENKIISRVSDKLKQIPHFVADANSTDPALLLSENASLLSLSELDSTFSHLRSRLHNLSLQLGVEPAMESQEAGAEKPSQQAGAGTRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVFFQQRGASAAGSALVYRDVLKQLLLCDLYVLEPFISPPPEDHLTQFLFRRGSSRSLCEDPVCTPFVKKVFEKYHCRNRRCGPLNVTLAGEACRRKDHVALKAVRIRQLEFLQPLVEDPRLDLRVIQLVRDPRAVLASRIVAFAGKYENWKKWLSEGQDQLSEDEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARRPLQKAREMYSFAGIPLTPQVEDWIQKNTQATRDSSDVYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPTMHLFGYKLARDAASLTNRSISLLEERGTFWVT
Protein: Entericidin B (P0ADB7)
Organism: Escherichia coli (strain K12)
Function: Plays a role in the bacteriolysis. Is activated under conditions of high osmolarity by the factor sigma S. Entericidin A functions as an antidote.
Subcellular location: Cell membrane; Lipid-anchor.
Interaction partners:
- Entericidin A
Sequence:
MVKKTIAAIFSVLVLSTVLTACNTTRGVGEDISDGGNAISGAATKAQQ
Protein: Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (Q5UPJ7)
Organism: Acanthamoeba polyphaga mimivirus (APMV)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Interaction partners:
Sequence:
MENTDHTNNEHRLTQLLSIAEECETLDRLKQLVDSGRIFTAYNGFEPSGRIHIAQALITVMNTNNIIECGGQMIIYIADWFAKMNLKMNGDINKIRELGRYFIEVFKACGINLDGTRFIWASEFIASNPSYIERMLDIAEFSTISRVKRCCQIMGRNESDCLKASQIFYPCMQAADVFELVPEGIDICQLGIDQRKVNMLAIEYANDRGLKIPISLSHHMLMSLSGPKKKMSKSDPQGAIFMDDTEQEVSEKISRAYCTDETFDNPIFEYIKYLLLRWFGTLNLCGKIYTDIESIQEDFSSMNKRELKTDVANYINTIIDLVREHFKKPELSELLSNVKSYQQPSK