wanglab/gogpt-training-data huggingface dataset:
Protein: Comb gap splice variant cg14 (Q9GT73)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ENHLIMHSRFHGSLNPFVCAECGASFPRKFQLVNHGRIHGKIPHSCTVCGKEFLQKRTLVSHMRRVHTGEQAHPCVSCGEGFLTKAELHQHVRTAHNGVNPNTSSATIIANQQLQQAHHHQAGQQTHPQTITVVSNPGNSTLLTVSTTDANGVARPQFVCRECGSAFNSREALALHLRLHTGDKSLMTDLCALTAALPGHFLSTASLNPGTVVTANPNLVGQSPVPVQIISSTGQVMSQTTLVQAANSTHPQAVVTAVPTMPVHGQQQHLQHVAQQQQQQQQQQQQQQQHVVSVAPANKPKSHFCASCGKGFAAKHGLMQHNRRHPNGGCTVRTHVCECGKAFFQKNHLMLHQRQHLETKPAISQQQLVVPTTSY
Protein: Actin-related protein 3 (Actin-like protein 3) (Q4V7C7)
Organism: Rattus norvegicus (Rat)
Function: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). Plays a role in ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19343716}. Cell projection {ECO:0000250|UniProtKB:P61158}. Nucleus {ECO:0000250|UniProtKB:P61158}. Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). {ECO:0000250|UniProtKB:P61158}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 5
- Actin nucleation-promoting factor WAS
- Actin nucleation-promoting factor WASL
- Hematopoietic lineage cell-specific protein
- Actin-related protein 2/3 complex subunit 1A
Sequence:
MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDFFIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVKEFNKYDTDGSKWIKQYTGVNAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
Protein: ISG12a protein (Q3UK07)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAFSGTGTLVASIVSKMTSSAAMVKAGGAVSGTILAGSKGLILLTQSALGSATSALGALKVGTILSGFSASTLAASPIGAKAVVAVLGGAMTVAAVPPALSAVGFTASGIAASSLAAKMMSLSAIANGGGVTAGGLVAILQSAGAAGLSVPSTVIVGSAGSAVVASVMNICESFYPFLMGSEVADMATEVADMAIEVADISTEEALPNLSNTEKD
Protein: ATP-dependent zinc metalloprotease FTSH 2, chloroplastic (AtFTSH2) (EC 3.4.24.-) (Protein VARIEGATED 2) (O80860)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a complex that function as an ATP-dependent zinc metallopeptidase. Involved in the thylakoid formation and in the removal of damaged D1 in the photosystem II, preventing cell death under high-intensity light conditions, but not involved in thermotolerance.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:18431481}; Single-pass membrane protein {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:14630971}; Stromal side {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:14630971}.
Interaction partners:
- Zinc finger protein VAR3, chloroplastic
- Translation initiation factor IF-2
- ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
- Chaperone protein ClpC1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Protein THYLAKOID FORMATION 1
- Protease Do-like 8, chloroplastic
- Pentatricopeptide repeat-containing protein At4g16390, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 4, chloroplastic
- ATP-dependent zinc metalloprotease
Sequence:
MAASSACLVGNGLSVNTTTKQRLSKHFSGRQTSFSSVIRTSKVNVVKASLDGKKKQEGRRDFLKILLGNAGVGLVASGKANADEQGVSSSRMSYSRFLEYLDKDRVNKVDLYENGTIAIVEAVSPELGNRVERVRVQLPGLSQELLQKLRAKNIDFAAHNAQEDQGSVLFNLIGNLAFPALLIGGLFLLSRRSGGGMGGPGGPGNPLQFGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGAKIPKGVLLIGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTDILKVHAGNKKFDNDVSLEIIAMRTPGFSGADLANLLNEAAILAGRRARTSISSKEIDDSIDRIVAGMEGTVMTDGKSKSLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEIIFGDSEVTTGAVGDLQQITGLARQMVTTFGMSDIGPWSLMDSSAQSDVIMRMMARNSMSEKLAEDIDSAVKKLSDSAYEIALSHIKNNREAMDKLVEVLLEKETIGGDEFRAILSEFTEIPPENRVPSSTTTTPASAPTPAAV
Protein: Xanthine-guanine phosphoribosyltransferase (XGPRT) (EC 2.4.2.-) (EC 2.4.2.22) (Xanthine phosphoribosyltransferase) (P0A9M5)
Organism: Escherichia coli (strain K12)
Function: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine. Does not ribophosphorylate adenine.
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Adenine phosphoribosyltransferase
- GMP synthase
- Hypoxanthine phosphoribosyltransferase
- Guanosine-inosine kinase
- Inosine-5'-monophosphate dehydrogenase
- GMP reductase
- Guanylate kinase
- Purine nucleoside phosphorylase DeoD-type
- Purine nucleoside phosphorylase 2
- Pyrimidine 5'-nucleotidase YjjG
Sequence:
MSEKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGVVFVPPISGR
Protein: CRE-UNC-96 protein (O76566)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSETEDVNLNLDPEKPKVRSVVRSDSGLENEIPKISGTSSALIEEGLSLLNLKSSLSPNVAPVAVDLLDRTCPSPDYGLTSERLASVKTPRFKRIDFDDRLEDLNPNKPAWKSWQENIKDSYHKVKVSAEKKREDNEFMDNMMLGRARPIRGESPYRNLSLDTGFIPSVRSRSSIMGPSLSDRSRLATSSSTTNMFNAGSGPYAAPALTISQGIESRYEERANNVELMLLKNAPLPERYKSITTREFRRAPEPSAGSFSEQDDYDFSHYTTARPYYSRPNRDDPDYFDFDLQHSVDMFKRPEGRYIPRKPQEWENKLISESTGKGTAPLSGHMFTRPDTDWRNNNTSYLSAALRTPKFWEQRFENIGKHVRDSNPISLESINRNRPVTSRFTEYRDPDYDDYEDPLDD
Protein: Transcription factor BHLH062 (Basic helix-loop-helix protein 1) (OsbHLH1) (Basic helix-loop-helix protein 62) (OsbHLH062) (bHLH transcription factor bHLH062) (Q69V10)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor that plays a positive role in salt stress tolerance. Interacts with TIFY11A/JAZ9 and binds to the promoter of some potassium ion transporter genes to regulate potassium homeostasis during salt stress.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:25617318}.
Interaction partners:
- Protein TIFY 11a
- Protein TIFY 6a
- Protein NINJA homolog 1
Sequence:
MVPRDRVNAAAAGGGGEGRLVQSGIVNKKCDKKAPKRIHKSEREKLKRDKQNDLFNELGNLLEPDRQNNGKACVLGETTRILKDLLSQVESLRKENSSLKNESHYVALERNELHDDNSMLRTEILELQNELRTRMEGNPVWSHVNTRPALRVPYPTTGVFPVQHLPHLPVTTTAAFPQQLPVIIEQHYAATPRELQLFPESATSEDSEPSQEHGISDHVTRPQPRYPTPTATLPVNLFPVFPGRQDQQCSSGTSGTNEEDRIGRS
Protein: Ras-associating and dilute domain-containing protein (A7UA95)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development.
Interaction partners:
Sequence:
MFYGSSSASMSLPSKNRLKRQSRTFTQVLYRTLSYRDRRSVTDLPEQVRDDPAELSTQSSAPGVLKIFGDEISAGANYKSVLATPRSSAQELIKEALERYSLNKTSACNFVLCDVIGRFEGPDRRWRTECLRALGNNEKPLLLQDLWKPKEGFSRRFELRRRAEVEELAAKEKDTVTADINAQARKLQRNRAKGTMTLQHGSSFCRSLSETSLNLVGLPGEEPKRYYSTLPGPIRTRSARDSEIRKERDGGGVKHSLYQSPHLLLLQGYNQQDCLVYLLNREQHTVGQETASARPNICLSSPDVLPLHCRIRRAAQRRSSSDQRLLLEPVAHGNVLVNFMRIERPTPIRHGDLLSFGAHYIFLYKDPLSAKPLPAQTLTRLRTLAKLCDGESGGLPEKGDACRMCGAVLHEPAASSRRSSKAPARGSQKRKLALEFERAHEDALVNRVLTLIEPSGDDHKLTPAYLLCLCIKHSANTFPPGSFGKLLQKIAKRIQTIAWEKTKELAQKQAQHQDPASLSLLSISDLVPDLQFIFFWMSNAIEILYFIQQKSPAYMQTIELMDDKAGSKESLLSATISANEEAMTILEEVIMYTFQQCVYYITKTLYVVLPGLLDCNPFGTEPSSEQCRRAAGVCVCAVCVMPEAVRRVVSVFQTTSDLLQQYQVHSEIQSQMFAYLFFFTNVSLFNQLIDKGPARGWFQRSRVLQIQASVKILLDWAKGAGHNHLAQKFFAKFCSTVTILASPPQQLSQMSWKALCAEHPSLKPVQLHRILTQYQLMAELGPLPIWQPSSEDEAYIYRTVDLLESFENHPPIVLPSAGFKVDLESDCVEDSIYRQLLYVRHFVWGLRTKTHPSNGCTDRQDAQREPPQPHSSPHPAPSVRGEGEGEVRSSSTTLGGRGEGAGAEDRTRDKPTHGIHYRNGSGARYANQSQATDSSCILTPPNTPLYPEHTYIQSNTAHYPEHASQEHTHTHSHTKTNGCMRSTPEHKKINGFISNGIEGPLSGCGFPFPVPVSHLGPKSDDICSVFVVDLDKGPYGLGMGLIDGLHTPLNSPGIYIRTLIPDGPAAADGRLCIGDRILAVNGTSLIGADYQSAVDLIRLGGGRLRFLVAKSDLEVSEKISASSC
Protein: Acetylcholine regulator unc-18 (Uncoordinated protein 18) (P34815)
Organism: Caenorhabditis elegans
Function: May participate in the axonal transport system and influences the acetylcholine flow in motor neurons. Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8939465}. Cell membrane {ECO:0000269|PubMed:21423527}; Peripheral membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:11245684}. Note=Localization at the cell membrane is dependent on unc-64 (PubMed:21423527). Localizes to axons of cholinergic motor neurons (PubMed:11245684). {ECO:0000269|PubMed:11245684, ECO:0000269|PubMed:21423527}.
Interaction partners:
- Syntaxin-1A homolog
- Phorbol ester/diacylglycerol-binding protein unc-13
- Rab-3-interacting molecule unc-10
- Synaptotagmin-1
- Synaptobrevin-1
- Ras-related protein Rab-3
- Protein lin-10
- Synaptosomal-associated protein
- C2 domain-containing protein
- Putative complexin-1
Sequence:
MSLKQIVGHKLLNDVIRPLKKGDGRSAWNVLIVDTLAMRMLSSCCKMHNIMEEGITIVEDLNKRREPLPTLEAIYLIAPTAESIDKLIQDYCARNLYKCAHVFFTEACSDQLFSTLSKSAAARFIKTLKEINIAFTPYESQVFNLDSPDTFFLYYNAQKQGGLTSNLERIAEQIATVCATLGEYPSLRYRADFERNVELGHLVEQKLDAYKADDPSMGEGADKARSQLIIIDRGYDAITPLLHELTLQAMCYDLLGIENDVYKYETGGSDENLEKEVLLDENDDLWVEMRHKHIAVVSQEVTKNLKKFSESKGNKGTMDSKSIKDLSMLIKRMPQHKKELNKFSTHISLAEECMKQYQQGVDKLCKVEQDLSTGIDAEGERVRDAMKLMVPLLIDPAVRCEDRLRLILLYILSKNGITDENLNKLLQHANISMADKETITNAAYLGLNIVTDTGRKKTWTPTKKERPHEQVYQSSRWVPVIKDIIEDAIDERLDTKHFPFLAGRQVNQGYRAPASARYGQWHKERGQQSNYRSGPRLIIYIIGGVTFSEMRACYEVTAARKPWEVVIGSDRIITPDKFLTNLRDLNKPRDI
Protein: Carbonic anhydrase-related protein 11 (CA-RP XI) (CA-XI) (CARP XI) (Carbonic anhydrase-related protein 2) (CA-RP II) (CARP-2) (O70354)
Organism: Mus musculus (Mouse)
Function: Does not have a catalytic activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MGGAARLSAPQALVLWAALGAAAHIGPAPDPEDWWSYKENLQGNFVPGPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLRGTLYNTGRHVSFLPASRPVVNVSGGPLLYSHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLNRDTITRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPLAHRALRGNRDPRHPERRCRGPNYRLHVDGGPHGR
Protein: Formin binding protein 1 (H0Y7W6)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}.
Interaction partners:
Sequence:
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKGAKTYI
Protein: Oligouridylate-binding protein 1A (F4HV67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQNQRLIKQQQQQQQQQHQQAMIQQAMMQQHPSLYHPGVMAPPQMEPLPSGNLPPGFDPTTCRSVYAGNIHTQVTEILLQEIFASTGPIESCKLIRKDKSSYGFVHYFDRRCASMAIMTLNGRHIFGQPMKVNWAYATGQREDTSSHFNIFVGDLSPEVTDAALFDSFSAFNSCSSYYRDARVMWDQKTGRSRGFGFVSFRNQQDAQTAINEMNGKWVSSRQIRCNWATKGATFGEDKHSSDGKSVVELTNGSSEDGRELSNEDAPENNPQFTTVYVGNLSPEVTQLDLHRLFYTLGAGVIEEVRVQRDKGFGFVRYNTHDEAALAIQMGNAQPFLFSRQIRCSWGNKPTPSGTASNPLPPPAPASVPSLSAMDLLAYERQLALAKMHPQAQHSLRQAGLGVNVAGGTAAMYDGGYQNVAAAHQQLMYYQ
Protein: Tripartite motif-containing protein 14 (Q14142)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the innate immune defense against viruses and bacteria. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways. Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation. Acts as a scaffold between TBK1 and STAT3 to promote phosphorylation of STAT3 and resolve interferon-stimulated gene (ISG) expression. Inhibits the transcriptional activity of SPI1 in a dose-dependent manner (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:24379373, ECO:0000269|PubMed:28476934, ECO:0000269|PubMed:29053956}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:32404352}. Nucleus {ECO:0000269|PubMed:35145029}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 14
- T-cell receptor-associated transmembrane adapter 1
- Mitochondrial antiviral-signaling protein
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Gamma-butyrobetaine dioxygenase
Sequence:
MAGAATGSRTPGRSELVEGCGWRCPEHGDRVAELFCRRCRRCVCALCPVLGAHRGHPVGLALEAAVHVQKLSQECLKQLAIKKQQHIDNITQIEDATEKLKANAESSKTWLKGKFTELRLLLDEEEALAKKFIDKNTQLTLQVYREQADSCREQLDIMNDLSNRVWSISQEPDPVQRLQAYTATEQEMQQQMSLGELCHPVPLSFEPVKSFFKGLVEAVESTLQTPLDIRLKESINCQLSDPSSTKPGTLLKTSPSPERSLLLKYARTPTLDPDTMHARLRLSADRLTVRCGLLGSLGPVPVLRFDALWQVLARDCFATGRHYWEVDVQEAGAGWWVGAAYASLRRRGASAAARLGCNRQSWCLKRYDLEYWAFHDGQRSRLRPRDDLDRLGVFLDYEAGVLAFYDVTGGMSHLHTFRATFQEPLYPALRLWEGAISIPRLP
Protein: Cilia- and flagella-associated protein 161 (Q568D2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:F6RJC2}.
Interaction partners:
- Phosphatidylethanolamine binding protein 4.
- Cilia and flagella-associated protein 52.
- EF-hand domain-containing family member C2
- Coiled-coil domain-containing 146
- Meiosis-specific nuclear structural protein 1
- Radial spoke head 14 homolog.
- DLEC1 cilia and flagella-associated protein.
- Stabilizer of axonemal microtubules 2.
- Protein Flattop
- Leucine-rich repeat-containing 34
Sequence:
MAHVRTYNPRVRVGNWKEDVTLEEETSKEFILQKDRGELTVQKEGALKQSILKPVSLSVSQDGFLHFGDTVMLVNCGDGGHMQRSPCVLSIIADSSNVTSHSQTNTGPHLLGPLQVGGAHSMDPCVRNTFIIISVDGSSDGEVVRYDQSFALKTTGGFAGELFLASDHKSFQKCAKKSRLQELSLVEEFDFLCWWKVLYFDPQDRLENEGYPVQVNNKVLISHCKTNQCLAALSNHILWSQFGKEYELTAHTFLDSHKAEQDNNHWLFSTAHPANQSQSLLQLQQEEHKENQEDTQVKDCS
Protein: 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (3-ketosteroid-9-alpha-hydroxylase, oxygenase component) (KSH) (Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase) (EC 1.14.15.30) (Rieske-type oxygenase) (RO) (B6V6V5)
Organism: Rhodococcus rhodochrous
Function: In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione. KSH has the highest activity with 3-keto-delta4 steroid substrates.
Interaction partners:
Sequence:
MTVPQERIEIRNIDPGTNPTRFARGWHCIGLAKDFRDGKPHQVKVFGTDLVVFADTAGKLHVLDAFCRHMGGNLARGEIKGDTIACPFHDWRWNGQGRCEAVPYARRTPKLGRTKAWTTMERNGVLFVWHCPQGSEPTPELAIPEIEGYEDGQWSDWTWTTIHVEGSHCREIVDNVVDMAHFFYVHFQMPEYFKNVFDGHIAGQHMRSYGRDDIKTGVQMDLPEAQTISDAFYYGPSFMLDTIYTVSEGTTIESKLINCHYPVTNNSFVLQFGTIVKKIEGMSEEQAAEMATMFTDGLEEQFAQDIEIWKHKSRIENPLLTEEDGPVYQLRRWYNQFYVDLEDVTPDMTQRFEFEVDTSRALESWHKEVEENLAGTAE
Protein: Repressor of RNA polymerase III transcription MAF1 homolog (Q5XIH0)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the repression of RNA polymerase III-mediated transcription in response to changing nutritional, environmental and cellular stress conditions to balance the production of highly abundant tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and maintenance (By similarity). Also plays a key role in cell fate determination by promoting mesorderm induction and adipocyte differentiation (By similarity). Mechanistically, associates with the RNA polymerase III clamp and thereby impairs its recruitment to the complex made of the promoter DNA, TBP and the initiation factor TFIIIB. When nutrients are available and mTOR kinase is active, MAF1 is hyperphosphorylated and RNA polymerase III is engaged in transcription. Stress-induced MAF1 dephosphorylation results in nuclear localization, increased targeting of gene-bound RNA polymerase III and a decrease in the transcriptional readout. Additionally, may also regulate RNA polymerase I and RNA polymerase II-dependent transcription through its ability to regulate expression of the central initiation factor TBP (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H063}. Cytoplasm {ECO:0000250|UniProtKB:Q9H063}.
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase III subunit RPC3
- RNA polymerase III subunit E
- DNA-directed RNA polymerase III subunit RPC6
- RNA polymerase I and III subunit C.
- DNA-directed RNA polymerase I subunit RPA1
- RNA polymerase III subunit D
Sequence:
MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEDESPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLRWVVNAVNCSLFSAVREDFKALKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNALDLELGAEEVDEESGGGGGGGEGRAEETSTMEEDRVPVICM
Protein: 2310061I04Rik protein (Q497V8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEEHLAVMHERLRQELPTLFLRSHDYTIYSMDVEFINEILNIRTKGRTFYVMSLTLCRFLVWNYFAQFRLEILQLTRHPENWTLQARWRLIGLPIHMLFLRFYRRDKEDLYRTFDAFSTFYLNSSGLICRHHLDKLMPSHSPSTPVKKLLVGALVALGLSEPEPSLHLCSKA
Protein: Nucleoside diphosphate kinase, mitochondrial (NDK) (NDP kinase, mitochondrial) (EC 2.7.4.6) (Nucleoside diphosphate kinase D) (NDPKD) (nm23-M4) (Q9WV84)
Organism: Mus musculus (Mouse)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (By similarity).
Subcellular location: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O00746}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000250|UniProtKB:O00746}. Note=Predominantly localized in the mitochondrion intermembrane space. Colocalizes with OPA1 in mitochondria (By similarity). {ECO:0000250|UniProtKB:O00746}.
Interaction partners:
- Nucleoside diphosphate kinase A
- Thymidylate kinase
- Nucleoside diphosphate kinase 6
- GTP:AMP phosphotransferase AK3, mitochondrial
- Nucleoside diphosphate kinase B
- Nucleoside diphosphate kinase 3
- UMP-CMP kinase 2, mitochondrial
- UMP-CMP kinase
- Deoxyuridine triphosphatase.
- CTP synthase 1
Sequence:
MGSLFGRVAALRALLCGPRFQCLLVRPSSGGPPWPQERTLVAVKPDGVQRRLVGTVIQRFERRGFKLVGMKMLQAPESILAEHYRDLQRKPFYPALISYMSSGPVVAMVWEGPNVVHISRAMIGHTDSTEAAPGTIRGDFSVHISRNVIHASDSVDGAQREIELWFQSSELLNWADGGHHSSCYPA
Protein: SEC14-like protein 1 (Q92503)
Organism: Homo sapiens (Human)
Function: May play a role in innate immunity by inhibiting the antiviral RIG-I signaling pathway. In this pathway, functions as a negative regulator of RIGI, the cytoplasmic sensor of viral nucleic acids. Prevents the interaction of RIGI with MAVS/IPS1, an important step in signal propagation. May also regulate the SLC18A3 and SLC5A7 cholinergic transporters.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17092608, ECO:0000269|PubMed:23843640}. Golgi apparatus {ECO:0000269|PubMed:17092608}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 9
- Septin-9
Sequence:
MVQKYQSPVRVYKYPFELIMAAYERRFPTCPLIPMFVGSDTVNEFKSEDGAIHVIERRCKLDVDAPRLLKKIAGVDYVYFVQKNSLNSRERTLHIEAYNETFSNRVIINEHCCYTVHPENEDWTCFEQSASLDIKSFFGFESTVEKIAMKQYTSNIKKGKEIIEYYLRQLEEEGITFVPRWSPPSITTSSETSSSSSKKQAASMAVVIPEAALKEGLSGDALSSPSAPEPVVGTPDDKLDADYIKRYLGDLTPLQESCLIRLRQWLQETHKGKIPKDEHILRFLRARDFNIDKAREIMCQSLTWRKQHQVDYILETWTPPQVLQDYYAGGWHHHDKDGRPLYVLRLGQMDTKGLVRALGEEALLRYVLSINEEGLRRCEENTKVFGRPISSWTCLVDLEGLNMRHLWRPGVKALLRIIEVVEANYPETLGRLLILRAPRVFPVLWTLVSPFIDDNTRRKFLIYAGNDYQGPGGLLDYIDKEIIPDFLSGECMCEVPEGGLVPKSLYRTAEELENEDLKLWTETIYQSASVFKGAPHEILIQIVDASSVITWDFDVCKGDIVFNIYHSKRSPQPPKKDSLGAHSITSPGGNNVQLIDKVWQLGRDYSMVESPLICKEGESVQGSHVTRWPGFYILQWKFHSMPACAASSLPRVDDVLASLQVSSHKCKVMYYTEVIGSEDFRGSMTSLESSHSGFSQLSAATTSSSQSHSSSMISR
Protein: Ribonuclease H2 subunit C (RNase H2 subunit C) (Ribonuclease HI subunit C) (Q9CQ18)
Organism: Mus musculus (Mouse)
Function: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ribonuclease H2 subunit B
- Ribonuclease H2 subunit A
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- Double-stranded RNA-specific adenosine deaminase
Sequence:
MKNPEEAADGKQRIHLRPGSLRGAAPAKLHLLPCDVLVSRPAPVDRFFTPAVRHDADGLQASFRGRGLRGEEVAVPPGFAGFVMVTEEKGEGLIGKLNFSGDAEDKADEAQEPLERDFDRLIGATGSFSHFTLWGLETVPGPDAKVHRALGWPSLAAAIHAQVPED