wanglab/gogpt-training-data huggingface dataset:
Protein: Desmoglein-1-beta (Dsg1-beta) (Desmoglein-5) (Q7TSF1)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12631242}; Single-pass type I membrane protein {ECO:0000269|PubMed:12631242}. Cell junction, desmosome {ECO:0000269|PubMed:12631242}. Cytoplasm {ECO:0000250|UniProtKB:Q02413}. Nucleus {ECO:0000250|UniProtKB:Q02413}.
Interaction partners:
- Desmocollin-1
- Corneodesmosin
- Desmoglein-1-alpha
- Junction plakoglobin
- Desmoglein-1-gamma
- Desmoplakin
- Filaggrin
- Periplakin
- Envoplakin
- Kallikrein-7
Sequence:
MDWHSFRIAALLLTSLVVLEVNSEFQIQVRDHNAKNGTIKWHSIRRQKREWIKFAAACREGEDNSKRNPIAKIHSDCAANQPVTYRISGVGIDQPPYGIFIINQKTGEINITSIVDREVTPFFIIYCRALNAQGQDLENPLELRVRVMDINDNPPVFSMTTFLGQIEENSNANTLVMKLNATDADEPNNLNSMIAFKIIRQEPSDSPMFIINRKTGEIRTMNNFLDREQYSQYSLVVRGSDRDGGADGMSAESECSITILDVNDNIPYLEQSSYDIEIEENALHSQLVQIRVIDLDEEFSDNWKAIIFFISGNEGNWFEIEMNERTNVGTLKVVKPLDYEAMKNLQLSIGVRNVAEFHQSIISQYRLTATMVTVTVLNVIEGSVFRPGSKTFVVDSRMEANHRVGEFVATDLDTGRASTNVRYEMGNNPENLLVVDSRTGIITLRNRVTMEQYQRLNGEYKGTVLSIDDSLQRTCTGTIVIELSGTGWVPGSDGGGSSSGSGGNRDPVTNGYQGTSTVGPQRVTGSGGVTSSGGGSGVNNTPGRQNPLDEPEPEPFDITEDNVHFGPAGIGLLIMGFLVLGLVPFLLICCDCGGAPGGGAGFEPVPECSDGAIHTWAIEGPQPEPHDGITTICVPQMPPGNANVIEYIDNSGVYTNEYCGREMQDLGGGERTTGFELMDGVKTSAAPEICQEYSGTLRRNSMRECRDGGLNMNFMESYFCQKAYAYADEDEGRPSNDCLLIYDIEGVGSPAGSVGCCSFIGEDLDESFLDTLGPKFKKLADISLGKEIDSYPDPDSSWPPQSTEPMCPQSTEPLGSGYPPISPHFGTTTVISENAYPSGPGVQHPLPIPDPLGYGNVTVRESYATSGTLKPSVHFHDNQQASNVVVTERVVGPVPGADLHGMLEIPDLRDGTNVIVTERVIAPGSSLPTSLTIPNPRETSNVVVTERVIQPTSGMIGNLSMTPELSSAQNVIVTERVVSGAGMSGIAGTAGLGGVGGIGSSGLVSTTMGAAGTGLNMGGTATIGHMRSSSDHHFSQTIGSASPNMARSRITKYSTVQYSK
Protein: Glutathione-regulated potassium-efflux system ancillary protein KefF (Quinone oxidoreductase KefF) (EC 1.6.5.2) (P0A754)
Organism: Escherichia coli (strain K12)
Function: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its function could be to reduce the redox toxicity of electrophilic quinones in parallel with acting as triggers for the KefC efflux system.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01414}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01414}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01414}.
Interaction partners:
- Glutathione-regulated potassium-efflux system protein KefC
- Glutathione-regulated potassium-efflux system protein KefB
- Putative metabolite transport protein YaaU
- NADPH:quinone oxidoreductase MdaB
- Protein FixC
Sequence:
MILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVFSHGWAYGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAHHG
Protein: Cysteine S-methyltransferase OspZ (EC 2.1.1.-) (Effector protein OspZ) (A0A3T2V133)
Organism: Shigella flexneri
Function: Cysteine methyltransferase effector that inhibits host cell NF-kappa-B activation by preventing nuclear translocation of host protein RELA/p65. Acts by mediating cysteine methylation of host proteins TAB2 and TAB3: methylation of a conserved cysteine residue of the RanBP2-type zinc finger (NZF) of TAB2 and TAB3 disrupts zinc-binding, thereby inactivating the ubiquitin chain-binding activity of TAB2 and TAB3, leading to NF-kappa-B inactivation. Also mediates cysteine methylation of host protein ZRANB3, inactivating its ability to bind ubiquitin chains.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q2TH00}. Host cytoplasm {ECO:0000250|UniProtKB:Q2TH00}. Host nucleus {ECO:0000250|UniProtKB:Q2TH00}. Note=Secreted via the type III secretion system (T3SS). Mainly localizes in the cytoplasm of the infected cells, and occasionaly in the host nucleus. {ECO:0000250|UniProtKB:Q2TH00}.
Interaction partners:
Sequence:
MISPIKNIKNVFPINTANTEYIVRNIYPRVEHGYFNESPNIYDKKYISGITRSMAQLKIEEFINEKSRRLNYMKTMYSPCPEDFQPISRDEASIPEGSWLTVISGKRPMGQFSVDSLYHPDLHALCELPEISCKIFPKENSDFLYIIVVFRNDSPQGELRANRFIELYDIKREIMQVLRDESPELKSIKSEIIIAREMGELFSYASEEIDSYIKQMNDRFSQIKARMSVT
Protein: Protein Pixie (ATP-binding cassette sub-family E member 1) (Q9VSS1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in translation initiation and quality control of translation. Together with pelo and HBS1, is required for 48S complex formation from 80S ribosomes and dissociation of vacant 80S ribosomes. Stabilizes core components of eIF3 complex promoting their assembly into translation initiation-competent complexes. Together with pelo and HBS1, recognizes stalled ribosomes and promotes dissociation of elongation complexes assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway. Plays a role in the regulation of mRNA turnover (By similarity). Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA. As part of the Pink1-regulated signaling, ubiquitinated by Cnot4 upon mitochondria damage; this modification generates polyubiquitin signals that recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy. Required in the wing disk for cell division and growth as well as cell survival. During muscle embryogenesis, required for the recruitment of Pak to muscle attachments in the embryo, hence may play a role in proper muscle morphogenesis and proper guidance and targeting of subsets of myotubes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16291791}.
Interaction partners:
- Eukaryotic peptide chain release factor subunit 1
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit C
- Protein pelota
- Eukaryotic translation initiation factor eIF1
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation release factor 3, isoform A
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MSRRKENEEVDKQTRIAIVSDDKCKPKRCRQECKKTCPVVRMGKLCIEVTPTSKIASLSEELCIGCGICVKKCPFEAITIINLPSNLEKHTTHRYSKNSFKLHRLPIPRPGEVLGLVGQNGIGKSTALKILAGKQKPNLGKYANPPDWTEILSYFRGSELQNYFTKILEDNLKALVKPQYVDQIPKAVRGAVGDLLDKKDERELQTKICEMLDLSHIRDREIAQLSGGELQRFAIAMVCIQNADIFMFDEPSSYLDVKQRLNAALTIRSLLHPTKFIIVVEHDLSVLDYLSDFICCLYGVPGCYGVVTMPFSVREGINIFLDGFVPTENMRFRTESLTFKVSESATEEEIKRMNHYVYPAMVKTLGKFELTVEKGHFSDSEILVLLGENGTGKTTFIRMLAGNLQPDGEVELPMLNISYKPQKISPKFQNHVRHLLHDKIRDAYVHPQFIADVMKPMKIEEIMDQEVQNLSGGELQRVALVLCLGKPADVYLIDEPSAYLDSEQRLVAAKVIKRYILHAKKTGFVVEHDFIMATYLADRVIVIEGQPSVKTTAFSPQSLLNGMNRFLELLGITFRRDPNNFRPRINKNNSVKDTEQKRSGQFFFLEDEACN
Protein: Glycoprotein 5 (Protein GP5) (G(L)) (Q04569)
Organism: Porcine reproductive and respiratory syndrome virus (strain Lelystad) (PRRSV)
Function: Major envelope protein present in abundant amounts in the virion envelope. Mediates virion sialic acid-dependent attachment the sialoadhesin receptor SIGLEC1. This attachment induces virion internalization into alveolar macrophages predominantly through clathrin-dependent endocytosis.
Subcellular location: Virion {ECO:0000269|PubMed:17913250}. Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRCSHKLGRFLTPHSCFWWLFLLCTGLSWSFADGNGDSSTYQYIYNLTICELNGTDWLSSHFGWAVETFVLYPVATHILSLGFLTTSHFFDALGLGAVSTAGFVGGRYVLCSVYGACAFAAFVCFVIRAAKNCMACRYARTRFTNFIVDDRGRVHRWKSPIVVEKLGKAEVDGNLVTIKHVVLEGVKAQPLTRTSAEQWEA
Protein: Acetyl-CoA acetyltransferase, cytosolic (EC 2.3.1.9) (Cytosolic acetoacetyl-CoA thiolase) (Q8CAY6)
Organism: Mus musculus (Mouse)
Function: Involved in the biosynthetic pathway of cholesterol.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BWD1}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit alpha, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetoacetyl-CoA synthetase
Sequence:
MNAGSDPVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRMGEVPLADSILCDGLTDAFHNYHMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFLTDGTGTVTPANASGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAFAAVSAAIAKELGLNPEKVNIDGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQRG
Protein: DCI protein (Dodecenoyl-Coenzyme A delta isomerase (3,2 trans-enoyl-Coenzyme A isomerase), isoform CRA_a) (Enoyl-CoA delta isomerase 1) (Q96DC0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKFKNPPVNSLSLEFLTELVISLEKLENDKSFRGVILTSDRPGVFSAGLDLTEMCGRSPAHYAGYWKAVQELWLRLYQSNLVLVSAINGACPAGGCLVALTCDYRILADNPRYCIGLNETQLGIIAPFWLKDTLENTIGHRAAERALQLGLLFPPAEALQVGIVDQVVPEEQVQSTALSAIAQWMAIPDHARQLTKAMMRKATASRLVTQRDADVQNFVSFISKDSIQKSLQMYLERLKEEKG
Protein: ISWI chromatin-remodeling complex ATPase ISW2 (EC 3.6.4.-) (Imitation switch protein 2) (Q08773)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Imitation switch two complex protein 1
- DNA polymerase epsilon subunit D
- Protein DLS1
- ISWI chromatin-remodeling complex ATPase ISW1
- ISWI one complex protein 2
- ISWI one complex protein 4
- ISWI one complex protein 3
- Histone H4
- Histone H3
- Chromo domain-containing protein 1
Sequence:
MTTQQEEQRSDTKNSKSESPSEVLVDTLDSKSNGSSDDDNIGQSEELSDKEIYTVEDRPPEYWAQRKKKFVLDVDPKYAKQKDKSDTYKRFKYLLGVTDLFRHFIGIKAKHDKNIQKLLKQLDSDANKLSKSHSTVSSSSRHHRKTEKEEDAELMADEEEEIVDTYQEDIFVSESPSFVKSGKLRDYQVQGLNWLISLHENKLSGILADEMGLGKTLQTISFLGYLRYVKQIEGPFLIIVPKSTLDNWRREFLKWTPNVNVLVLHGDKDTRADIVRNIILEARFDVLITSYEMVIREKNALKRLAWQYIVIDEAHRIKNEQSALSQIIRLFYSKNRLLITGTPLQNNLHELWALLNFLLPDIFGDSELFDEWFEQNNSEQDQEIVIQQLHSVLNPFLLRRVKADVEKSLLPKIETNVYVGMTDMQIQWYKSLLEKDIDAVNGAVGKREGKTRLLNIVMQLRKCCNHPYLFEGAEPGPPYTTDEHLIFNSGKMIILDKLLKRLKEKGSRVLIFSQMSRLLDILEDYCYFRDFEYCRIDGSTSHEERIEAIDEYNKPNSEKFVFLLTTRAGGLGINLVTADTVILFDSDWNPQADLQAMDRAHRIGQKKQVHVYRFVTENAIEEKVIERAAQKLRLDQLVIQQGTGKKTASLGNSKDDLLDMIQFGAKNMFEKKASKVTVDADIDDILKKGEQKTQELNAKYQSLGLDDLQKFNGIENQSAYEWNGKSFQKKSNDKVVEWINPSRRERRREQTTYSVDDYYKEIIGGGSKSASKQTPQPKAPRAPKVIHGQDFQFFPKELDALQEKEQLYFKKKVNYKVTSYDITGDIRNEGSDAEEEEGEYKNAANTEGHKGHEELKRRIEEEQEKINSAPDFTQEDELRKQELISKAFTNWNKRDFMAFINACAKYGRDDMENIKKSIDSKTPEEVEVYAKIFWERLKEINGWEKYLHNVELGEKKNEKLKFQETLLRQKIEQCKHPLHELIIQYPPNNARRTYNTLEDKFLLLAVNKYGLRADKLYEKLKQEIMMSDLFTFDWFIKTRTVHELSKRVHTLLTLIVREYEQPDANKKKRSRTSATREDTPLSQNESTRASTVPNLPTTMVTNQKDTNDHVDKRTKIDQEA
Protein: Metal transporter Nramp3 (AtNramp3) (Q9SNV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar metal transporter involved in intracellular metal homeostasis. Can transport iron (Fe), manganese (Mn) and cadmium (Cd). Regulates metal accumulation under Fe starvation. Acts redundantly with NRAMP4 to mobilize vacuolar Fe and provide sufficient Fe during seed germination. In association with NRAMP4, required for optimal growth and photosynthesis under Mn deficiency. Exports Mn from vacuoles in leaf mesophyll cells, making Mn available for functional photosystem II in chloroplasts. Involved in basal resistance to the bacterial pathogen E.chrysanthemi.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:12787249, ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:12787249}.
Interaction partners:
- Fe
- Vacuolar iron transporter 1
- Putative cadmium/zinc-transporting ATPase HMA4
- Ferric reduction oxidase 2
- Metal tolerance protein 1
- Vacuolar cation/proton exchanger 4
- Metal tolerance protein 11
- Solute carrier family 40 member 2
- Nicotianamine synthase 1
- Putative metal tolerance protein C3
Sequence:
MPQLENNEPLLINEEEEEETAYDETEKVHIVRNEEEDDLEHGVGCGGAPPFSWKKLWLFTGPGFLMSIAFLDPGNLEGDLQAGAVAGYSLLWLLMWATAMGLLVQLLSARLGVATGRHLAELCRDEYPTWARMVLWVMAELALIGSDIQEVIGSAIAIKILSNGILPLWAGVVITALDCFVFLFLENYGIRKLEAVFAVLIATMGVSFAWMFGQAKPSGSELLIGILVPKLSSRTIQKAVGVVGCIIMPHNVFLHSALVQSREVDKRQKYRVQEALNYYTIESTIALFISFLINLFVTTVFAKGFYNTDLANSIGLVNAGQYLQEKYGGGVFPILYIWAIGLLAAGQSSTITGTYAGQFIMGGFLNFKMKKWLRALITRSCAIIPTIIVALVFDSSEATLDVLNEWLNVLQSIQIPFALIPLLCLVSKEQIMGSFKIGPLYKTIAWLVAALVIMINGYLLLEFFSNEVSGIVYTGFVTLFTASYGAFILYLIARGITFTPWPFKAESSH
Protein: Cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMP-N-acetylneuraminic acid hydroxylase) (EC 1.14.18.2) (CMP-N-acetylneuraminate monooxygenase) (CMP-Neu5Ac hydroxylase) (CMP-NeuAc hydroxylase) (Q61419)
Organism: Mus musculus (Mouse)
Function: Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. Catalyzes the conversion of CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7608218, ECO:0000269|PubMed:8781965}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
- N-acylneuraminate cytidylyltransferase
- N-acetylneuraminate-9-phosphate synthase
- N-acylneuraminate-9-phosphatase
- NADH-cytochrome b5 reductase 3
- NADH-cytochrome b5 reductase-like
- NADH-cytochrome b5 reductase 1
- Cytochrome b5 reductase 4
- Beta-1,4 N-acetylgalactosaminyltransferase 2
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
Sequence:
MMDRKQTAETLLTLSPAEVANLKEGINFFRNKTTGKEYILYKEKDHLKACKNLCKHQGGLFMKDIEDLDGRSVKCTKHNWKLDVSTMKYINPPGSFCQDELVIEMDENNGLSLVELNPPNPWDSDPRSPEELAFGEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWWLLHEPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLSQRRPDIPIYVGDTERPVFWNLDQSGVGLTNINVVPFGIWQQVDKSLRFMILMDGVHPEMDTCIIVEYKGHKILNTVDCTRPNGGRLPEKVALMMSDFAGGASGFPMTFSGGKFTEEWKAQFIKAERRKLLNYKAQLVKDLQPRIYCPFAGYFVESHPSDKYIKETNTKNDPNQLNNLIRKNSDVVTWTPRPGAVLDLGRMLKDPTDSKGIVEPPEGTKIYKDSWDFGPYLEILNSAVRDEIFCHSSWIKEYFTWAGFKNYNLVVRMIETDEDFSPFPGGYDYLVDFLDLSFPKERPSREHPYEEIHSRVDVIRYVVKNGLLWDDLYIGFQTRLLRDPDIYHHLFWNHFQIKLPLTPPNWKSFLMHCD
Protein: ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial (AtFTSH11) (EC 3.4.24.-) (Q9FGM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V. Involved in thermotolerance but not in high light stress resistance or in the assembly/stability of the complexes I and V of the mitochondrial oxidative phosphorylation system.
Subcellular location: Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side. Plastid, chloroplast thylakoid membrane; Single-pass membrane protein; Stromal side.
Interaction partners:
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
- NADH dehydrogenase 1 alpha subcomplex subunit 13-B
- Protein TIC 100
- Protein TIC 56, chloroplastic
- Protein TIC 40, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Rhomboid-like protein 16, chloroplastic
- YlmG homolog protein 2, chloroplastic
- Lon protease homolog 4, chloroplastic/mitochondrial
Sequence:
MSSSTLQASLFLRPPLHTSSFKLYPCLFSSSSLSFCPQSLSSFYRLSSVLHNSRFRPLPCSLRQDNVASDSDFIPKDSAFEVTDSAESNRLVSDTEVSELETNDRFVGGEETKSGGEEAEVSNGVTEGKEEDQKKSKFRIVVLMMALWAAIKRAIEKVMEWEWLSWWPFSRQEKRLEKLIAEADANPKDAALQGALLAELNKHIPEAVVQRFEQREHTVDSRGVAEYIRALVITNAISEYLPDEQTGKPSSLPALLQELKHRASGNMDESFVNPGISEKQPLHVTMVNPKVSNKSRFAQELVSTILFTVAVGLVWIMGAAALQKYIGSLGGIGTSGVGSSSSYSPKELNKEITPEKNVKTFKDVKGCDDAKQELEEVVEYLKNPSKFTRLGGKLPKGILLTGAPGTGKTLLAKAIAGEAGVPFFYRAGSEFEEMFVGVGARRVRSLFQAAKKKAPCIIFIDEIDAVGSTRKQWEGHTKKTLHQLLVEMDGFEQNEGIIVMAATNLPDILDPALTRPGRFDRHIVVPSPDVRGREEILELYLQGKPMSEDVDVKAIARGTPGFNGADLANLVNIAAIKAAVEGAEKLSSEQLEFAKDRIVMGTERKTMFVSEDSKKLTAYHESGHAIVALNTKGAHPIHKATIMPRGSALGMVTQLPSNDETSVSKRQLLARLDVCMGGRVAEELIFGLDHITTGASSDLSQATELAQYMVSSCGMSEAIGPVHIKERPSSDMQSRIDAEVVKLLREAYERVKSLLKRHEKQLHTLANALLEYETLTAEDIKRILLPKQEGEKFEEQQQEEGDLVLA
Protein: Mitochondrial chaperone BCS1 (BCS1-like protein) (EC 3.6.1.-) (Q9CZP5)
Organism: Mus musculus (Mouse)
Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:21274865}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome b-c1 complex subunit 8
- Mitochondrial ribosome-associated GTPase 1
- Large ribosomal subunit protein bL36m
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Complex III assembly factor LYRM7
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Tetratricopeptide repeat protein 19, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Large ribosomal subunit protein uL16m
- Cytochrome b-c1 complex subunit 9
Sequence:
MPFSDFVLALKDNPYFGAGFGLVGVGTALAMARKGAQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETSYLQHESGRISTKFEFIPSPGNHFIWYQGKWIRVERNRDMQMVDLQTGTPWESVTFTALGTDRKVFFNILEEARALALQQEEGKTVMYTAVGSEWRTFGYPRRRRPLDSVVLQQGLADRIVKDIREFIDNPKWYIDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAVENPIKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNYIDRLDPALIRPGRVDLKEYVGYCSHWQLTQMFQRFYPGQAPSLAENFAEHVLKATSEISPAQVQGYFMLYKNDPMGAVHNIESLR
Protein: Lysine-specific demethylase 7A (JmjC domain-containing histone demethylation protein 1D) (Lysine-specific demethylase 7) ([histone H3]-dimethyl-L-lysine9 demethylase 7A) (EC 1.14.11.65) (Q3UWM4)
Organism: Mus musculus (Mouse)
Function: Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9', 'Lys-27' and 'Lys-36' (H3K9me2, H3K27me2, H3K36me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Lysine-specific demethylase 6B demethylase 6B)
- Lysine-specific demethylase 6A
- F-box/LRR-repeat protein 19
- Lysine-specific demethylase 3A demethylase 3A)
- Lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
- Lysine-specific demethylase 3B demethylase 3B)
- Histone H3.1
- Histone H3.2
- Histone demethylase UTY demethylase UTY)
- Lysine-specific demethylase 5A
Sequence:
MAGAAAAVAAGAAAGAAAAAGSVSAPGRASAPPPPPPVYCVCRQPYDVNRFMIECDVCKDWFHGSCVGVEEHHAVDIDLYHCPDCAALHGSSLMKKRRNWHRHDYTEVDDGSKPVQAGTRAFVKELRSRVFPSADEIIVKMHGSQLTQRYLEKHGFDVPIMVPKLDDLGLRLPSPAFSVMDVERYVGGDKVIDVIDVARQADSKMTLHNYVKYFMNPDRPKVLNVISLEFSDTKMSELVEVPDIARKLSWVENYWPDDSVFPKPFVQKYCLMGVQDSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTNENLALYESWSSSVTQSEVFFGDKVDKCYKCVVKQGHTLFVPTGWIHAVLTSQDCMAFGGNFLHNLNIGMQLRCYEMEKRLKTPDLFKFPFFEAICWFVAKSLLETLKELKEDGFQPQSYLVQGVKALHTALKLWMKKELVSEHAFEIPDNVRPGHLIKELSKVIRAIEEENGKPVKSQGIPSVCPVSRPSNEASPPYHSRRKMRKLRDHNVRTPSNLDILELHTREVLKRLEMCPWEEDLLSSKLNGKFNKHLQPSSTVPEWRAKDNDLRLLLTNGRIIKDERQLFADRSLYTADSENEEDKKPTQNANMKTEQSSGREEAESQGSPKPLNRIFTSVRSELRSRPSEYSDGSDSEDSGPDCTALKINFATEDSESSGDEKKHEITSHFKEESDIVRNLLQKSQKPSRQEIPVKRECPTSTSTEEEAIQGMLSMAGLHYSSCLQRQIQSTDCSGEKNSLQDPSSCHGSNPEFRQLYRCNKPVEFGYHAKTEDQDLMTSSWNKQFDRTSRFNAQDLSRSQKHIKKESSSEINQKAQSRHCVDSNSSSIQNGKYTLNPSLVSCQISNGSLSPERPIGETSFSMPLHPTKRPASNPPPISNQATKGKRPKKGMATAKQRLGKILKLNRNGHARFFV
Protein: Toll-like receptor (A0A096MKA9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU363040}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU363040}.
Interaction partners:
Sequence:
MVKSLWDSLCNMSQDREPIVESFHFVCTLALIVGSMTQFSDEFESVVDYSNKNLTHVPKDLSPSTKSLSLSQNSISDLQMSDISFLSELRVLRLSHNRIRRLDFGVFLLNRDLEYLDVSHNQLQNISCCPMVNLKHLDLSFNDFEVLPVYKEFGNLMKLSFLGLSAAKFRQLDLLPISHLHLSCVLLDLVNYQIKDGETESLQVPNTNVLHLVFHPNSLFSVQVNISVNALGCLQLSNIKLNDKNCQSLIIFLSELTRGPTLLNLTLQHIETNWKCFVRLLQFLWPRPVEYLNIYNLTITESISRETFIYVETVLKSLKIEHVTNQVFLFVKDALYSVFAEMNIRMLTLSDTPFIHMVCPEFPSTFAFLNFTQNVFTDSIFQGCSTLKRLETLILQRNGLKNLFKVALMTKTMSSLETLDVSLNSLNSHVYDRTCAWAESIRVLNLSSNVLSDSVFRCLPPKVKVLDLHNNRIVSIPKDVTHLQALQELNVASNFLTDLPGCGAFSSLSVLVIDHNSVSHPSSDFFQSCQNIRSITAGNNPFRCTCELREFVKNIGQASREVVEGWPDSYRCDYPDSIKGTPLQDFHMSPLSCDTILLTVTIGATLLLLAAIGASLCLYFDLPWYLRMLWQWTQTRHRARNIPLEELQRNLQFHAFVSYSEHDSAWVKNELLPNLEKDDIRVCLHERNFVPGKSIVENIIHFIEKSYKSIFVLSPHFIQSEWCHYELYFAHHNLFHEGSDNLILILLEPIQQNNIPSRYHKLRALMAQRTYLEWPIEKGKRGLFWANLRASFIMKLALVNENDVKT
Protein: Uncharacterized deaminase C1683.02 (EC 3.5.4.-) (Q9P6J8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenosine kinase
- Putative purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase
- IMP-specific 5'-nucleotidase 1
- Adenine deaminase
- Inosine-5'-monophosphate dehydrogenase
- Probable guanine deaminase
- Cell polarity protein alp11
- Uricase
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15
Sequence:
MTDIERFIEKLPKAELHLHLEGTLEAELKLKLSHRNKIPLKQSSIEEIKESYNFHDLASFLEVYYEGVELLLHEQDFYDLCYQYLRKAASQNVVYAEMFFDPQLHTRRGISFETVIKGLIRARDDAMRDFHIYSQLIMCFIREMSFENAEETLNASLPYKSEIIGIGLDSNEENNPPIKFLKVFQRARQLGYRLTCHCDLHQKNTTTHIRQALEDIGVERIDHGINILDDPELIKLALERNIPFTVCPFSNEIVYPGKAQPEIRIMLDTGLKVTINSDDPAYMHCFYITENFNLAQKGASLTKKELVQICRNSFEAAWISEEKRNHYLEALNSFASAYD
Protein: Probable arabinan endo-1,5-alpha-L-arabinosidase A (EC 3.2.1.99) (Endo-1,5-alpha-L-arabinanase A) (ABN A) (A2QT85)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MYRLLSVASVPLLASLVHGYADPGACSGVCTTHDPGLIRRESDGTYFLFSTGNKISYVSASSIEGPWTSVGSMLPDGSSIDLDGNDDLWAPDVSYVDGLYYVYYAVSTFGSQDSAIGLATSETMEYGSWTDHGSTGIASSSAKIYNAIDPNLIYADGTYYINFGSFWDDIYQVPMKSTPTAAASSSYNLAYDPSGTHAEEGSYMFQYGDYYYLFYSAGICCGYDTSMPASGEEYHIKVCRSTSPTGDFVDSDGTACTDGGGTMVLESHGEVYGPGGQGVYDDPNLGPVLYYHYMNTTIGYADSDAQFGWNTIDFSSGWPVV
Protein: Ribosome maturation factor RimP (O25687)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Required for maturation of 30S ribosomal subunits.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01077}.
Interaction partners:
- Small ribosomal subunit protein uS12
- Ribosome-binding factor A
- YlxR domain-containing protein
- Translation initiation factor IF-2
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS7
- Ribosomal RNA small subunit methyltransferase A
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS6
Sequence:
MTKKIEEKIGGVIESLGYLLYDVSLVKENEQHVLRVSLKNPNGAVSLDICQQVSEIISPLLDVCDFIQDAYILEVSSMGLERTLKTPKHFKLSLGEKVEVKLTNKESFQAVLKDANDLSADFELEDHAIKSVEYKDLKKVKTLFEW