wanglab/gogpt-training-data huggingface dataset:
Protein: Probable zinc metalloprotease EGY1, chloroplastic (EC 3.4.24.-) (Protein AMMONIUM OVERLY SENSITIVE 1) (Protein ETHYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN 1) (AtEGY1) (Q949Y5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane-associated and ATP-independent metalloprotease required for development of both thylakoid grana and well-organized lamellae in chloroplast. Required for the accumulation of chlorophyll and chlorophyll a/b binding (CAB) proteins (from both PS I and PS II) in chloroplast membranes, and for grana formation and normal chloroplast development. Involved in the regulation of nuclear gene expression in response to ammonium stress and interacts with ABA signaling. Carries out beta-casein degradation in an ATP-independent manner in vitro.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes in endodermal and cortex plastids.
Interaction partners:
- Stigma-specific STIG1-like protein 4
- Rhodanese-like domain-containing protein 4A, chloroplastic
- Inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Membrane-bound transcription factor site-2 protease homolog
- ATP-dependent zinc metalloprotease FTSH 2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP28, chloroplastic
- ENHANCED DISEASE RESISTANCE protein
- Putative methyl-CpG-binding domain protein 12
- Protein LHCP TRANSLOCATION DEFECT
- Hyperosmolality-gated Ca2+ permeable channel 1.8
Sequence:
MGTLTSVAFAAAVNIRFRSFHRENIKTTITTLPKWQKRLCFSSTEDSHRFRIAKCLGNDENSNRDDSIGENGETHKSSVVKTATFEEEDEETSKSSSTTSSSNEFGSDKTSMPSTIDPTYSSFQIDSFKLMELLGPEKVDPADVKLIKDKLFGYSTFWVTKEEPFGDLGEGILFLGNLRGKKEDVFAKLQRKLVEVASDKYNLFMIEEPNSEGPDPRGGARVSFGLLRKEVSEPGPTTLWQYVIALILFLLTIGSSVELGIASQINRLPPEVVKYFTDPNAVEPPDMELLYPFVDAALPLAYGVLGILLFHELGHFLAAVPKKVKLSIPYFIPNITLGSFGAITQFKSILPDRSTKVDISLAGPFAGAALSVSMFAVGLFLSTEPDAANDLVQVPSMLFQGSLLLGLISRATLGYAALHAATVSIHPLVIAGWCGLTTTAFNMLPVGCLDGGRAVQGAFGKNALVTFGLSTYVMLGLRVLGGPLALPWGLYVLICQRTPEKPCLNDVTEVGTWRKALVGIALILVVLTLLPVWDELAEEVGIGLVTTF
Protein: Roundabout 3 (Q9GPP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLRFVFIVFLLKWTHAQGSHPPRIVEHPIDTTVPRHEPATLNCKAEGSPTPTIQWYKDGVPLKILPGSHRITLPAGGLFFLKVVNSRRETDAGIYWCEAKNELGVARSRNATLQVAVLRDEFRLEPQNTRIAQGDTALLECAAPRGIPEPTVTWKKGGQKLDLEGSKRVRIVDGGNLAIQDARQTDEGQYQCIAKNPVGVRESSLATLKVHVKPYIIRGPHDQTVLEGASVTFPCRVGGDPMPDVLWLRTASGGNMPLDRVSVLEDRSLRLERVTIADEGEYSCEADNVVGAITAMGTLTVYAPPKFIQRPASKSVELGADTSFECRAIGNPKPTIFWTIKNNSTLIFPGAPPLDRFHSLNTEEGHSILTLTRFQRTDKDLVILCNAMNEVASITSRVQLSLDSQEDRPPPIIISGPVNQTLPIKSLATLQCKAIGLPSPTISWYRDGIPVQPSSKLNITTSGDLIISDLDRQQDQGLYTCVASSRAGKSTWSGFLRIELPTNPNIKFYRAPEQTKCPSAPGQPKILNATASALTIVWPTSDKAGASSFLGYSVEMYCTNQSRTWIPIASRLSEPIFTVESLTQGAAYMFIVRAENSLGFSPPSPISEPITAGKLVGVRDGSESTGTSQLLLSDVETLLQANDVVELLEANASDSTTARLSWDIDSGQYIEGFYLYARELHSSEYKMVTLLNKGQGLSSCTVPGLAKASTYEFFLVPFYKSIVGKPSNSRRMRTLEDVPEAPPYGMEAIQFNRTSVFLKWLPPQPNRTRNGILTSYNVVVKGLDVHNTTRIFKNMTIDAATPTLLLANLTTGVTYYIAVAAATRVGVGPFSKPAVLRIDARTQSLDTGYTRYPISRDIADDFLTQTWFIVLLGSIIAIIVFLLGALVLFKRYQFIKQTSLGSLHGNHAIGTVRKFPTLPLNGGGAVGAGGSNSTAAAGQSGHGLWIDPTSGVWRQAAGGGNPGGVGSCTTKEQLPGYAQATAQQGQQPTLLPDYERLSPLNMPDYAEVACSTFKSPTHGAPPMGGGGGGQSASLYDSCGAYATTNVVANVKLYQNRYATKPSQSSGSNNNNHQGNDYQSTGMYSAPPSAHYGCLEPKQQQQQQQPNLMTTSTASTAILTNSPAKVKKINITENKMDQLEGKSERTNPFNQQQQLLLASNALKQGLGAYANTTLAAQMASGGGAGTLRRQRQPKTLYKSENNILGKSGLRQNTMNASVGAPSNGQMDFLTGGPPSEGGDFSGLGLCNSTNQLLNDWASSASIAAPGDYHFGSKQPSKQHLYVKAKDGTWSAVSSDAYQSFKHQQQHHPFLAGSGDNTKSLASVNSLAGDSKFLSSFGSSANV
Protein: Succinylglutamate desuccinylase (EC 3.5.1.96) (P76215)
Organism: Escherichia coli (strain K12)
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Interaction partners:
- N-succinylglutamate 5-semialdehyde dehydrogenase
- N-succinylarginine dihydrolase
- Succinylornithine transaminase
- Arginine N-succinyltransferase
- Bifunctional protein PutA
- Gamma-glutamyl phosphate reductase
- NADP-specific glutamate dehydrogenase
- Glutaminase 1
- Glutaminase 2
- Glutamate synthase large chain
Sequence:
MDNFLALTLTGKKPVITEREINGVRWRWLGDGVLELTPLTPPQGALVISAGIHGNETAPVEMLDALLGAISHGEIPLRWRLLVILGNPPALKQGKRYCHSDMNRMFGGRWQLFAESGETCRARELEQCLEDFYDQGKESVRWHLDLHTAIRGSLHPQFGVLPQRDIPWDEKFLTWLGAAGLEALVFHQEPGGTFTHFSARHFGALACTLELGKALPFGQNDLRQFAVTASAIAALLSGESVGIVRTPPLRYRVVSQITRHSPSFEMHMASDTLNFMPFEKGTLLAQDGEERFTVTHDVEYVLFPNPLVALGLRAGLMLEKIS
Protein: Carminomycin 4-O-methyltransferase DnrK (COMT) (EC 2.1.1.292) (Anthracycline 4-O-methyltransferase) (Q06528)
Organism: Streptomyces peucetius
Function: Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 4-O-position of carminomycin to form daunorubicin. In vitro, it also methylates the anthracyclines rhodomycin D (10-carbomethoxy-13-deoxycarminomycin) and 13-deoxy-carminomycin at the 4-hydroxyl position. It is quite specific with respect to the length of the carbohydrate chain at the C7 position, but it can accept substrates with bulky substituent at C10 position.
Interaction partners:
Sequence:
MTAEPTVAARPQQIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTDTRPEALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQRAWHDLTQAVARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLRASFDSLLACDQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVLEMAGTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSFVLLNWPDHDAVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLRMLVFLGGALRTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPAATGA
Protein: POU domain, class 4, transcription factor 1 (Brain-specific homeobox/POU domain protein 3A) (Brain-3A) (Brn-3A) (Homeobox/POU domain protein RDC-1) (Oct-T1) (Q01851)
Organism: Homo sapiens (Human)
Function: Multifunctional transcription factor with different regions mediating its different effects. Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor. Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain). Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins. Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity. May positively regulate POU4F2 and POU4F3. Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord. Plays a role in TNFSF11-mediated terminal osteoclast differentiation. Negatively regulates its own expression interacting directly with a highly conserved autoregulatory domain surrounding the transcription initiation site.
Subcellular location: Nucleus {ECO:0000269|PubMed:12934100}. Cytoplasm {ECO:0000250|UniProtKB:P17208}.
Interaction partners:
- Neurogenin-1
- Neurogenin-2
- GTP-binding protein Rit2
- Transcription factor ATOH1
- LIM/homeobox protein Lhx9
- Cellular tumor antigen p53
- Achaete-scute homolog 1
- Insulin gene enhancer protein ISL-1
- Visual system homeobox 2
- RNA-binding protein with multiple splicing
Sequence:
MMSMNSKQPHFAMHPTLPEHKYPSLHSSSEAIRRACLPTPPLQSNLFASLDETLLARAEALAAVDIAVSQGKSHPFKPDATYHTMNSVPCTSTSTVPLAHHHHHHHHHQALEPGDLLDHISSPSLALMAGAGGAGAAAGGGGAHDGPGGGGGPGGGGGPGGGPGGGGGGGPGGGGGGPGGGLLGGSAHPHPHMHSLGHLSHPAAAAAMNMPSGLPHPGLVAAAAHHGAAAAAAAAAAGQVAAASAAAAVVGAAGLASICDSDTDPRELEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEGAQREKMNKPELFNGGEKKRKRTSIAAPEKRSLEAYFAVQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKFSATY
Protein: DNA-directed RNA polymerases I and III subunit RPAC1 (DNA-directed RNA polymerase I subunit C) (RNA polymerases I and III subunit AC1) (AC40) (DNA-directed RNA polymerases I and III 40 kDa polypeptide) (RPA40) (RPA39) (RPC40) (O15160)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:26151409, ECO:0000269|PubMed:33335104}. Nucleus, nucleolus {ECO:0000269|PubMed:34887565}. Cytoplasm, cytosol {ECO:0000269|PubMed:33335104}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerase III subunit RPC7
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MAASQAVEEMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEGTIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGEAAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIFSVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
Protein: Probable G-protein coupled receptor 174 (Q9BXC1)
Organism: Homo sapiens (Human)
Function: Putative receptor for purines coupled to G-proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MPANYTCTRPDGDNTDFRYFIYAVTYTVILVPGLIGNILALWVFYGYMKETKRAVIFMINLAIADLLQVLSLPLRIFYYLNHDWPFGPGLCMFCFYLKYVNMYASIYFLVCISVRRFWFLMYPFRFHDCKQKYDLYISIAGWLIICLACVLFPLLRTSDDTSGNRTKCFVDLPTRNVNLAQSVVMMTIGELIGFVTPLLIVLYCTWKTVLSLQDKYPMAQDLGEKQKALKMILTCAGVFLICFAPYHFSFPLDFLVKSNEIKSCLARRVILIFHSVALCLASLNSCLDPVIYYFSTNEFRRRLSRQDLHDSIQLHAKSFVSNHTASTMTPELC
Protein: N(6)-adenosine-methyltransferase non-catalytic subunit METTL14 (Methyltransferase-like protein 14) (hMETTL14) (Q9HCE5)
Organism: Homo sapiens (Human)
Function: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis. In the heterodimer formed with METTL3, METTL14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing. M6A acts as a key regulator of mRNA stability by promoting mRNA destabilization and degradation (By similarity). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (By similarity). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (By similarity). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421, ECO:0000269|PubMed:26458103, ECO:0000269|PubMed:29348140}.
Interaction partners:
- RNA-binding protein 15
- Pre-mRNA-splicing regulator WTAP
- E3 ubiquitin-protein ligase Hakai
- Protein virilizer homolog
- Zinc finger CCCH domain-containing protein 13
- N
- Putative RNA-binding protein 15B
- RNA N
- N
- Microprocessor complex subunit DGCR8
Sequence:
MDSRLQEIRERQKLRRQLLAQQLGAESADSIGAVLNSKDEQREIAETRETCRASYDTSAPNAKRKYLDEGETDEDKMEEYKDELEMQQDEENLPYEEEIYKDSSTFLKGTQSLNPHNDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLEEYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLDPKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPGWLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERLRPKSPPPKSKSDRGGGAPRGGGRGGTSAGRGRERNRSNFRGERGGFRGGRGGAHRGGFPPR
Protein: Cadherin-7 (Q90763)
Organism: Gallus gallus (Chicken)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin alpha-2
- Uncharacterized protein.
- Catenin beta 1
- Plakoglobin
Sequence:
MKLGKVEFCHLLQIIALFLCLSGMNQAEPSRSRSKPYFQSGRTRTKRSWVWNQFFVLEEYMGSDPLYVGKLHSDVDKGDGSIKYILSGEGASSIFIIDENTGDIHATKRLDREEQAYYTLRAQAHDRLTNKPVEPESEFVIKIQDINDNEPKFLDGPYTAGVPEMSPVGTSVVQVTATDADDPTYGNSARVVYSILQGQPYFSVEPKTGIIKTALPNMDREAKDQYLLVIQAKDMVGQNGGLSGTTSVTVTLTDVNDNPPRFPRRSYQYNVPESLPLASVVARIKAADADVGPNAEMEYKIVDGDGLGVFKISVDKDTQEGIITIQKELDFEAKTSYTLRIEAANMHVDPRFLSLGPFSDMTTVKIIVEDVDEPPVFTSRLYSMVVSEAAKVGTIIGTVAAHDPDASNSPVRYSIDRNTDLERYFNIDANSGVITTAKSLDRETNAVHNITVLAMESQNPAQIGRGYVAITILDINDNAPEFAMEYETTVCENAQPGQIIQKISAIDKDDPPNGHQFYFSLTAEAANNHNFTLQDNKDNTATVLTRRNGFRRQEQSVFYLPIFIVDSGSPSLSSTNTLTIRVCDCDADGIAQTCNAEAYILPAGLSTGALIAILACVLTLLVLVLLIVTMRRRKKEPLIFDEERDIRENIVRYDDEGGGEEDTEAFDMAALRNLNIIRDTKTRRDVTPEIQFLSRPTFKSIPDNVIFREFIWERLKEADVDPCAPPYDSLQTYAFEGNGSVAESLSSLDSISSNSDQNYDYLSDWGPRFKRLADMYGSGPDCLYS
Protein: DNA-directed primase/polymerase protein (EC 2.7.7.102) (EC 2.7.7.7) (A0A3Q2TTB3)
Organism: Gallus gallus (Chicken)
Function: DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them. Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (By similarity). Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as UV lesions, R-loops and G-quadruplexes, to allow DNA replication to continue. Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion (By similarity). Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase (By similarity). Also required for reinitiating stalled forks after ultraviolet (UV) damage during nuclear DNA replication (By similarity). Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides (By similarity). In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96LW4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q96LW4}. Chromosome {ECO:0000250|UniProtKB:Q96LW4}.
Interaction partners:
- Uncharacterized protein
- Replication protein A 70 kDa DNA-binding subunit
- Uncharacterized protein.
- TIMELESS-interacting protein
- Timeless circadian regulator.
- Zinc finger RANBP2-type containing 3.
- HNH domain-containing protein.
- Replication protein A 14 kDa subunit
- Ring finger and WD repeat domain 3.
- ApaG domain-containing protein.
Sequence:
MKRKWEERVKKVEELASYYERNPLPTVYKPRLSKPLQPSRVWKIFCRQADAFRFVKTCKEDVHVFALERNTQNGQRFYLVTTYQELWYYYTKGYKTSLMHCYEVIPEKDACKLYFDLEFYKAANPGADGKDMVAKLIELVSQKLKELYDVNCSARDVLNLDSSTDEKFSRHLIFLPCKTVFKDNIHVGNFVRTILQPAIRLVGSNVAAPIAEGGAGYTSQCSAPTVELDGPLTNLTAVEDASKGWPAIADQRKETETSHHGENSEFSFLIVNNKEGDKQLFVDLGVYTRNRNFRMYKSSKAGKNVILTIAEDNKFVPNCEENVSLEEAYFLSSLVCNVRFEDGTKILSSNFVEEEIKMSAFLRSKTTRSTREPMEGYQESPYPEIDCFVRSLINKDGVQGGIRQWNYFSGEEILVYDISGYRWCENIGRAHRSNNIMILVDLKKEVWYQKCHDPVCREKNFKSQSLPLPSRICLSSLFIEEEDHMVTDERENTEVTSHSNPADLSESSAYLAINTSQDTQWDNASDDAYLVETAEDVELAEAADYSLGYDTEEIPDEVLLEMSWKQDTCSKDDS
Protein: RNA-binding protein 1 (Q02427)
Organism: Drosophila melanogaster (Fruit fly)
Function: Contributes to the activation of female-specific DSX splicing in vivo by recognizing the RBP1 target sequences within the purine-rich polypyrimidine tract of the female-specific 3' splice site.
Subcellular location: Nucleus {ECO:0000269|PubMed:1340470}.
Interaction partners:
- Transformer-2 sex-determining protein
- LD32469p
- LD40489p
- LD29830p
- RNA-binding protein 8A
- Eukaryotic initiation factor 4A-III
- Splicing factor U2AF 50 kDa subunit
- Uncharacterized protein, isoform A
- Splicing factor U2af 38 kDa subunit
- Protein mago nashi
Sequence:
MPRYREWDLACKVYVGNLGSSASKHEIEGAFAKYGPLRNVWVARNPPGFAFVEFEDRRDAEDATRALDGTRCCGTRIRVEMSSGRSRDRRRGEGGSSGRSGSGRYRITPSARTTSTATSSFYNINNLQQQPSSQPQPATFNLQL
Protein: Inward rectifier potassium channel Kirbac3.1 (D9N164)
Organism: Paramagnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)
Function: Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.
Subcellular location: Membrane {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}; Multi-pass membrane protein {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}.
Interaction partners:
Sequence:
MTGGMKPPARKPRILNSDGSSNITRLGLEKRGWLDDHYHDLLTVSWPVFITLITGLYLVTNALFALAYLACGDVIENARPGSFTDAFFFSVQTMATIGYGKLIPIGPLANTLVTLEALCGMLGLAVAASLIYARFTRPTAGVLFSSRMVISDFEGKPTLMMRLANLRIEQIIEADVHLVLVRSEISQEGMVFRRFHDLTLTRSRSPIFSLSWTVMHPIDHHSPIYGETDETLRNSHSEFLVLFTGHHEAFAQNVHARHAYSCDEIIWGGHFVDVFTTLPDGRRALDLGKFHEIAQ
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (P33316)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of 2'-deoxyuridine 5'-triphosphate (dUTP) into 2'-deoxyuridine 5'-monophosphate (dUMP) and inorganic pyrophosphate and through its action efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis. Inhibits peroxisome proliferator-activated receptor (PPAR) activity by binding of its N-terminal to PPAR, preventing the latter's dimerization with retinoid X receptor (By similarity). Essential for embryonic development (By similarity).
Subcellular location: [Isoform 2]: Nucleus {ECO:0000269|PubMed:8631816, ECO:0000269|PubMed:9070952}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion {ECO:0000269|PubMed:8631816, ECO:0000269|PubMed:9070952}.
Interaction partners:
- Thymidylate synthase
- Thymidylate kinase
- Deoxycytidylate deaminase
- Inosine triphosphate pyrophosphatase
- Thymidine kinase 2, mitochondrial
- Nucleoside diphosphate kinase 6
- Nucleoside diphosphate kinase A
- 5'
- Adenylate kinase 9
- Nucleoside diphosphate kinase B
Sequence:
MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
Protein: Cation/H(+) antiporter 19 (Protein CATION/H+ EXCHANGER 19) (AtCHX19) (Q9LUN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May operate as a cation/H(+) antiporter.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- F-actin-capping protein subunit alpha
Sequence:
MASTNVTGQCPGPMKATSNGAFQNESPLDFALPLIILQIVLVVVFTRLLAYFLKPLKQPRVIAEIIGGILLGPSALGRSKAYLDTIFPKKSLTVLDTLANIGLLFFLFLVGLELDFAAIKKTGKKSLLIAIAGISLPFIVGVGTSFVLSATISKGVDQLPFIVFMGVALSITAFPVLARILAELKLLTTDIGRMAMSAAGVNDVAAWILLALAIALSGDGTSPLVSVWVLLCGTGFVIFAVVAIKPLLAYMARRCPEGEPVKELYVCVTLTVVLAASFVTDTIGIHALFGAFVVGIVAPKEGPFCRILTEKIEDLVSGLLLPLYFAASGLKTDVTTIRGAQSWGLLVLVILTTCFGKIVGTVGSSMLCKVPFREAVTLGFLMNTKGLVELIVLNIGKDRKVLNDQAFAILVLMALFTTFITTPIVMLIYKPARKGAPYKHRTIQRKDHDSELRILACFHSTRNIPTLINLIESSRGTGKKGRLCVYAMHLMELSERSSAIAMVHKARNNGLPIWNKIERSTDQMVIAFEAYQHLRAVAVRPMTAISGLSSIHEDICTSAHQKRVAMILLPFHKHQRMDGAMESIGHRFHEVNQRVLQRAPCSVGILVDRGLGGTSQVVASEVAYKVVIPFFGGLDDREALAYGMKMVEHPGITLTVYKFVAARGTLKRFEKSEHDEKEKKEKETDEEFVRELMNDPRGNESLAYEERVVESKDDIIATLKSMSKCNLFVVGRNAAVASLVKSTDCPELGPVGRLLSSSEFSTTASVLVVQGYDPAADTRPLVEEDAEYDQSSRDISDLTA
Protein: RNA polymerase sigma factor (C5ASQ2)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Interaction partners:
- Phyllosphere-induced regulator PhyR
- Anti-sigma factor
Sequence:
MRNDTEATLDRPAMTDGRPKLSDSIRSHLGDHLRSVYDTLGAGEDTPSRFSELIGKLEAALKAQGERIDPEFRNGLLSAVPSLRAFALSLTSNPARSDDLVQDTLLKGWQHRARFQPGTNLNAWLFTILRNIFYSDHRKRVREVEDQDGSYAARLATAPHQGDRLDVEDLQTALAKLPPDQREALVLVGAEGVSYEEAATIMGCKVGTVKSRVSRARGRLAELLGYDEEDLSSDRLIQSAMPDA