wanglab/gogpt-training-data huggingface dataset:
Protein: NACHT, LRR and PYD domains-containing protein 9A (NALP-theta) (Q66X03)
Organism: Mus musculus (Mouse)
Function: May be involved in inflammation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q66X22}.
Interaction partners:
- Baculoviral IAP repeat-containing protein 1f
- Baculoviral IAP repeat-containing protein 1b
- Pyrin
- NLR family CARD domain-containing protein 4
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 9C
- Apoptosis-associated speck-like protein containing a CARD
- Gasdermin-D
- Baculoviral IAP repeat-containing protein 1e
- NACHT, LRR and PYD domains-containing protein 6
Sequence:
MMDSSGYGLLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPGKAWDMVLSLFLQVNREDLSTMAQTERRDKQTKYKEFMKNTFQHIWTMETNTYIPDRSYHEFIEVQYRALQDIFDCESEPVTVVVSGSRGGGKTTFLRKAMLDWASRNLLQNRFQYVFHFSVFSLNNITELSLAELISSTLPESSETVDDILSDPKRILFILDGFDYLKFDLELRTNLCNDWRKKLPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQTIEIYCVSFFNTQTGVEIFKNLKSIKPLFNLCRCPHLCWMICSTIKWQYERREVASRFGRTLGLLYTIFMVSAFKSTYARNPSKQNRARIRTLCTLAVEGMWKQVYVFDSDDLRRNGISESDKKVWLRMKFLQNQGSNIVFYHSTLQWYFAVLFYFLQYKDTRHPVIGNLAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISSKEVRQEIIRYIKSLSQQECNEKLVVHPQNLFFCILDNQEERFVRQLMDRFEEMTVDISDVDDMSATPYCLHRAPKVKNLHLHIQKRVFLEIHDPEYGDLELFKLGQKCSFTTNFGDGLLFCTFLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLCEMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDPNCTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALNHKACNLEVLGLDKSLFSEESQTLLQAVEKKNKNLKVLHFPWLKEELEKRGVRLVWNSKN
Protein: Coronin (Q7SX58)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Kinesin-like protein KIF22
- Seizure-related 6 homolog
- Aspartate beta-hydroxylase domain-containing protein 2
- Double C2-like domain-containing protein alpha isoform X2
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- Protein yippee-like 3
- Serine/threonine-protein phosphatase 4 catalytic subunit A
- Proline-rich transmembrane protein 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- Lysozyme
Sequence:
MSRKVVRSSKFRHVFGQAVKADQCYDDIRISQMTWDSNFCSVNPKFVSMIVDASGGGAFIVLPLSKTGRIDMSQPTVCGHTGPVLDIEFCPHNDNIIASGSEDCSVMIWEIPEGGLVTPLRDPVVKLEGHSKRVGLVSWHPTAHNVLMSAGCDNVVILWNVARGEAVVRIDTVHTDLIYSVCWNRNGSQILTACKDKKLRVIDPRKGTVIYEKDKPHEGSRPVRAVFVSDGKILTTGFSRMSERQVALWDPNNFGEPLTLQELDTSSGVLLPFFDPDTGIVYLCGKGDSSIRYFEVTDEAPYVHYLSMYSSKESQKGMGYMPKRGLEVNKCEIARFYKLHERKCEPVVMTVPRKSDLFQEDLYPNTVGPEPSVEADDWFAGKDGEPILISLKDGFVATTKNKEFKVIKSLMSTTSSSSCNRQSDSGDVQALQNEVKKLKEMVEDLTKRVNDLESK
Protein: Cyclin dependent kinase 13 (A0A2R8YD28)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAKAAKASNTSTPTKGNTETSASASQTNHVKDVKKIKIEHAPSPSSGGTLKNDKAKTKPPLQVTKVENNLIVDKATKKAVIVGKESKSAATKEESVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKEADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHSKRRPKICGPRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIRHEENEVSDKQI
Protein: Oxidized purine nucleoside triphosphate hydrolase (EC 3.6.1.56) (2-hydroxy-dATP diphosphatase) (7,8-dihydro-8-oxoguanine triphosphatase) (8-oxo-dGTPase) (Methylated purine nucleoside triphosphate hydrolase) (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1) (P53369)
Organism: Rattus norvegicus (Rat)
Function: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP. Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP (By similarity). Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11817101}. Nucleus {ECO:0000269|PubMed:11817101}. Nucleus membrane {ECO:0000269|PubMed:11817101}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11817101}.
Interaction partners:
- N-glycosylase/DNA lyase
- ADP-sugar pyrophosphatase
- Nucleotide triphosphate diphosphatase NUDT15
- Adenine DNA glycosylase
Sequence:
MSTSRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELLEESGLRVDTLHKVGHISFEFVGSPELMDVHIFSTDHVHGTPTESEEMRPQWFQLDQIPFADMWPDDSYWFPLLLQKKKFCGHFKFHGQDTILSYSLREVDEF
Protein: Catenin delta 1 (A0A0G2JXM1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANSLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHNHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETSDDGTTRRTETTVKKVVKTMTTRTVQPVPMGPDGLPVDASAVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYGRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPPDQYYWAPLAQHERGSLASLDSLRKGMPPPPNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPILVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEALPSVANSTGPHAASCFGAKKGKDEWFSRGKKPTEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIADLLTSEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVVSILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIPMSNMGSNTKSLDNNYSTLNERGDHNRTLDRSGDLGDMEPLKGAPLMQDEGQESLEEELDVLVLDDEGNQVSYPPMQKI
Protein: COP9 signalosome complex subunit 8 (CSN complex subunit 8) (Constitutive photomorphogenesis protein 9) (Protein FUSCA 7) (P43255)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8953769}. Nucleus {ECO:0000305|PubMed:8953769}.
Interaction partners:
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5a
- COP9 signalosome complex subunit 6b
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex-related / CSN complex-like protein
Sequence:
MDLSPVKEALAAKSFDKIADICDTLMLQVASEGIEYHDDWPYAIHLLGYFYVDDCDSARFLWKRIPTAIKERKPEVVAAWGIGQKLWTHDYAGVYEAIRGYDWSQEAKDMVAAFSDLYTKRMFQLLLSAYSTITIHDLALFLGMTEDDATTYVVENGWTVDAASQMASVKKQAVKREQKVDSSKLQRLTEYVFHLEH
Protein: Translation initiation factor beta propellor-like domain-containing protein (Q57UC1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Translation initiation factor, putative
Sequence:
MESNVSDTSLVGVPLLPLILRKDNSLLLALFSEKKQELIEIESSSMTGDYRECEVCFNPARSTAFAHATATHVRYSEVVPVGKSVNDVTPSENHSWQLNLIFEVEERNTVALSFSATGAVLVTYSVMDSKRPEGNMALYNAATGQLLRRCMQARWPGMVWTQQDLYCVRPVQGCLHVLNGNLLSEDAAALSKLDLQLPQDKEIELSMCPSSMPILALFKPFHKQTQGTLFIYRLPNLGDGAMFQATFGRAESATLLWSGSGNHLAVLVKSERDASGKSYYGTVLLYLVDVGGRKIKQIKFPSGESVHDCQWSPTVDELMVVHGKMPVNKTTLYDKAGVALMTFGEAPRNVILWSPNGRFCTLGGTGNLAGDFVFFDVRPPSSGSNGRGPAETTSTVAVSTGEFNHKCSVQLWAPDSHIFLCAIIFTRLRIDNKLVFYKNNGEQLLTQKYPILYGAHWVQTQQTHLYPMRSASPRKTEAQAKPQPYRPPHASAAASALLRRPDSSTPKQAKPAGPPGATVVVQKKKRR
Protein: 5-hydroxytryptamine receptor 2A (5-HT-2) (5-HT-2A) (Serotonin receptor 2A) (P14842)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11960784, ECO:0000269|PubMed:2300586, ECO:0000269|PubMed:2854054}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:11960784}. Cytoplasmic vesicle {ECO:0000269|PubMed:11960784}. Membrane, caveola {ECO:0000269|PubMed:11960784}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35363}. Presynapse {ECO:0000269|PubMed:11960784}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 2C
- 5-hydroxytryptamine receptor 2B
- Metabotropic glutamate receptor 2
- 5-hydroxytryptamine receptor 1B
- Guanine nucleotide-binding protein subunit alpha-11
- Sodium-dependent serotonin transporter
- Voltage-dependent L-type calcium channel subunit alpha-1C
- 5-hydroxytryptamine receptor 1A
- Voltage-dependent L-type calcium channel subunit alpha-1D
Sequence:
MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV
Protein: Vomeronasal type-1 receptor (Q8R2D2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MSSLKNILYFQAGLGILANTFLLCFYTFTILGHRSKPMDPTSCQLTFAHILFLLAGGDNWLAVILESLNIENDFKCKAIFYTSRVMRGFSICITCLLSVFQAVTISPHTSLLAKFKHKLNTYIFYAVLYIWFFNFLANSHMIFYVGGFNNVSETNQMRVTQSCSLFPMNYVISGLIFTVTTFRDVFLVGVMLITSAYIVIILFRHQRHCRHLHSIRHLRVSPEKRATQTILLLVVFFVVMYWVDFIISSTSLLLWMYDPVILTVQKLVVTAYPTITPLVQISSDKRVINVLKNSQSKCQQIF
Protein: Sterol carrier protein 2 (SCP-2) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Non-specific lipid-transfer protein) (NSL-TP) (Propanoyl-CoA C-acyltransferase) (EC 2.3.1.176) (SCP-2/3-oxoacyl-CoA thiolase) (SCP-2/thiolase) (EC 2.3.1.16) (SCP-chi) (SCPX) (Sterol carrier protein X) (SCP-X) (P22307)
Organism: Homo sapiens (Human)
Function: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity).
Subcellular location: [Isoform SCP2]: Peroxisome {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000269|PubMed:10706581, ECO:0000269|PubMed:17157249}. Mitochondrion {ECO:0000269|PubMed:17157249}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P32020}. Mitochondrion {ECO:0000250|UniProtKB:P32020}.; SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome {ECO:0000250|UniProtKB:P11915}.
Interaction partners:
- Peroxisomal targeting signal 1 receptor
- Peroxisomal multifunctional enzyme type 2
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 3
- Enoyl-CoA delta isomerase 2
- Bile acid-CoA:amino acid N-acyltransferase
- Long-chain fatty acid transport protein 5
- Peroxisomal bifunctional enzyme
- Acyl-coenzyme A thioesterase 8
Sequence:
MSSSPWEPATLRRVFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYKMGFPEAASSFRTHQIEAVPTSSASDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQLQPGNAKL
Protein: Ras-related GTP-binding protein C (Rag C) (RagC) (EC 3.6.5.-) (GTPase-interacting protein 2) (TIB929) (Q99K70)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGA or RRAGB and cycles between an inactive GTP-bound and an active GDP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9HB90}. Nucleus {ECO:0000250|UniProtKB:Q9HB90}. Lysosome membrane {ECO:0000250|UniProtKB:Q9HB90}. Note=Predominantly cytoplasmic. Recruited to the lysosome surface by the Ragulator complex. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA. {ECO:0000250|UniProtKB:Q9HB90}.
Interaction partners:
- Serine/threonine-protein kinase mTOR
- Ras-related GTP-binding protein B
- Ras-related GTP-binding protein A
- Ras-related GTP-binding protein D
- Regulatory-associated protein of mTOR
- Ragulator complex protein LAMTOR2
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR5
- Ragulator complex protein LAMTOR1
- Folliculin
Sequence:
MSLQYGAEETPLAGSYGAADSFPKDFGYGVEEEEEEAAAGGGGGAGAGGGCGPGGADSSKPRILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTGALIYVIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSPVDMQSYELCCDMIDVVIDVSCIYGLKEDGSGSAYDKESMAIIKLNNTTVLYLKEVTKFLALVCILREESFERKGLIDYNFHCFRKAIHEVFEVGVTSHRSCSHQTSAPSLKALAHNGTPRNAI
Protein: ATP synthase subunit 4, mitochondrial (P05626)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit 5, mitochondrial
- ATP synthase protein 8
- ATP synthase subunit H
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit a
- ATP synthase subunit J, mitochondrial
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit 9, mitochondrial
Sequence:
MSMSMGVRGLALRSVSKTLFSQGVRCPSMVIGARYMSSTPEKQTDPKAKANSIINAIPGNNILTKTGVLGTSAAAVIYAISNELYVINDESILLLTFLGFTGLVAKYLAPAYKDFADARMKKVSDVLNASRNKHVEAVKDRIDSVSQLQNVAETTKVLFDVSKETVELESEAFELKQKVELAHEAKAVLDSWVRYEASLRQLEQRQLAKSVISRVQSELGNPKFQEKVLQQSISEIEQLLSKLK
Protein: Probable starch synthase 4, chloroplastic/amyloplastic (AtSS4) (EC 2.4.1.21) (Soluble starch synthase IV) (SSIV) (Q0WVX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the priming of starch granule formation. May play a regulatory role in the control of starch accumulation in plastids. Is necessary and sufficient to establish the correct number of starch granules observed in chloroplasts.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21645200, ECO:0000269|PubMed:29866647, ECO:0000269|PubMed:30055112}. Plastid, amyloplast {ECO:0000269|PubMed:19666739, ECO:0000269|PubMed:21645200}. Plastid, chloroplast stroma {ECO:0000269|PubMed:29866647}.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
Sequence:
MTTKLSSFCFLTHGLAGISCEREHGSSRRFFYLPSRRLVSTSCKMRQQRGFDSSKRQEVKKGSPKPILSINSGLQSNNDEESDLENGSADSVPSLKSDAEKGSSIHGSIDMNHADENLEKKDDIQTTEVTRRKSKTAKKKGESIHATIDIGHDDGKNLDNITVPEVAKALSLNKSEGEQISDGQFGELMTMIRSAEKNILRLDEARATALDDLNKILSDKEALQGEINVLEMKLSETDERIKTAAQEKAHVELLEEQLEKLRHEMISPIESDGYVLALSKELETLKLENLSLRNDIEMLKSELDSVKDTGERVVVLEKECSGLESSVKDLESKLSVSQEDVSQLSTLKIECTDLWAKVETLQLLLDRATKQAEQAVIVLQQNQDLRNKVDKIEESLKEANVYKESSEKIQQYNELMQHKVTLLEERLEKSDAEIFSYVQLYQESIKEFQETLESLKEESKKKSRDEPVDDMPWDYWSRLLLTVDGWLLEKKIASNDADLLRDMVWKKDRRIHDTYIDVKDKNERDAISAFLKLVSSPTSSGLYVVHIAAEMAPVAKVGGLGDVVAGLGKALQRKGHLVEIILPKYDCMQYDRVRDLRALDTVVESYFDGKLYKNKIWIGTVEGLPVHFIEPQHPSKFFWRGQFYGEQDDFRRFSYFSRAALELLLQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGLDSARICFTCHNFEYQGTASASELGSCGLDVNQLNRPDRMQDHSSGDRVNPVKGAIIFSNIVTTVSPTYAQEVRTAEGGKGLHSTLNFHSKKFIGILNGIDTDSWNPATDPFLKAQFNAKDLQGKEENKHALRKQLGLSSAESRRPLVGCITRLVPQKGVHLIRHAIYRTLELGGQFVLLGSSPVPHIQREFEGIEQQFKSHDHVRLLLKYDEALSHTIYAASDLFIIPSIFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDIDDDTIPTQFQNGFTFQTADEQGFNYALERAFNHYKKDEEKWMRLVEKVMSIDFSWGSSATQYEELYTRSVSRARAVPNRT
Protein: Nitrate transporter (Nitrate permease) (P22152)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Permease for nitrate uptake.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Nitrate reductase
- Nitrite reductase [NAD
- Nitrate reductase
- Nitrate/nitrite transporter
- Uncharacterized protein
- Oxidoreductase, 2-nitropropane dioxygenase family, putative
- Oxidoreductase 2-nitropropane dioxygenase family, putative
- Nitrogen assimilation transcription factor nirA
- Ammonium transporter
- Ammonium transporter
Sequence:
MDFAKLLVASPEVNPNNRKALTIPVLNPFNTYGRVFFFSWFGFMLAFLSWYAFPPLLTVTIRDDLDMSQTQIANSNIIALLATLLVRLICGPLCDRFGPRLVFIGLLLVGSIPTAMAGLVTSPQGLIALRFFIGILGGTFVPCQVWCTGFFDKSIVGTANSLAAGLGNAGGGITYFVMPAIFDSLIRDQGLPAHKAWRVAYIVPFILIVAAALGMLFTCDDTPTGKWSERHIWMKEDTQTASKGNIVDLSSGAQSSRPSGPPSIIAYAIPDVEKKGTETPLEPQSQAIGQFDAFRANAVASPSRKEAFNVIFSLATMAVAVPYACSFGSELAINSILGDYYDKNFPYMGQTQTGKWAAMFGFLNIVCRPAGGFLADFLYRKTNTPWAKKLLLSFLGVVMGAFMIAMGFSDPKSEATMFGLTAGLAFFLESCNGAIFSLVPHVHPYANGIVSGMVGGFGNLGGIIFAIIFRYSHHDYARGIWILGVISMAVFISVSWVRPVPKSQMRE
Protein: HTH-type transcriptional regulator MalT (ATP-dependent transcriptional activator MalT) (P06993)
Organism: Escherichia coli (strain K12)
Function: Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box (5'-GGA[TG]GA-3'). Displays weak ATPase activity, but this activity is not required for promoter binding.
Interaction partners:
- Diaminopropionate ammonia-lyase
- Small heat shock protein IbpB
- 3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenasepropanoate dehydrogenase)
- Recombination-promoting nuclease RpnA
- L-fucose isomerase
- Maltoporin
- Maltose/maltodextrin-binding periplasmic protein
- Probable [Fe-S]-dependent transcriptional repressor FeoC
- Maltose/maltodextrin transport system permease protein MalF
- D-tagatose-1,6-bisphosphate aldolase subunit GatY
Sequence:
MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLALITSPAGYGKTTLISQWAAGKNDIGWYSLDEGDNQQERFASYLIAAVQQATNGHCAICETMAQKRQYASLTSLFAQLFIELAEWHSPLYLVIDDYHLITNPVIHESMRFFIRHQPENLTLVVLSRNLPQLGIANLRVRDQLLEIGSQQLAFTHQEAKQFFDCRLSSPIEAAESSRICDDVSGWATALQLIALSARQNTHSAHKSARRLAGINASHLSDYLVDEVLDNVDLATRHFLLKSAILRSMNDALITRVTGEENGQMRLEEIERQGLFLQRMDDTGEWFCYHPLFGNFLRQRCQWELAAELPEIHRAAAESWMAQGFPSEAIHHALAAGDALMLRDILLNHAWSLFNHSELSLLEESLKALPWDSLLENPQLVLLQAWLMQSQHRYGEVNTLLARAEHEIKDIREDTMHAEFNALRAQVAINDGNPDEAERLAKLALEELPPGWFYSRIVATSVLGEVLHCKGELTRSLALMQQTEQMARQHDVWHYALWSLIQQSEILFAQGFLQTAWETQEKAFQLINEQHLEQLPMHEFLVRIRAQLLWAWARLDEAEASARSGIEVLSSYQPQQQLQCLAMLIQCSLARGDLDNARSQLNRLENLLGNGKYHSDWISNANKVRVIYWQMTGDKAAAANWLRHTAKPEFANNHFLQGQWRNIARAQILLGEFEPAEIVLEELNENARSLRLMSDLNRNLLLLNQLYWQAGRKSDAQRVLLDALKLANRTGFISHFVIEGEAMAQQLRQLIQLNTLPELEQHRAQRILREINQHHRHKFAHFDENFVERLLNHPEVPELIRTSPLTQREWQVLGLIYSGYSNEQIAGELEVAATTIKTHIRNLYQKLGVAHRQDAVQHAQQLLKMMGYGV
Protein: Protein Tat (Q98XH7)
Organism: Human immunodeficiency virus type 1 (HIV-1)
Subcellular location: Host nucleus, host nucleolus {ECO:0000256|ARBA:ARBA00004307, ECO:0000256|RuleBase:RU003311}.
Interaction partners:
Sequence:
MEPVDPKLEPWKHPGSQPKTACNNCYCKRCCLHCQVCFMTKGLGIYYGRKKRRQRRRASQDRQTHQDSLSEQ
Protein: Biflaviolin synthase CYP158A1 (EC 1.14.19.69) (Cytochrome P450 158A1) (CYP158A1) (Q9KZF5)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Catalyzes oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (two isomers of biflaviolin and one triflaviolin).
Interaction partners:
- Bifunctional albaflavenone monooxygenase/terpene synthase
- CDA peptide synthetase III
- Phenyloxazoline synthase MbtB
- Peptide synthase
- Peptide synthase
- Peptide synthetase
- CDA peptide synthetase I
- Polyketide synthase
- DNA polymerase I
Sequence:
MTQETTTLTGQSPPPVRDWPALDLDGPEFDPVLAELMREGPLTRVRLPHGEGWAWLATRYDDVKAITNDPRFGRAEVTQRQITRLAPHFKPRPGSLAFADQPDHNRLRRAVAGAFTVGATKRLRPRAQEILDGLVDGILAEGPPADLVERVLEPFPIAVVSEVMGVPAADRERVHSWTRQIISTSGGAEAAERAKRGLYGWITETVRARAGSEGGDVYSMLGAAVGRGEVGETEAVGLAGPLQIGGEAVTHNVGQMLYLLLTRRELMARMRERPGARGTALDELLRWISHRTSVGLARIALEDVEVHGTRIAAGEPVYVSYLAANRDPDVFPDPDRIDLDRDPNPHLAYGNGHHFCTGAVLARMQTELLVDTLLERLPGLRLAVPAEQVAWRRKTMIRGPRTLPCTW