wanglab/gogpt-training-data huggingface dataset:
Protein: G protein-activated inward rectifier potassium channel 4 (GIRK-4) (Cardiac inward rectifier) (Heart KATP channel) (Inward rectifier K(+) channel Kir3.4) (KATP-1) (Potassium channel, inwardly rectifying subfamily J member 5) (F1MYR9)
Organism: Bos taurus (Bovine)
Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.Can be blocked by external barium.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P48548}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G protein-activated inward rectifier potassium channel 1
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Gamma-aminobutyric acid type B receptor subunit 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Guanine nucleotide binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Calcium-transporting ATPase
Sequence:
MAGDSRNAMNQDMEIGVTPRDPKKIPKQARDYIPIATDRTRLLSEGKKPRQRYMEKSGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTITWLFFGFIWWLIAYIRGDLDHVGDREWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIVLLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISLRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIICHEINEKSPFWEMSRAQLTQEEFEVVVILEGMVEATGMTCQARSSYMDTEVLWGHRFTPVLTLEKGFYEVDYNTFHDTYETNTPSCCAKELAEMKREGRLLQYHPSPPLPGGCVGAELGAEAEQEGEEEPEGLSGSQETKDSA
Protein: SNW domain-containing protein 1 (A0A8I5ZP60)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367140}.
Interaction partners:
Sequence:
LISCSFLPAPTQLSQDQLEAEERARSQRSRQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDPEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKDPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPLDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLETRIKTNRFVPDKEFSGSDGRKRGREGPVQFEEDPFGLDKFLEEAKQHGGSKRPSDSSRPKEHEHEGKKRRKE
Protein: Meiotic recombination protein REC8 (Cohesin REC8) (Sporulation protein 69) (Q12188)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Replaces the SCC1 mitosis-specific cohesin to ensure sister chromatid cohesion during meiosis. Is cleaved by ESP1 shortly before the first meiotic division, and dissociates from chromatin, allowing sister chromatids to segregate. Is protected from cleavage by SPO13. Promotes localization of the LINC complex subunit MPS3 on nuclear envelope in mitotic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:10412984, ECO:0000269|PubMed:12101124, ECO:0000269|PubMed:16269332, ECO:0000269|PubMed:30417519}. Chromosome {ECO:0000269|PubMed:10412984, ECO:0000269|PubMed:12101124, ECO:0000269|PubMed:15819623, ECO:0000269|PubMed:16269332}. Chromosome, centromere {ECO:0000269|PubMed:10412984, ECO:0000269|PubMed:16269332}. Note=Localizes at chromosome cores during pachytene. Disappears from chromosome arms shortly before the first meiotic division, but persists in the vincinity of centromeres until the onset of anaphase II. {ECO:0000269|PubMed:10412984, ECO:0000269|PubMed:16269332}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Cohesin subunit SCC3
- Sister chromatid cohesion protein PDS5
- Separin
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Meiosis-specific protein SPO11
- Meiosis-specific protein HOP1
- Structural maintenance of chromosomes protein 1
- Protein RED1
- MutS protein homolog 4
Sequence:
MAPLSLNFKDDKKYKGLTTVWLLSALGNSIVKESNNYYSNKSNSTGNISSSTVKKKDIVNISIPKTCDEIQNFENDFSLRYISNLLYGVTICYNKKTEYVLNDLNHLLVQLQKNDVYAFKAKNKSTRINGLNSNNSIIGNKNNNYTWEECVFFDDDPLYDITKVPALEFLNTTLQDNVSFIEEAKSIRRQDYINELSNSNRFELHGDMTNSDAQSNLGSNVRNSFPLDEIPVDVDFNLDLDDIVSHQGTPLGSHSSSQKDGNDFKFNYQGDELVLNFENDNENNSNGGEDTSVENEGPVANLKDYELGLEAQASEEENDLQQKLNTRMQRGHRADVGGQFSKVQFDAKTSYPNEVLKFNHGNYSHLMEKNRIRKLTGQNFLTSNISSLVRSCGEEEFFSTNWLSIFNDFSNIKTSEWDLYPQGFSSVERGRKRAHSLVSTQSSSSTRSHEYGRKSFRNNKNDNYSSDMENDNLLLNLEQINEDLEDGHYIEENSQGNILDFNLNLPPSSFGRSHTRNSTRSSGFNEDIVGALRRRVGPSEQNFAEEDDSSNSCFSDGSQQNLQQDKTNFQDVILDYQTKKFYDYIKERSIVVGRTTRSNPPFKRKMLLVDIIPSRMGEAQTGANFDDVERGVSRQIAASAFLSLLNLATKGMVKLNEYPVADAVTKDLKLRREDEIIVYA
Protein: Amine oxidase [copper-containing] 2 (EC 1.4.3.21) (Amine oxidase copper-containing 2) (Retina-specific copper amine oxidase) (RAO) (Semicarbazide-sensitive amine oxidase) (SSAO) (O75106)
Organism: Homo sapiens (Human)
Function: Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:19588076}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19588076}. Note=Either not translocated to the plasma membrane or below detection level. {ECO:0000269|PubMed:19588076}.
Interaction partners:
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Aldehyde dehydrogenase, mitochondrial
- Amine oxidase [copper-containing] 3
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase family 3 member B2
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLELLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRNSPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFINNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVYFEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
Protein: Late embryogenesis abundant protein 6 (Late embryogenesis abundant protein 4-1) (AtLEA4-1) (Q39138)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved dehydration tolerance. Involved in the adaptive response of vascular plants to withstand water deficit. May possess chaperone-like activity under water deficit (By similarity).
Interaction partners:
- Late embryogenis abundant protein 2
- Protein SENESCENCE-ASSOCIATED GENE 21, mitochondrial
- Late embryogenesis abundant protein 7
- Late embryogenesis abundant
- Late embryogenesis abundant protein 29
- Late embryogenesis abundant protein 46
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Outer envelope pore protein 16-2, chloroplastic
- Late embryogenesis abundant protein 31
Sequence:
MQSAKQKISDMASTAKEKMVICQAKADEKAERAMARTKEEKEIAHQRRKAKEAEANMDMHMAKAAHAEDKLMAKQSHYHVTDHGPHVPQQAPVPAPAPVMGHGYGHNPTGVTSVPPQTYHPTYPPTGHHNHHHY
Protein: Cuticle collagen dpy-5 (Protein dumpy-5) (P91285)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment.
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- Cuticle collagen sqt-1
- Phorbol ester/diacylglycerol-binding protein unc-13
- Endoprotease bli-4
- Cuticle collagen 6
- Thioredoxin-related transmembrane protein 1
- Protein unc-119
- Cuticle collagen rol-6
- Band 7 domain-containing protein
- Cuticle collagen dpy-13
Sequence:
MVKAVVGFGAACGISAIVACLWAALVITNDINDMYDDVMGELGGFRDISDDTWGTLLDVRHGAGESAEQYVRGIFGRHKRSNSQCSCGLPSQGCPAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKECIKCPAGPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGEPGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGPQGAVGADAEYCPCPERKRRRV
Protein: Phosphoribosylamine--glycine ligase, chloroplastic (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GARS) (Phosphoribosylglycinamide synthetase) (P52420)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Amidophosphoribosyltransferase 2, chloroplastic
- Amidophosphoribosyltransferase 1, chloroplastic
- Amidophosphoribosyltransferase 3, chloroplastic
- Phosphoribosylglycinamide formyltransferase, chloroplastic
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Phosphoribosylaminoimidazole-succinocarboxamide synthase, chloroplastic
- AICARFT/IMPCHase bienzyme family protein
- Adenylosuccinate lyase
- phosphoribosylaminoimidazole carboxylase
- Adenylosuccinate lyase
Sequence:
MSSLCASNCYPSSSSINLFSNNNNPTKPFLLSLRFASSNSLPFVAPLKFSTTNHVLSNSRFSSNRIQRRLFLLRCVSEESQPSLSIGNGGSEERVNVLVIGGGGREHALCHALKRSPSCDSVLCAPGNAGISSSGDATCVPDLDISDSLAVISFCQKWNVGLVVVGPEVPLVAGLANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGVTVAMELEEAFEAVDSMLVKGVFGSAGCQVVVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTKELQDFVMESIIHPTVKGMAEEGCKFVGVLFAGLMIEKKSGLPKLIEFNVRFGDPECQVLMMRLESDLAKVLLAACKGELSGVSLDWSKDSAMVVVMASNGYPGSYEKGSIIKNLEEAERVAPGVKVFHAGTGLDSEGNVVATGGRVLGVTAKGKDLEEARERAYSAVQQINWPGGFFRHDIGWRALRQKQVATKEE
Protein: ATP-dependent RNA helicase DDX19A (EC 3.6.4.13) (DDX19-like protein) (DEAD box protein 19A) (Q9NUU7)
Organism: Homo sapiens (Human)
Function: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UMR2}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMR2}. Note=Associates with the nuclear pore complex cytoplasmic fibrils. {ECO:0000250|UniProtKB:Q9UMR2}.
Interaction partners:
- Nuclear pore complex protein Nup214
- MIF4G domain-containing protein
- ATP-dependent RNA helicase DDX19B
- CBP80/20-dependent translation initiation factor
- mRNA export factor GLE1
- Nuclear pore complex protein Nup88
- NACHT, LRR and PYD domains-containing protein 3
- ATP-dependent RNA helicase DDX25
- Golgi SNAP receptor complex member 1
- Nuclear pore glycoprotein p62
Sequence:
MATDSWALAVDEQEAAVKSMTNLQIKEEKVKADTNGIIKTSTTAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
Protein: Uncharacterized protein C3G6.07 (O14143)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSEQSSPYLTLAPADYEGEDVSNEKEKNSVIPDVIDYYNKGRQYYQSFVVYKATANTIFQFSYLLYIYIDLTKADQTEVLQFLKTYVEDESFVGDDFVMPKYTLVLPYRVYRDHVKKHGDIITPK
Protein: Crabp2b protein (A4VCG2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MESNTEKTFADFSGSWKMKSSENFEELLKALGVNVFLRKIAVAAASKPAVEISQQGESLSVQTSTSVRTTHVSFTVGESFNETTVDGRPCTSFPKWETDCKIYCEQTLQKGEGPETSWTRELTNDGQMILTMRAGDVVCTRVYERD
Protein: CDP-diacylglycerol pyrophosphatase (EC 3.6.1.26) (CDP-diacylglycerol phosphatidylhydrolase) (CDP-diglyceride hydrolase) (P06282)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Single-pass membrane protein.
Interaction partners:
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Uncharacterized protein YnbB
- Diacylglycerol kinase
- Protein UshA
- UDP-2,3-diacylglucosamine hydrolase
Sequence:
MKKAGLLFLVMIVIAVVAAGIGYWKLTGEESDTLRKIVLEECLPNQQQNQNPSPCAEVKPNAGYVVLKDLNGPLQYLLMPTYRINGTESPLLTDPSTPNFFWLAWQARDFMSKKYGQPVPDRAVSLAINSRTGRTQNHFHIHISCIRPDVRKQLDNNLANISSRWLPLPGGLRGHEYLARRVTESELVQRSPFMMLAEEVPEAREHMGRYGLAMVRQSDNSFVLLATQRNLLTLNRASAEEIQDHQCEILR
Protein: GH27752p (Q9VQI4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH20441p
- GH06435p
- GH03227p
- Cytosol aminopeptidase
- GH18325p
- GH07855p
- Uncharacterized protein, isoform E
- GH17939p
- GH14622p
- AT18965p
Sequence:
MMLSTYQHDYVPPSAKRYEFLTRPRGAEAHSGPQVKECECVDESKIMMPPNASKDCGGVEWTGIAPMGKLVDPRIIPTQLTQDQVDKMAFSAETDCFKLQPNRFLKILRTVYPDLYERLKVMPKEELSRRLETNRMNTTYQIDYCNMNEYPEGIYESLKTEDESKNANKLMSERGPCNEFRSNVMNELEREASAGYEMSSDECQKNYKPFKTSFSDSSQTIESGSSSHWNSAPTTYRKVPTFSEYMDSISRNGCVIMRNKLHDHSKCLAKYCKHELKFTCTDMK
Protein: Homeobox protein unplugged (Q4V5A3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a regulatory role in neural branching of the tracheae: segment-specific aspects of these neural branching patterns appear to be generated by homeotic regulation of expression. May have a role with oc/otd in the postembryonic development of the brain.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:8582298}. Note=In tracheal precursor cells as they migrate and extend. {ECO:0000269|PubMed:8582298}.
Interaction partners:
Sequence:
MERPALLQNGEIGTMESPTTRLASKPFPKPFSIESLIANQTPATATPPSPPEERDQEQEAEQEQELSARAMVASSALGLTQFPLYNPWLHGYFAQNHERLTHLIAGGCYLPSSPAGHPAAQQPQAQAQPQPPPPHPPTHALEKQLPPTLPHPLDTRFLPFNPAAAGVAPTDLSYRRLAELMNQDYVHSLSVHARLQHMAAAGRMHEDQANPGMAQLQEPTPPQAHSSPAKSGSHSPMEPALDVGMDEDFECSGDSCSDISLTMSPRNYNGEMDKSRNGAYTNSDSEDCSDDEGAQSRHEGGGMGGKDSQGNGSSSNSKSRRRRTAFTSEQLLELEREFHAKKYLSLTERSQIATSLKLSEVQVKIWFQNRRAKWKRVKAGLTSHGLGRNGTTSGTKIVVPIPVHVNRFAVRSQHQQLEKMCLSGPKPDLRKKLSAEAIGGFEKFSGSTNASSPSGGPVGLGVGVGVGVGVGLGVSTPLSLARSIY
Protein: Immune protein Tsi6 (Q9I740)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Immunity protein that plays a role in preventing early activation of toxin Tse6.
Interaction partners:
- NAD
- Effector EagT6
- Type VI secretion system spike protein VgrG1a
- Four-helix bundle copper-binding protein
- Immune protein Tsi7
- Type VI secretion system spike protein VgrG1b
- Toxin protein Tse5
- Immune protein Tsi1
- Immune protein Tsi3
- DNase toxin Tse7
Sequence:
MTPIEYIDRALALVVDRLARYPGYEVLLSAEKQLQYIRSVLLDRSLDRSALHRLTLGSIAVKEFDETDPELSRALKDAYYVGIRTGRGLKVDLP
Protein: Rho-GTPase-activating protein RGD3 (P38870)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:32941095}; Peripheral membrane protein {ECO:0000269|PubMed:32941095}. Cell membrane {ECO:0000269|PubMed:32941095}; Peripheral membrane protein {ECO:0000269|PubMed:32941095}. Bud tip {ECO:0000269|PubMed:32941095}. Bud neck {ECO:0000269|PubMed:22842922, ECO:0000269|PubMed:32941095}. Note=Relocalizes from bud neck to cytoplasm upon DNA replication stress (PubMed:22842922). Localizes to dynamic polarized vesicles that, while distinct from constitutive secretory vesicles, are dependent on actin and MYO2 function (PubMed:32941095). {ECO:0000269|PubMed:22842922, ECO:0000269|PubMed:32941095}.
Interaction partners:
- Uncharacterized protein YHR180W
Sequence:
MSVKEHNEEDIIGDELQNSRQLSIDCDSVKISLRNTYWTKDYTTGIKLFIKHMKRENDLLIKDIKFYNDFVNKFWKPTLNNLQKMEATNSMNSRLLEVMSKQFNIISTEQVERDCKIPLQELRDLNESFLREAENDLSSRYSAYIKDLVAAKEALIGCEKRVQSIYKLKKANTPVENSSSVFDNGKDSAPLTRLNFVCEFPYTLDERLKFEDCDQFMSFLQTLKGKVILEKSVFSVPGLSNQSFQGRSLIKELKKLEPRLNLSLFNIDRIGNEFIQLGIIQEYSLSFYSSKVSQFDQEKYYYWNSEVLATQESNGNAGNRKKKSYGELTHSDNEHEEKSNVSSIKTSISDWIRKVSQHDNDDCDAAGSTDMNKNEWKSLKQQLESSQDIFFSKCCQLEYSKVQLEKTIYDYCKNYSKMEDGIKRALESSNMMFQQKCEKFTDSPVCSLQEAQLPQETANADVRGFFLRDNGIPFRRWNILEASDPVDACKEISIKSEKFFCGSEINNELAALDTLGAIKIILRQIEKEPNANKVIQSWHRDIDFVRVSNLKRDLLGEFKGSKTTENTNSIITAHFFENSHSYVTNDLVGLIKLWLLELPDSLIPSNHYDDLIKAEKSLTSLCEQFPTSSLRFLQELANHFQLINSKYSLPPQTIQDLFRDNSDIDIPLAHHFVRRTGLQNPIDIKILSPTLSTFFINERTVETLQTLIANRITTATTATLTEPPTIIIKDTTAPIHSTPKPPPNDKDGHFIPRPFKTSSTPTTPERPKRKSGLFLPINVNDVPST
Protein: Large ribosomal subunit protein eL31z (60S ribosomal protein L31-1) (Q9SLL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein eL32z
- Small ribosomal subunit protein eS24y
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein eL42z/eL42y
- Small ribosomal subunit protein eS1y
- Large ribosomal subunit protein uL24y
Sequence:
MEKGKGRKEEVVTREYTINLHRRLHSCTFKKKAPNAIKEIRKFALKAMGTKDVRVDVKLNKQIWSKGIRGPPRRIRVRVARKRNDDEDAKEEFFSLVTVAEIPAEGLSGLGTKVIEEEE
Protein: ASPSCR1 tether for SLC2A4, UBX domain containing (J3KRY8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKCYDPVGKTPGSLGSSASAGQAAASAPLPLESGELSRGDLSRPEDADTSGPCCEHTQEKQSTRAPAAAPFVPFSGGGQRLGGPPGPTRPLTSSSAKLPKSLSSPGGPSKPKKSKSGQDPQQEQEQERERDPQQEQERERPVDREPVDREPVVCHPDLEERLQAWPAELPDEFFELTVDDVRRRLAQLKSERKRLEEAPLVTKAFREAQIKEKLERYPKVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLGNPELSFYLFITPPKTVLDDHTQTLFQANLFPAALVHLGAEEPAGVYLEPGLLEHAISPSAADVLVARYMSRAAGSPSPLPAPDPAPKSEPAAEEGALVP
Protein: Ferric uptake regulation protein (Ferric uptake regulator) (P0A3E5)
Organism: Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Function: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSDQSELKNMGLKATFPRLKILDIFRKSDLRHLSAEDVYRALIAENVEIGLATVYRVLTQFEQAGILTRSQFDTGKAVFELNDGDHHDHLICTNCGTVFEFSDPDIEKRQYKVAKDNGFVLESHAMVLYGICGNCQKGR
Protein: Uncharacterized protein YDL157C, mitochondrial (Q12082)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Peroxisomal membrane protein PEX34
Sequence:
MSNILAVFNPPPQRELEKEETMDCVPCQVMSTMFSVGFGSYLASGKPFKYGKKEAKRGISLTEFEKRNPQWWKVTLRSFGGLLIAFGFVRGTEGWLWHKNKEYKNYKKLSNDGETQAN
Protein: DUF866-domain-containing protein (Q59YD2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm2
- U2 snRNP complex subunit
- U1 small nuclear ribonucleoprotein C
- Sm protein B
- Sm domain-containing protein
- Small nuclear ribonucleoprotein Sm D1
- V-type ATPase assembly factor PKR1
Sequence:
MVKFLLKASAELSNVTGLEPSDTPEHPYEYTFQIECTKCRTTHDKDIQINQYEKHEISGSRGEASFVFRCKECKHEHSASILRTNEKLSTTEDSVNDKASATILEIDARGIDFLKFIPIGEFSAVGSETNTKFADIDLSEGEWYDVDEKSNDEVSIVDVSWEISRS
Protein: Cytochrome c oxidase subunit 7A2-like, mitochondrial (Cytochrome c oxidase subunit 7A-related protein) (Supercomplex assembly factor 1) (Q61387)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of oxidative phosphorylation and energy metabolism. Necessary for the assembly of mitochondrial respiratory supercomplex.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q99KD6}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MYYKFSSFTQKLAGAWASEAYTPQGLKPVSTEAPPIIFATPTKLTSSVTAYDYSGKNKVPELQKFFQKADGFHLKRGLPDQMLYRTTMALTLGGTIYCLIALYMASQPRNK
Protein: Metal transporter CNNM4 (Ancient conserved domain-containing protein 4) (Cyclin-M4) (Q6P4Q7)
Organism: Homo sapiens (Human)
Function: Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22399287}; Multi-pass membrane protein {ECO:0000269|PubMed:22399287}.
Interaction partners:
- Cystathionine beta-synthase
- Cytochrome c oxidase assembly protein COX11
- Cystathionine beta-synthase-like protein
- Protein tyrosine phosphatase type IVA 2
- Protein tyrosine phosphatase type IVA 1
- Matrix metalloproteinase-20
- Solute carrier family 41 member 1
- GMP synthase
Sequence:
MAPVGGGGRPVGGPARGRLLLAAPVLLVLLWALGARGQGSPQQGTIVGMRLASCNKSCGTNPDGIIFVSEGSTVNLRLYGYSLGNISSNLISFTEVDDAETLHKSTSCLELTKDLVVQQLVNVSRGNTSGVLVVLTKFLRRSESMKLYALCTRAQPDGPWLKWTDKDSLLFMVEEPGRFLPLWLHILLITVLLVLSGIFSGLNLGLMALDPMELRIVQNCGTEKERRYARKIEPIRRKGNYLLCSLLLGNVLVNTSLTILLDNLIGSGLMAVASSTIGIVIFGEILPQALCSRHGLAVGANTILLTKFFMLLTFPLSFPISKLLDFFLGQEIRTVYNREKLMEMLKVTEPYNDLVKEELNMIQGALELRTKTVEDIMTQLQDCFMIRSDAILDFNTMSEIMESGYTRIPVFEDEQSNIVDILYVKDLAFVDPDDCTPLKTITRFYNHPVHFVFHDTKLDAMLEEFKKGKSHLAIVQKVNNEGEGDPFYEVLGLVTLEDVIEEIIKSEILDESDMYTDNRSRKRVSEKNKRDFSAFKDADNELKVKISPQLLLAAHRFLATEVSQFSPSLISEKILLRLLKYPDVIQELKFDEHNKYYARHYLYTRNKPADYFILILQGKVEVEAGKENMKFETGAFSYYGTMALTSVPSDRSPAHPTPLSRSASLSYPDRTDVSTAATLAGSSNQFGSSVLGQYISDFSVRALVDLQYIKITRQQYQNGLLASRMENSPQFPIDGCTTHMENLAEKSELPVVDETTTLLNERNSLLHKASHENAI
Protein: U2 snRNP component ist3 (Complexed with cdc5 protein 29) (RNA-binding protein cwf29) (O94290)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for pre-mRNA splicing and spliceosome assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cdc5
- Spliceosome-associated protein 49
- Pre-mRNA-splicing factor sap145
- U2 snRNP component prp10
- Pre-mRNA-splicing factor ini1
- Pre-mRNA-splicing factor prp12
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor dre4
- Pre-mRNA-splicing factor sap62
- Pre-mRNA-splicing factor cwf26
Sequence:
MNSIRQIERLNEQELDKPFSSSWHQDYSDSAYIYIGNLDFDLNEDDILCVFSEFGEPVDINLVRDKETGKSKGFAFLKYEDQRSTVLAVDNMTNVKLLDRLVRVDHVASYKVPQKEKEPANLVPLGESGSSLSVSTINTSNLPDHDYKTIIQNEVEQTLSPKDEKDLLDPMRDYIHREKRRKLKHESSDRSDKSDSNRHSRHHRRHSRSRRHRDLDG
Protein: 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA (3',5'-cyclic AMP phosphodiesterase) (cAMP phosphodiesterase) (EC 3.1.4.53) (P0AEW4)
Organism: Escherichia coli (strain K12)
Function: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specific for cAMP.
Interaction partners:
- Adenylate cyclase
- Esterase YqiA
- Uncharacterized protein YqiB
- DNA-binding transcriptional dual regulator CRP
- ADP-ribose pyrophosphatase
- Nucleoside triphosphate pyrophosphohydrolase
- Protein UshA
- 5'/3'-nucleotidase SurE
- Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase
- Adenylate kinase
Sequence:
MESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHTLLLLHHHPLPAGCSWLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIAPGWRTLELHADGTLTTEVHRLADTRFQPDTASEGY