wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-2-macroglobulin-like protein 1 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9) (A8K2U0)
Organism: Homo sapiens (Human)
Function: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.
Subcellular location: Secreted {ECO:0000269|PubMed:16298998}.
Interaction partners:
- Kallikrein-7
- Chymotrypsinogen B2
- Chymotrypsinogen B
- Kallikrein-6
- Periplakin
- Envoplakin
Sequence:
MWAQLLLGMLALSPAIAEELPNYLVTLPARLNFPSVQKVCLDLSPGYSDVKFTVTLETKDKTQKLLEYSGLKKRHLHCISFLVPPPAGGTEEVATIRVSGVGNNISFEEKKKVLIQRQGNGTFVQTDKPLYTPGQQVYFRIVTMDSNFVPVNDKYSMVELQDPNSNRIAQWLEVVPEQGIVDLSFQLAPEAMLGTYTVAVAEGKTFGTFSVEEYVLPKFKVEVVEPKELSTVQESFLVKICCRYTYGKPMLGAVQVSVCQKANTYWYREVEREQLPDKCRNLSGQTDKTGCFSAPVDMATFDLIGYAYSHQINIVATVVEEGTGVEANATQNIYISPQMGSMTFEDTSNFYHPNFPFSGKIRVRGHDDSFLKNHLVFLVIYGTNGTFNQTLVTDNNGLAPFTLETSGWNGTDVSLEGKFQMEDLVYNPEQVPRYYQNAYLHLRPFYSTTRSFLGIHRLNGPLKCGQPQEVLVDYYIDPADASPDQEISFSYYLIGKGSLVMEGQKHLNSKKKGLKASFSLSLTFTSRLAPDPSLVIYAIFPSGGVVADKIQFSVEMCFDNQVSLGFSPSQQLPGAEVELQLQAAPGSLCALRAVDESVLLLRPDRELSNRSVYGMFPFWYGHYPYQVAEYDQCPVSGPWDFPQPLIDPMPQGHSSQRSIIWRPSFSEGTDLFSFFRDVGLKILSNAKIKKPVDCSHRSPEYSTAMGAGGGHPEAFESSTPLHQAEDSQVRQYFPETWLWDLFPIGNSGKEAVHVTVPDAITEWKAMSFCTSQSRGFGLSPTVGLTAFKPFFVDLTLPYSVVRGESFRLTATIFNYLKDCIRVQTDLAKSHEYQLESWADSQTSSCLCADDAKTHHWNITAVKLGHINFTISTKILDSNEPCGGQKGFVPQKGRSDTLIKPVLVKPEGVLVEKTHSSLLCPKGKVASESVSLELPVDIVPDSTKAYVTVLGDIMGTALQNLDGLVQMPSGCGEQNMVLFAPIIYVLQYLEKAGLLTEEIRSRAVGFLEIGYQKELMYKHSNGSYSAFGERDGNGNTWLTAFVTKCFGQAQKFIFIDPKNIQDALKWMAGNQLPSGCYANVGNLLHTAMKGGVDDEVSLTAYVTAALLEMGKDVDDPMVSQGLRCLKNSATSTTNLYTQALLAYIFSLAGEMDIRNILLKQLDQQAIISGESIYWSQKPTPSSNASPWSEPAAVDVELTAYALLAQLTKPSLTQKEIAKATSIVAWLAKQHNAYGGFSSTQDTVVALQALAKYATTAYMPSEEINLVVKSTENFQRTFNIQSVNRLVFQQDTLPNVPGMYTLEASGQGCVYVQTVLRYNILPPTNMKTFSLSVEIGKARCEQPTSPRSLTLTIHTSYVGSRSSSNMAIVEVKMLSGFSPMEGTNQLLLQQPLVKKVEFGTDTLNIYLDELIKNTQTYTFTISQSVLVTNLKPATIKVYDYYLPDEQATIQYSDPCE
Protein: Arabinose operon regulatory protein (HTH-type transcriptional regulator AraC) (P0A9E0)
Organism: Escherichia coli (strain K12)
Function: Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose. Functions both as a positive and a negative regulator. In the presence of arabinose, activates the expression of the araBAD, araE, araFGH and araJ promoters. In the absence of arabinose, negatively regulates the araBAD operon. Represses its own transcription. Acts by binding directly to DNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Regulatory protein SoxS
- Multiple antibiotic resistance protein MarA
- Melibiose operon regulatory protein
- Ribulokinase
- Lactose operon repressor
- Beta-galactosidase
- DNA-binding transcriptional dual regulator CRP
- Arabinose-proton symporter
- Right origin-binding protein
- RNA polymerase sigma factor RpoD
Sequence:
MAEAQNDPLLPGYSFNAHLVAGLTPIEANGYLDFFIDRPLGMKGYILNLTIRGQGVVKNQGREFVCRPGDILLFPPGEIHHYGRHPEAREWYHQWVYFRPRAYWHEWLNWPSIFANTGFFRPDEAHQPHFSDLFGQIINAGQGEGRYSELLAINLLEQLLLRRMEAINESLHPPMDNRVREACQYISDHLADSNFDIASVAQHVCLSPSRLSHLFRQQLGISVLSWREDQRISQAKLLLSTTRMPIATVGRNVGFDDQLYFSRVFKKCTGASPSEFRAGCEEKVNDVAVKLS
Protein: Glutaryl-CoA dehydrogenase, mitochondrial (EC 1.3.8.6) (A0A8I5ZN89)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MVPAMLTGYMSLRGVSAWLLSRKLGLRFSRVPRTWSSAAAHTASRPVFDWKDPLVLEEQLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNKSYTLSGTKTWITNSPVADLFVVWARCEDNCIRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTVEK
Protein: Peroxiredoxin-6 (EC 1.11.1.27) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Glutathione-dependent peroxiredoxin) (Lysophosphatidylcholine acyltransferase 5) (LPC acyltransferase 5) (LPCAT-5) (Lyso-PC acyltransferase 5) (EC 2.3.1.23) (Non-selenium glutathione peroxidase) (NSGPx) (Q5ZJF4)
Organism: Gallus gallus (Chicken)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O35244}. Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}.
Interaction partners:
- Glutathione reductase
- Glutathione peroxidase
- Uncharacterized protein.
- Uncharacterized protein.
- Glutathione S-transferase.
- Hematopoietic prostaglandin D synthase
- glutathione transferase
- Glutathione S-transferase
- Glutathione S-transferase 2
- Glutathione S-transferase
Sequence:
MPGLLLGDEAPNFEADTTQGGIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFSKRNVKMIALSIDSVPDHLAWSKDINAYNGDQPVEKLPFPIIADKDRELAVKLGMLDPDERDKDGMPLTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTAYKKVATPVDWKCGDSVMVVPTLPDEEAKKLFPKGVFTKDLPSGKKYLRYTPQPE
Protein: Nuclear segregation protein BFR1 (Brefeldin A resistance protein 1) (P38934)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Implicated in secretion, nuclear segregation and in maintenance of cell size.
Interaction partners:
- Protein SCP160
- Haze protective factor 1
- Protein NAM8
- mRNA-binding protein PUF3
- ATP-dependent RNA helicase DHH1
- Small ribosomal subunit protein RACK1
- SWIRM domain-containing protein YOR338W
- Nuclear fusion protein BIK1
- Probable ATP-dependent RNA helicase DHR1
- Tubulin beta chain
Sequence:
MSSQQHKFKRPDVSVRDKKLDTLNVQLKKIDTEIGLIRKQIDQHQVNDTTQQERKKLQDKNKEIIKIQADLKTRRSNIHDSIKQLDAQIKRKNNQIEEKLGKKAKFSSTAEAKQRINEIEESIASGDLSLVQEKLLVKEMQSLNKLIKDLVNIEPIRKSVDADKAKINQLKEELNGLNPKDVSNQFEENQQKLNDIHSKTQGVYDKRQTLFNKRAALYKKRDELYSQIRQIRADFDNEFKSFRAKLDKERLKREEEQRLSKLLEQKDVDMGKLQEKLTHAKIPAFTYEIGAIENSLLVLDPTYVKPKKNILPDLSSNALETKPARKVVADDLVLVTPKKDDFVNVAPSKSKKYKKKNQQKNTENEQPASIFNKVDGKFTLEPTLIATLAELDVTVPINSDDVKITVEQLKKKHEELLSKQEEQTKQNIESVEKEIEKLNLDYSNKEQQVKKELEEKRLKEQEESEKDKEN
Protein: VHS domain-containing protein (Q383K2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Clathrin heavy chain
Sequence:
MVLLSVLDKAKDMASRLLPTPYLELVEEATEPCLSTPKLSAVTLLCDNANTRAESVADVVRAVRRRIANSDPTVQYLTVIVLESLVKNCNTKLHTEVAAQKGIVKELYNIATRSATSEKECLAKEAALALILNFSVWFAGHPNSRLKFLTSVAEAVRRAVGPNAFDGIQPDIDTRLSMAVGPTGQRTRPPAKQPNKSIHHPPETGLPPGAHVVDAIGIVLPTDEELGTMLDVCMTLAEYLNDIKVNEDGSVEMDDVIESILSSIRSSNKLILLILGSDLKPSNREMLVDVCNSQNNLMQRLSKRAPSQDTRQGGTTAQSTSDSLSGASVAATAKTPSASSKMTAASAAKPSAPPETPKEQPVKLLGASQTVKRPVKPTGGESAAHPQNPLDLLDDLFPAAPAQAPAAAPPAVEAVGKGAENNCEDMYSSEEVSEERNRKPVKHVYTDFEDLLARQAPK
Protein: CRIB domain-containing protein RIC6 (ROP-interactive CRIB motif-containing protein 6) (Target of ROP protein RIC6) (Q1PF35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Is involved in pollen tube growth regulation through its interaction with ARAC11/ROP1.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11752391}; Peripheral membrane protein {ECO:0000305|PubMed:11752391}.
Interaction partners:
- Transcription factor TRY
- Cytochrome c oxidase subunit 6b-1
- Lysine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MQLTMSSSKMKSLLKGLRYISQVFESEKEEEIQIGNPTDVKHVAHIGWDGPSANATAPSWMTEFNSGGGFESAEGVGEDDSSIKCMSEYGGRSRDLPNLPKSTRKAASEKGSPTKDKSSDKTKRRSSNKGTSSSSRRPKEATEEQDELSSWPSGLPEIPKKSRRKKKSTKETAVNGGSSRSTRRSDVDNMSEYMSETGSVRSMPQFDNRDDF
Protein: Glutamate receptor 1 (Glutamate receptor I) (dGLUR-I) (Kainate-selective glutamate receptor) (Q03445)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists (By similarity). Forms ligand-gated ion channels which are activated by kainate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1359540}; Multi-pass membrane protein {ECO:0000269|PubMed:1359540}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GH12419p1
- Glutamate [NMDA] receptor subunit 1
- Peripheral plasma membrane protein CASK
- NMDA receptor 2, isoform C
- Neuropilin and tolloid-like, isoform B
- Glutamate receptor IIB
- PRKCA-binding protein
- FI04462p
- Glutamate receptor IIA
- Glutamate receptor IIC
Sequence:
MHSRLKFLAYLHFICASSIFWPEFSSAQQQQQTVSLTEKIPLGAIFEQGTDDVQSAFKYAMLNHNLNVSSRRFELQAYVDVINTADAFKLSRLICNQFSRGVYSMLGAVSPDSFDTLHSYSNTFQMPFVTPWFPEKVLAPSSGLLDFAISMRPDYHQAIIDTIQYYGWQSIIYLYDSHDGLLRLQQIYQELKPGNETFRVQMVKRIANVTMAIEFLHTLEDLGRFSKKRIVLDCPAEMAKEIIVQHVRDIKLGRRTYHYLLSGLVMDNHWPSDVVEFGAINITGFRIVDSNRRAVRDFHDSRKRLEPSGQSQSQNAGGPNSLPAISAQAALMYDAVFVLVEAFNRILRKKPDQFRSNHLQRRSHGGSSSSSATGTNESSALLDCNTSKGWVTPWEQGEKISRVLRKVEIDGLSGEIRFDEDGRRINYTLHVVEMSVNSTLQQVAEWRDDAGLLPLHSHNYASSSRSASASTGDYDRNHTYIVSSLLEEPYLSLKQYTYGESLVGNDRFEGYCKDLADMLAAQLGIKYEIRLVQDGNYGAENQYAPGGWDGMVGELIRKEADIAISAMTITAERERVIDFSKPFMTLGISIMIKKPVKQTPGVFSFLNPLSQEIWISVILSYVGVSFVLYFVTRFPPYEWRIVRRPQADSTAQQPPGIIGGATLSEPQAHVPPVPPNEFTMLNSFWYSLAAFMQQGCDITPPSIAGRIAAAVWWFFTIILISSYTANLAAFLTVERMVAPIKTPEDLTMQTDVNYGTLLYGSTWEFFRRSQIGLHNKMWEYMNANQHHSVHTYDEGIRRVRQSKGKYALLVESPKNEYVNARPPCDTMKVGRNIDTKGFGVATPIGSPLRKRLNEAVLTLKENGELLRIRNKWWFDKTECNLDQETSTPNELSLSNVAGIYYILIGGLLLAVIVAIMEFFCRNKTPQLKSPGSNGSAGGVPGMLASSTYQRDSLSDAIMHSQAKLAMQASSEYDERLVGVELASNVRYQYSM
Protein: Aldo-keto reductase family 1 member A1 (EC 1.1.1.2) (EC 1.1.1.372) (EC 1.1.1.54) (3-DG-reducing enzyme) (Alcohol dehydrogenase [NADP(+)]) (Aldehyde reductase) (Glucuronate reductase) (EC 1.1.1.19) (Glucuronolactone reductase) (EC 1.1.1.20) (S-nitroso-CoA reductase) (ScorR) (EC 1.6.-.-) (P51635)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids (By similarity). Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone. Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Displays no reductase activity towards retinoids (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JII6}.
Interaction partners:
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- Lambda-crystallin homolog
- Alcohol dehydrogenase class-3
- Aldehyde dehydrogenase family 3 member B1
Sequence:
MTASSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKYALSVGYRHIDCASVYGNETEIGEALKESVGAGKAVPREELFVTSKLWNTKHHPEDVEPAVRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVKYDSTHYKETWKALEALVAKGLVKALGLSNFSSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVICIPKSITPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVPMITVDGKRVPRDAGHPLYPFNDPY
Protein: Liver carboxylesterase 1 (Acyl-coenzyme A:cholesterol acyltransferase) (ACAT) (Brain carboxylesterase hBr1) (Carboxylesterase 1) (CE-1) (hCE-1) (EC 3.1.1.1) (Cholesteryl ester hydrolase) (CEH) (EC 3.1.1.13) (Cocaine carboxylesterase) (Egasyn) (HMSE) (Methylumbelliferyl-acetate deacetylase 1) (EC 3.1.1.56) (Monocyte/macrophage serine esterase) (Retinyl ester hydrolase) (REH) (Serine esterase 1) (Triacylglycerol hydrolase) (TGH) (P23141)
Organism: Homo sapiens (Human)
Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins. Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process. First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:10562416}. Cytoplasm {ECO:0000269|PubMed:16024911}. Lipid droplet {ECO:0000269|PubMed:16024911}. Note=Moves from cytoplasm to lipid droplets upon lipid loading. Associates with lipid droplets independently of triglycerides (TG) content of the droplets and hydrolyzes cholesteryl esters more efficiently from mixed droplets. {ECO:0000269|PubMed:16024911}.
Interaction partners:
- Beta-glucuronidase
- Cytochrome P450 3A4)
- Cocaine esterase
- Myeloperoxidase
- Cytochrome P450 2E1
- Arylamine N-acetyltransferase 2
- Cytidine deaminase
- Arylamine N-acetyltransferase 1
- Neutral cholesterol ester hydrolase 1
- UDP-glucuronosyltransferase 1A6
Sequence:
MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL
Protein: Guanine nucleotide-binding protein subunit beta-5 (Gbeta5) (Transducin beta chain 5) (O14775)
Organism: Homo sapiens (Human)
Function: Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, hence involved in the termination of the signaling initiated by the G protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (Probable). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors. May play an important role in neuronal signaling, including in the parasympathetic, but not sympathetic, control of heart rate (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P62881}.
Interaction partners:
- Regulator of G-protein signaling 11
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 9-binding protein
- Regulator of G-protein signaling 6
- Regulator of G-protein signaling 7
- Regulator of G-protein signaling 9
- Guanine nucleotide-binding protein G
- Phosducin-like protein
- Guanine nucleotide-binding protein G
Sequence:
MCDQTFLVNVFGSCDKCFKQRALRPVFKKSQQLSYCSTCAEIMATEGLHENETLASLKSEAESLKGKLEEERAKLHDVELHQVAERVEALGQFVMKTRRTLKGHGNKVLCMDWCKDKRRIVSSSQDGKVIVWDSFTTNKEHAVTMPCTWVMACAYAPSGCAIACGGLDNKCSVYPLTFDKNENMAAKKKSVAMHTNYLSACSFTNSDMQILTASGDGTCALWDVESGQLLQSFHGHGADVLCLDLAPSETGNTFVSGGCDKKAMVWDMRSGQCVQAFETHESDINSVRYYPSGDAFASGSDDATCRLYDLRADREVAIYSKESIIFGASSVDFSLSGRLLFAGYNDYTINVWDVLKGSRVSILFGHENRVSTLRVSPDGTAFCSGSWDHTLRVWA
Protein: Emb|CAB85507.1 (Glutaredoxin family protein) (Q9LZC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g04440)
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
Sequence:
MGCVSSKLGKKKLIREIRVNNGGDHIVSLTSTTYGHLDLDERAETSPKSLEVTKGEVFESEIIPRRSIKRDDPEIINTWELMEDLEDSMHVSNPQKISPKSRGIFGKSWKTPVKSVVESPKRGSSKRFGGKENNSRGVSPNQILKPKNILETPKRGVMRLSFPLKSEESSVTVTQRRKSYSPMFDPDLVASYERELSQEKEQIKMVISPVVHESRKTEKTERILEKFPEKCPPGGEHSVVIYITTLRGIRKTFEDCNVVRSILDSHEVRFSERDVSMHSVFKEEIRGIMGTKHVKIPAVFVKGRMVGSVEEVMRLEEEGKLGILLEGIPAARLGGSCCRGCGGMRFMMCVVCNGSCKVREEEKKSMVKCLKCNENGLVLCPICS
Protein: Nap1l4a protein (Nucleosome assembly protein 1-like 4a) (A4QP71)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDKKNEKGEARGKGGTKPDKPEAFLQVERVPYFNLLPKNVKRRVYALKRLQLQSGNIEAKFYEEVHELERKYAGLYQPILDKRREIVTGAVEPTDEECEWHSDKEEDELADDLQKKAALEEKQADSASAVDPKGIPDFWLTIFKHVDMLGEMLQEHDEPILKHLQDVTVKFSEPGQPMSFTLEFHFEPNSYFSNTVLTKVYKMKSEPDAADPFSFEGPEIVDCEGCKIDWHKGKDVTVKIVKKKQKHKGRGTIRTVSKEIPQDSFFNFFNPVKASPDGMDEDLDFTLATDFEIGHFFRERVIPRAVLYFTGEALEDDESFEEEDLEEGEEEDLDEEGEEEEEGDFDPTA
Protein: Paired box 3b (Paired box protein Pax-3b) (F1Q9S0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MTAFPGTIPRMMRPSLSPNYPRSGFPMEVSTPMGQGRVNQLGGVFINGRPLPNHIRHKIVEMAHHGIRPCVISRQLRVSHGCVSKILCRYQETGSIRPGAIGGTKSKTTSPDVEKRVEEYKRENPGIFSWEIRDKLLKEGICDRNNVPTVSSISRIMRGRSGTRADEEEEEEDEEDIERREREENAHRGAHSIEGILADRSSPSDEGSEVESEPDLPLKRKQRRSRTTFTADQLEELERAFERTHYPDIYTREELAQRAKLTEARVQVWFSNRRARWRKQAGANQLMAFNHLIPGGFSHHAMSSLSPYQLSESPYPPAALPQDSGTVHRPQPLPHSSHQSSGGAGPEGGASYCLSSRHGYTGYSDAFGPHNTHNNNAINNGLSSQVMGLITPSGASHPTQAEFSLDSGSSVSSSCSQRMESLSSLPALSNLSNPQSYSSASFYSLEHSGHYQYSQYGQNSFHYLRPEIA
Protein: PDGF- and VEGF-receptor related, isoform N (EC 2.7.10.1) (Q7KTI7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAMLPRLILLPLLLILRISWSDAVPLQQFSPDPDDSIENCGGENGAPLMTPCKSAIILDAQTSTTLKCEDDEPMSWWTSQSQYVHVKSFDNTEDPARPFGTSLHLIEVTADYVAAYYCVKTSKFSQIAKEEQSDEAMIELVNQGYASSIYVYVNDPDTKLVDSHNVVTARQYTDVVIPCKPAMPDTEVLLETSNGEMHSSKSVGRYDPQRGFTIEIRSIVDGGDYYCRPNPPFPHNEEEMTSIEVRFIGNGHIDNGKPLPKPVIRSSVEHHVFTDTNFTLDCEQSAYVESVYGMEWFTPSRDENRIFASQSRTDPKTRNSTHQTGRSTLTVLNAQPSDTGLYKCVTTDNSNQNVQRATYRIKVLKQNESYLNVGEPSGHYNVQEYANRTIQMTANFEGFPTPSFSWFKPDGTEVRQSENNFKILSTELSTMLQVLNAQLQDSGTYVLRGSNSFGVVQREYNVSVMDAPALKMSDAYVQVGSVARLECTVRSYPPAIVTFFFRPCSLEPQWPTCSVLNQNFSFQTRPRPGKLSVERIYEVSFLPTEPGILTCIAQNIIDGKERRTLTKAHVLLGNISENMTIYGFDKDHKIAKEDNVNFTCEALAYHFDGNLKWFINGEDLKESDSVHIETSHTKYSYKSTVHITTISDRDRGTYECRAYHNDKDAVYSSREIDLYVHDPSAPQWTNGGQEGHSKIKRKLSQTLELECASTAVPVAIVRWFKDDKEVTESKLRHIIEKESKLLITHLYPGDEGVYKCVVENRLDRIERSFTVVISDLPGISMAWVWFGVILFLILIGLCVFLAVRYQKEHKRHLALKAAGLANFEEGAVGHINPDLTLDEQAELLPYNREFEFPRENLKLGKQLGAGAFGVVLKGEAKGIRREEPTTTVAVKMVKATADNEVVRALVSELKIMVHLGQHLNVVNLLGAVTKNIAKRELMVIVEYCRFGNIQNFLLRNRKCFINQINPDTDHIDPSIMTQRMSDNYELHRDTNGGGLKYANVGFPIHSYINEPHNNNTQPPTHRRNSDNDPRSGTRAGRTGSGTATYSYDRQMDTCATVMTTVPEDDQIMSNNSVQPAWRSNYKTDSTEAMTVTTVDLISWAFQVARGMDYLSSKKVLHGDLAARNILLCEDNVVKICDFGLARSMYRGDNYKKSENGKLPIKWLALESLSDHVFSTYSDVWSYGIVLWEMFSLAKVPYPGIDPNQELFNKLNDGYRMEKPKFANQELYEIMLECWRKNPESRPLFAELEKRFANMLGEDVASHYLDLNNPYMQSNIEYMKKQSTDYLALMGSPDELAPAAPRYVNGHIVPDIRIEELPDDYMEMSRDSDPDACTAIFSPTRLEGESSDFPDFSSETTFNFPGARQSPTLSNNLNSGSSKPLRKKNGMPTVDVADQAPEEIPMLHRSSTGSDGSPEQGRRFNQALKQQYVTPTPSPRHHVETKLNGEPSENYVNMKPPRKNIPGKTTTGGGGAAAGASTEAFSNPSYQPLSTVNEKEQRRY
Protein: Shugoshin 1 (Shugoshin-like 1) (Q4KLP8)
Organism: Xenopus laevis (African clawed frog)
Function: Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the stag2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by espl1/separase at anaphase. May regulate kinetochore microtubule stability in mitosis, possibly to sense tension on mitotic chromosomes.
Subcellular location: Nucleus {ECO:0000269|PubMed:15339662}. Chromosome, centromere {ECO:0000269|PubMed:15339662}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15339662}. Nucleus speckle {ECO:0000250|UniProtKB:Q5FBB7}. Note=Localizes to the centromere. At anaphase, it dissociates from centromeres when chromatids separate. Localizes to kinetochores.
Interaction partners:
Sequence:
MVKERCPKQAFQDSLEDIKERMKEKRIKKLAKVATVNKTLCTKVQILNSGSTAIKNYKANNTALALALEAEKLKTRQAQDLILGLKREHQRLIFEIFMLRRRLQSQQGRDTAESKLASLKDIIAKVTHNLLETASLLEPAHLLCSSANNNTPNPSKVEEKLSSGASAILRLPSHAPISDTLPKNVIPNRLEPEQRNFKDKVVLEANRNTAGVNRQSRGRRSHSNQPSFTSRLEECNNEDKTESGATMNKNVSLRRRASSLNICLEESLPLEDTNVNSEHTVVETERPFPTEEFSNESRTDREIDNVDNPASPLKVKCFPHANGSKMTGLASEAKQTSNKNKEEPRVGRERVKKGKAERVAVSQMKKPWENSKPRARSKSRDRSASKKSVAKEKMNSSLNSGDAFDFACEESIHVTPFRQNKQEESQNESSLEISSSEGELDDSLYKPYKDKSKNKNLKPDIAPVPLRSRSKRNTARKNSIAENELMSDVQAEANEKKITRNGLKRKSENSFTESAETYREKSFMPTCINTNNAIAENPEVKVFSDECNGGIIYTADEPSGASTPRISLSDVTNLPGNTDAKKHINLLFNEDEMKRSSTPSRKRRCKVSINYAEPKLSGKLRRGDPFTDSEFLQSPIFKNESKRNSLNRQSLSRYNEVFVGCRR