wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-sensitive inward rectifier potassium channel 12 (Potassium inwardly rectifying channel subfamily J member 12b) (E7F807)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
- Sodium channel protein type 4 subunit alpha A
Sequence:
MSVGKPHRYNIVSSSEEDVGRHGTMPALGNGFGNGKIQTRRKLRSRFVNKTGQCNVSFAHMDEQSQRYLADIFTTCVDSRWRWMFLLFSLAFVISWLAFGFAFWLIALVHGDLEKPQENFTPCVMQVNSFVAAFLFSVETQTTIGYGFRCVTEECPLAVFMVVFQSIVGCIIDSFMIGAIMAKMARPKKRAETILFSHNAVISMRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRITEEGEYIPLDQIDINVGYDQGLDRIFLVAPLTILHEINEESPLFGINQQDLETSDFEIVVILEGMVEATAMTAQVRSSYLSSEILWGHRFEPVVFEERNQYKVDYSHFHKTYEVPSTPRCSAKDLEDNKSLESGANFCYENELAFISRDEEEQEEDRGERGTELETLSANLNFDQRSYHKESEI
Protein: Two-component response regulator RocA1 (Q9HX68)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- histidine kinase
- histidine kinase
- Cyclic di-GMP phosphodiesterase RocR
- Probable two-component response regulator
- Oxygen sensor histidine kinase NreB
- histidine kinase
- histidine kinase
- Sensor protein
- histidine kinase
Sequence:
MHTVLIVDDHPVIRLAVRVLLEKHGLQVVAETDNGVDAIQLVREHEPDVVILDIGIPKLDGLTVISRIKSLGLRSQVLVLTSQSAEAFCKRCIQVGARGFVNKEEDLNNLINALNAVTAGYTFFPSLTFDTLGTPPERISESELIGLLSDREMIVLQHLAMGYSNKAIGEKLFLSNKTVSTYKTRLLQKLGLGSLVDLAEFAKRNSLIH
Protein: Delta-9 desaturase-like 5 protein (EC 1.14.19.-) (Q9LMI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- F20B24.22
- Lysophospholipid acyltransferase LPEAT1
- Heavy metal-associated isoprenylated plant protein 37
- Amino acid transporter AVT1B
- Cysteine-rich receptor-like protein kinase 42
- GDSL esterase/lipase At2g42990
- Formate dehydrogenase, chloroplastic/mitochondrial
- Phosphoglycerate mutase family protein
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Small ribosomal subunit protein mS47
Sequence:
MCDPIREDGSNKRGAVSKEKRPYIHREWSWADIIRALTVINVHFLCLLAPFNYKWEALRFGFVLYALTSLSITFSYHRNLAHRSFKLPKWLEYPLAYFAVFALQGDPLDWVSIHRFHHQFTDSDRDPHSPIEGFWFSHVWWICDTRYIKYKCGGRNNVMDLKQQWFYWFLRMTIGFHVLMFWTVLYLYGGLPYLTCGGGVGGVIGYHVTWLVNSACHIWGSRSWKTKDTSRNVWWLSLFTMGESWHNNHHAFESSARQGLEWWQIDITWYLIRLFEVLGLATDVKLPSEIQKQKLALTR
Protein: Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Q9HUF1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Interaction partners:
- Peptide methionine sulfoxide reductase MsrB
- DNA polymerase I
- Probable thioredoxin
- Probable thiol:disulfide interchange protein
- Probable thioredoxin
- Thioredoxin family protein
- Thiol:disulfide interchange protein DsbE
- DUF6436 domain-containing protein
Sequence:
MVLRSEILTKKSELPTPDQALPGRESAMPVPEAHFVNGRPLTAPFPAGLQQVLFGMGCFWGAERRLWQQPGVWVTAVGYAGGYTPNPTYDEVCSGLTGHSEVVLVVYNPQETSFEQLLKVFWEAHDPTQGMRQGGDIGTQYRSVIYTFDAAQKAAAMASRESFQAELAKAGYDRITTEIADVPPFYYAEAYHQQYLAKNPNGYCGLGGTGVCLPA
Protein: Eukaryotic translation initiation factor 3 subunit K (K7EK53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIDQAHQEERPIRQILYLGDLLETCHFQAFWQALDENMDLLEGITGFEDSVRKFICHVVGITYQHIDRWLLAEMLGDLSDSQLKVWMSKYGWSADESGQIFICSQEESIKPKNIVEKIDFDSVSSIMASSQ
Protein: Transcription termination factor Rho (EC 3.6.4.-) (ATP-dependent helicase Rho) (P0AG30)
Organism: Escherichia coli (strain K12)
Function: Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPase which utilizes all four ribonucleoside triphosphates as substrates.
Interaction partners:
- Transcription termination/antitermination protein NusG
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- Polyribonucleotide nucleotidyltransferase
- DNA-directed RNA polymerase subunit beta'
- Transcription termination/antitermination protein NusA
- Ribonuclease E
- RNA-binding protein Hfq
- Thioredoxin 1
- DNA-directed RNA polymerase subunit omega
Sequence:
MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (A0A8I6AIB0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MALVTLQRSPTPSAASSSASNSELEAGSDEDRKLNLSLSESFFMVKGAALFLQQGNSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESVWTDRVRYMVVVYTSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKEFKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYQFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAFNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQPADDTIAEPSEFLPETLDGALDTQLPCLEDATHPGLPRSLPSGGPSLPCCFRRLSDPLLLPHRDGAGGLVHLEDLERDALLEDEAQPVEVRKLVPSSQEGDRLCEKDVKRKLEFGSPKARSGSLPQVEELEKDGSPRPGRWRRASTQLERGLLDQENLNNNNSKRSCPDDFERDAVFGILSKVKPPYTSCADCMYPAAGAPEAFMERHEDPSSSAICTQPTFLPHVTSSPMAHTSNRSRAPERPTSGPANTSPFLLPAGSRKPDVSGSGAGVAPEPPASLPEPSRETSKALQKSLLSKNSHCDKNAANTEAAAKEELSTKKDPKPSKDLRLLFSQEGEKPTANSYLMQHQESIIQLQKAGLVRKHTKELERLKSLPSDSPSTCRDSAASRLEASIPEEGQEPAHPALDSQAGTEEKPVGGASQKSPPPTLLLRLDHTSKDFSKDFLKSACYTPTPSSISSNLTRSSSSDSIHSVRGKPGLVKQRAQEIETRLRLAGLTVSSPLKRSHSLAKLGSLNFSTEDLSSEADTSTIADSQDAKCTLSSFLPEPQAAPRNPSATSKPSGKSAPENLKIPVRVNKS
Protein: Protein lgg-2 (Q23536)
Organism: Caenorhabditis elegans
Function: Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to components of an atg-5-lgg-3-atg-16 complex to regulate autophagosome formation and cargo sequestration. Required for the degradation of specific sqst-1-containing aggregates during embryogenesis and the early stages of larval development. Involved in allophagy, which is an autophagic process in which paternal mitochondria and organelles are degraded during fertilization, and moreover is required for the degradation of lgg-1-positive allophagic autophagosomes in embryos. Involved in xenophagy, the autophagy-mediated degradation of pathogens and pathogen products, such as toxins. Also plays a role in membrane-pore repair. Through HOPS complex subunit vps-39, tethers lysosomes with autophagosomes to form autolysosomes. Plays a role in the distribution and clearance of germ cell specific P-granules from somatic cells to ensure exclusive localization of the P-granules in germ cells. Essential for dauer development and life-span extension.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:20523114, ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:37395461}. Cytoplasm {ECO:0000269|PubMed:24374177}. Cell membrane {ECO:0000305|PubMed:26687600}; Lipid-anchor {ECO:0000305|PubMed:26687600}. Note=In embryos, diffuse cytoplasmic localization with some areas displaying a more punctate distribution (PubMed:24374177). Specifically, upon fertilization localizes to autophagosomes around the male pronucleus. During the first embryonic divisions and after the 25-cell stage, localizes to a small population of autophagosomes and to another small population of autophagosomes containing both lgg-1 and lgg-2. Localization to autophagosomes is dependent on atg-7. {ECO:0000269|PubMed:24374177}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme ATG7
- Cysteine protease atg-4.1
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy-related protein 18
- FUN14 domain-containing protein fndc-1
- Serine/threonine-protein kinase unc-51
- Cysteine protease atg-4.2
- Ubiquitin-like protein atg-12
- Autophagy-related protein 5
- MRG domain-containing protein
Sequence:
MSGNRGGSYISGIVPSFKERRPFHERQKDVEEIRSQQPNKVPVIIERFDGERSLPLMDRCKFLVPEHITVAELMSIVRRRLQLHPQQAFFLLVNERSMVSNSMSMSNLYSQERDPDGFVYMVYTSQPAFG
Protein: PP2A regulatory subunit TAP46 (NbTAP46) (D2K8N5)
Organism: Nicotiana benthamiana
Function: Involved in the regulation of the TOR signaling pathway. Seems to act as a regulator of PP2A catalytic activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21216945}. Nucleus {ECO:0000269|PubMed:21216945}.
Interaction partners:
Sequence:
MGELSMQEMPLPALFEQGSKIHASAESSVDQDTVRKGCEILRQCEEMIGKLGLFSVNETKEDISTANLKYILVPYYLAELTEKVADNDRIKVLKASQAKLKEFISFCETMELVPEEEIETSTQGGANSSVDRRAKKIARFKRQRAAESKLLEIKERKERRGRSTKAAALSSPVETEEDDVLDDDGEEEREAWLTTISLGLCKAFDLLEMLKKEEEILSAVKEKQLQNGEKEFSQAILDERTKKVETWHRDAAARAHYTKPAAPITCATFAQDVIEGRAKVSQAHEHKHQPLIFGPASLVGRNPTTEREKIAAQVFQPHYRLPTMSIEEAGLTEMNMMNEWQERNVKLMEEANSSWYKDAPKSRPGEDDEEDDDDAAQDKARAWDDWKDDNPRGAGNKKLTPCG
Protein: Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase) (QPRTase) (Q15274)
Organism: Homo sapiens (Human)
Function: Involved in the catabolism of quinolinic acid (QA).
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinate phosphoribosyltransferase
- Nicotinamide riboside kinase 1
- Nicotinamide riboside kinase 2
- Glutamine-dependent NAD
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- NAD-capped RNA hydrolase NUDT12
- Cytosolic purine 5'-nucleotidase
Sequence:
MDAEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKSPGVLAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLFAKEVAPVPKIH
Protein: Bowman-Birk type proteinase inhibitor B6 (HOSPI-B6) (C0HLT2)
Organism: Hyacinthus orientalis (Common hyacinth)
Function: Serine protease inhibitor. Inhibits trypsin (Ki = 30 nM) and weakly inhibits chymotrypsin (Ki = 550 nM). Does not inhibit bacterial subtilisin.
Interaction partners:
Sequence:
GRRPCCNECGICDRSLDPMCICEDLVPQCHEGCQACEKVDTGTPMYQCRSFEYYHCGPICY
Protein: Opsin-5 (G-protein coupled receptor 136) (G-protein coupled receptor PGR12) (Neuropsin) (Q6VZZ7)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor which selectively activates G(i) type G proteins via ultraviolet A (UVA) light-mediated activation in the retina. Preferentially binds the chromophore 11-cis retinal and is a bistable protein that displays emission peaks at 380 nm (UVA light) and 470 nm (blue light). Required for the light-response in the inner plexiform layer, and contributes to the regulation of the light-response in the nerve fiber layer, via phosphorylated DAT/SLC6A3 dopamine uptake. Involved in local corneal and retinal circadian rhythm photoentrainment via modulation of the UVA light-induced phase-shift of the retina clock. Acts as a circadian photoreceptor in the outer ear and vibrissal pads, via modulation of circadian clock-gene expression in response to violet light during the light-to-dark transition phase and night phase of the circadian cycle. Required in the retina to negatively regulate hyaloid vessel regression during postnatal development via light-dependent OPN5-SLC32A1-DRD2-VEGFR2 signaling. Involved in the light-dependent regulation of retina and vitreous compartment dopamine levels.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MALNHTALPQDERLPHYLRDEDPFASKLSWEADLVAGFYLTIIGILSTFGNGYVLYMSSRRKKKLRPAEIMTINLAVCDLGISVVGKPFTIISCFCHRWVFGWFGCRWYGWAGFFFGCGSLITMTAVSLDRYLKICYLSYGVWLKRKHAYICLAVIWAYASFWTTMPLVGLGDYAPEPFGTSCTLDWWLAQASGGGQVFILSILFFCLLLPTAVIVFSYAKIIAKVKSSSKEVAHFDSRIHSSHVLEVKLTKVAMLICAGFLIAWIPYAVVSVWSAFGRPDSIPIQLSVVPTLLAKSAAMYNPIIYQVIDYRFACCQAGGLRGTKKKSLEDFRLHTVTAVRKSSAVLEIHPESSSRFTSAHVMDGESHSNDGDCGKK
Protein: Protein kinase shaggy (EC 2.7.11.1) (Protein zeste-white 3) (P18431)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for several developmental events such as syncytial blastoderm formation and embryonic segmentation. Is involved in transcriptional regulation. Required for arm phosphorylation. Wg signaling operates by inactivating the sgg repression of en autoactivation. Negatively controls the neuromuscular junction (NMJ) growth in presynaptic motoneurons. Plays a role in the regulation of microtubule dynamics and actin cytoskeleton during embryogenesis. Required for phosphorylation of sra in activated eggs. Essential for completion of meiosis, possibly by triggering calcineurin activation via sra phosphorylation. Phosphorylates microtubule-associated protein futsch in axons.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cell cortex. Synapse. Cell projection, axon. Note=In syncytial embryos, detected at the centrosomes throughout the cell cycle, and in the mitotic spindle and pseudocleavage furrows invaginating from the cell cortex during mitosis. Concentrated at the growing end of membranes during the cellularization process. After cellularization, localized to the centrosomes during mitosis and to the nucleus at the end of telophase. Enriched in the presynaptic side of the neuromuscular junction, with some signal detected also in axonal branches.
Interaction partners:
- Axin
- Armadillo segment polarity protein
- Adenomatous polyposis coli 2
- Protein timeless
- Segment polarity protein dishevelled
- Supernumerary limbs, isoform B
- Protein wingless
- Transcriptional activator cubitus interruptus
- Casein kinase I isoform alpha
- cAMP-dependent protein kinase catalytic subunit 1
Sequence:
MSGRPRTSSFAEGNKQSPSLVLGGVKTCSRDGSKITTVVATPGQGTDRVQEVSYTDTKVIGNGSFGVVFQAKLCDTGELVAIKKVLQDRRFKNRELQIMRKLEHCNIVKLLYFFYSSGEKRDEVFLNLVLEYIPETVYKVARQYAKTKQTIPINFIRLYMYQLFRSLAYIHSLGICHRDIKPQNLLLDPETAVLKLCDFGSAKQLLHGEPNVSYICSRYYRAPELIFGAINYTTKIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEVIKVLGTPTREQIREMNPNYTEFKFPQIKSHPWQKVFRIRTPTEAINLVSLLLEYTPSARITPLKACAHPFFDELRMEGNHTLPNGRDMPPLFNFTEHELSIQPSLVPQLLPKHLQNASGPGGNRPSAGGAASIAASGSTSVSSTGSGASVEGSAQPQSQGTAAAAGSGSGGATAGTGGASAGGPGSGNNSSSGGASGAPSAVAAGGANAAVAGGAGGGGGAGAATAAATATGAIGATNAGGANVTDS
Protein: Pyruvate ferredoxin/flavodoxin oxidoreductase family protein (Q725S7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain protein
- Pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit, putative
- Iron-sulfur cluster-binding protein
- Pyruvate ferredoxin oxidoreductase, beta subunit, putative
- Pyruvate:ferredoxin oxidoreductase
- Pyruvate ferredoxin oxidoreductase, beta subunit
- Pyruvate ferredoxin oxidoreductase, alpha subunit, putative
- Pyruvate ferredoxin oxidoreductase, alpha subunit
- Succinate--CoA ligase subunit alpha
- Pyruvate ferredoxin oxidoreductase, iron-sulfur binding subunit, putative
Sequence:
MAIYQDVIMAGFGGQGVMLIGNLLAYAGMHAGLNVTYIPVYGPEMRGGTANCTVVVSDEDIGSPIIQRPKSLIIMNQPSLDKFEARLEDGGVQVLNTSLVDASKAEARVRTVCVPANEIADGIGNTKMANMVALGAYVQATGIVPLEAVKESLKSVISAHYSHLIPKNADALQAGFDHAAKG
Protein: p44-55 outer membrane protein, silent (Q2GLF3)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
METGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDNLAAALAKTSGKDIVQFANAVKISSPTIDGKVCSGKHAALQAGQGTTYHEKPHQTDNNTAQCSGLGSGSAGADQKFLSKFVSAVGLSENKNWPTGQAGKSSSGPVVGAPNSNANAMARDLVDLNRDEKTIVAGLLAKTIEGGEVVEIRSVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITNHSHL
Protein: E3 ubiquitin-protein ligase UBR1 (EC 2.3.2.27) (N-recognin-1) (Ubiquitin-protein ligase E3-alpha-1) (Ubiquitin-protein ligase E3-alpha-I) (O70481)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IWV7}.
Interaction partners:
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 A
- Ubiquitin-conjugating enzyme E2 B
- Arginyl-tRNA--protein transferase 1
- E3 ubiquitin-protein ligase UBR4
- E3 ubiquitin-protein ligase UBR5
- E3 ubiquitin-protein ligase listerin
- Protein N-terminal glutamine amidohydrolase
- Putative E3 ubiquitin-protein ligase UBR7
- E3 ubiquitin-protein ligase AMFR
Sequence:
MADEEMDGAERMDVSPEPPLAPQRPASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSILTPLEWYLFGEDPDICLEKLKHSGAFQLCGKVFKSGETTYSCRDCAIDPTCVLCMDCFQSSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVDHEPGRAGTTKESLHCPLNEEVIAQARRIFPSVIKYIVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGVYATCQEAKEDIKSHSENVSQHPLHVEVLHSVVMAHQKFALRLGSWMNKIMSYSSDFRQIFCQACLVEEPGSENPCLISRLMLWDAKLYKGARKILHELIFSSFFMEMEYKKLFAMEFVKYYKQLQKEYISDDHERSISITALSVQMLTVPTLARHLIEEQNVISVITETLLEVLPEYLDRNNKFNFQGYSQDKLGRVYAVICDLKYILISKPVIWTERLRAQFLEGFRSFLKILTCMQGMEEIRRQVGQHIEVDPDWEAAIAIQMQLKNILLMFQEWCACDEDLLLVAYKECHKAVMRCSTNFMSSTKTVVQLCGHSLETKSYKVSEDLVSIHLPLSRTLAGLHVRLSRLGAISRLHEFVPFDGFQVEVLVEYPLRCLVLVAQVVAEMWRRNGLSLISQVFYYQDVKCREEMYDKDIIMLQIGASIMDPNKFLLLVLQRYELTDAFNKTISTKDQDLIKQYNTLIEEMLQVLIYIVGERYVPGVGNVTREEVIMREITHLLCIEPMPHSAIARNLPENENNETGLENVINKVATFKKPGVSGHGVYELKDESLKDFNMYFYHYSKTQHSKAEHMQKKRRKQENKDEALPPPPPPEFCPAFSKVVNLLSCDVMMYILRTIFERAVDMESNLWTEGMLQMAFHILALGLLEEKQQLQKAPEEEVAFDFYHKASRLGSSAMNAQNIQMLLEKLKGIPQLESQKDMITWILQMFDTVKRLREKSCLVVATTSGLECVKSEEITHDKEKAERKRKAEAARLHRQKIMAQMSALQKNFIETHKLMYDNTSEVTGKEDSIMEEESTSAVSEASRIALGPKRGPAVTEKEVLTCILCQEEQEVKLENNAMVLSACVQKSTALTQHRGKPVDHLGETLDPLFMDPDLAHGTYTGSCGHVMHAVCWQKYFEAVQLSSQQRIHVDLFDLESGEYLCPLCKSLCNTVIPIIPLQPQKINSENAEALAQLLTLARWIQTVLARISGYNIKHAKGEAPAVPVLFNQGMGDSTFEFHSILSFGVQSSVKYSNSIKEMVILFATTIYRIGLKVPPDELDPRVPMMTWSTCAFTIQAIENLLGDEGKPLFGALQNRQHNGLKALMQFAVAQRTTCPQVLIHKHLARLLSVILPNLQSENTPGLLSVDLFHVLVGAVLAFPSLYWDDTVDLQPSPLSSSYNHLYLFHLITMAHMLQILLTTDTDLSSGPPLAEGEEDSEEARCASAFFVEVSQHTDGLAGCGAPGWYLWLSLRNGITPYLRCAALLFHYLLGVAPPEELFANSAEGEFSALCSYLSLPTNLFLLFQEYWDTIRPLLQRWCGDPALLKSLKQKSAVVRYPRKRNSLIELPEDYSCLLNQASHFRCPRSADDERKHPVLCLFCGAILCSQNICCQEIVNGEEVGACVFHALHCGAGVCIFLKIRECRVVLVEGKARGCAYPAPYLDEYGETDPGLKRGNPLHLSRERYRKLHLVWQQHCIIEEIARSQETNQMLFGFNWQLL
Protein: ATP-sensitive inward rectifier potassium channel 15 (Inward rectifier K(+) channel Kir1.3) (Inward rectifier K(+) channel Kir4.2) (Potassium channel, inwardly rectifying subfamily J member 15) (Q99712)
Organism: Homo sapiens (Human)
Function: 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.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q91ZF1}.
Interaction partners:
- Inward rectifier potassium channel 16
- Inward rectifier potassium channel 2
Sequence:
MDAIHIGMSSTPLVKHTAGAGLKANRPRVMSKSGHSNVRIDKVDGIYLLYLQDLWTTVIDMKWRYKLTLFAATFVMTWFLFGVIYYAIAFIHGDLEPGEPISNHTPCIMKVDSLTGAFLFSLESQTTIGYGVRSITEECPHAIFLLVAQLVITTLIEIFITGTFLAKIARPKKRAETIKFSHCAVITKQNGKLCLVIQVANMRKSLLIQCQLSGKLLQTHVTKEGERILLNQATVKFHVDSSSESPFLILPMTFYHVLDETSPLRDLTPQNLKEKEFELVVLLNATVESTSAVCQSRTSYIPEEIYWGFEFVPVVSLSKNGKYVADFSQFEQIRKSPDCTFYCADSEKQQLEEKYRQEDQRERELRTLLLQQSNV
Protein: Proline--tRNA ligase, cytoplasmic (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) (Q9M1R2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- ATP binding / aminoacyl-tRNA ligase/ nucleotide binding protein
- Arginine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, chloroplastic/mitochondrial
- Lysine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MADPSEQKEKVVKEKKEKVKKEKVVKEKVAKASSSGQKKKDVKKETGLGLSVKKDENFGEWYSEVCKQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGFAPEVAWVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKAEADEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNTGRGVQGATSHCLGQNFAKMFEINFENEKAETEMVWQNSWAYSTRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANTQGIYDACTATASALCEAGIRAEEDLRDNYSPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELLEKIQQNMYEVAKQKREACVQEVKTWDEFIKALNEKKLILAPWCDEEEVERDVKARTKGETGAAKTLCSPFDQPELPEGTLCFASGKPAKKWTYWGRSY
Protein: Rho-related protein rac1C (P34146)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Overexpression promotes the formation of filopodia and membrane ruffles.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Protein BRICK1
- Cofilin-1A
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSIISPSSYENVSGKWGPEVFHHAPNVPIILVGTKMDMREDKETQDRLKEKKLYPVSYEQGLLKMKEINAFKYLECSALTQKGLKTVFDEAIRSVINPPVKKSKSKSGCNIL
Protein: Uncharacterized protein (Q383P3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MATTGYTLTERVEGIAFGKSALPAPPPPEKFLDIFSTLEDQFRDTCKGVGFLFGADSVTSNSNSVLVSNGWPPYARIASSFAAAAAHSELGKVLRWFAKAVVGLFVNGVKSGVGFPQQWDEYVRQQADLMEYRFELQGFGVLFTYILCQLAAVESAVSEGGVSGEYSPSEGAIVADVHLPDLGAAACYPETKQSGKLRPADGCKEAACASRVNQLVPRKRDKLTTAVGNASGPLSPLQPPARHSSATVSRTLERKTAMPPAVVSLGDGNVNGSLILGPSKSLLSPARGHMGIDPLYPQQLRQRSRPRSDTPPGCVPQPKQGGPTPVSRSVPRLSYSALQVRSCSPRDDVGDSGLYVGAPPPTSNDVSGLDDPSSHVFRRRREANKLLGDGDCGEQNGIRFSIGKASRVPPTTSLSPIEVQERMRASDLAKQYGVKSITNYAERDVENFKEQMKALRKLWEE