wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar transporter chaperone complex subunit 4 (Polyphosphate kinase) (SPX-dependent polyphosphate polymerase VTC subunit 4) (Vacuolar membrane polyphosphate polymerase catalytic subunit) (PolyP polymerase) (EC 2.7.4.1) (Q382V9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Component of a polyphosphate synthase complex that utilizes ATP to synthesize and translocate polyphosphate to acidocalcisomes in epimastigotes, insect-stages of Trypanosoma brucei. Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion (By similarity). Essential for infection and parasite survival in the mammalian host.
Subcellular location: Acidocalcisome membrane {ECO:0000269|PubMed:24114837, ECO:0000269|PubMed:24386955}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to acidocalcisomes of procyclic (PCF) and bloodstream (BSF) forms of T.brucei. {ECO:0000269|PubMed:24114837}.
Interaction partners:
- GP-PDE domain-containing protein
Sequence:
MPFSKAWRSAVYPDFREQGAYINYKATKDTLHRMKEDIANPATPDELYNSLLMQKATVYKWCENKVKELQMMAEALMKASDYLSEEETPTNMSMVFSMVGSSEAKYLPPSDARRVADAITYELLRFVECRNLNTDTIEHIIARMYRYAVLGPTGDRWKNINKEYDYHALSIDEIFFMLSKVYEHVNEVESMRRDGRSSIPCGTVGSQVFDRRSVKYWVHMQDLPFVIARIIPHLPLSTFQDTYAMSKERGVPFTLGSPISSVYYDNDKFLLYHRRLERLDGATLIRMRWYGRPLDSDWNKLESKDSVFMEIKVHHEAWSGERSNKRRFALKEKDVDAYIRGDLSLKPALEKLRSKNASEAEQEKFMSLATEILTKIHAYDLKPVLRTQCQRAAFQCGLDQSIRISIDTDLRVVAEDFGLSHHWRYNGADAPLSHFPYAVVEVKLQCAENERIAPWIEELMNCRYMESVPKFSKYAHGIATLYGHTPFIKMVPYWMPQLDIDIRASTKPEYNQWDPTIGIASGCWERTTDRVIFGTGHAQTQTVGASEARFLPRTDCLRTYQRVLKAIKRGAHMNSVAPTMSPTDRPPSDEKKLTEQQELAPVVQYDTDRRHKAYTAFHLYPYCEDGVESLCFTSTGGKHVAAEVFSGLIPWQTGKRIRVPQKYDPKTLLTSERFMVKWAEQATRVGVVGLAVIRFGNSMSLPNDMVAVHSFWRANFHIVLGSLMVVVAECVLVYAYVTFKSRSRRVYARRKIRYDDRRGPVALTFVILAVILITVMMHVMVRYGPMLTGSDTF
Protein: Histone-lysine N-methyltransferase CLF (OsCLF) (EC 2.1.1.356) (Protein SET DOMAIN GROUP 711) (SET family protein 24) (OsSET24) (Q5VN06)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development (Probable). Involved in the regulation of flowering. Represses flowering under long day (LD) conditions. Regulates the trimethylation on histone H3 'Lys-27' (H3K27me3) of the flowering regulators MADS14, MADS15, RFT1, EHD1, HD3A and LF.
Interaction partners:
- Polycomb group protein FIE1
- Polycomb group protein EMF2B
- Polycomb group protein FIE1
- Probable lysine-specific demethylase SE14
- Polycomb group protein EMF2A
- Histone-binding protein MSI1
- Calmodulin-lysine N-methyltransferase
- Lysine-specific demethylase JMJ703
- Lysine-specific demethylase JMJ706
- Histone-lysine N-methyltransferase EZ1
Sequence:
MAGDSRNEPMFCEEGSSESGYVLCVIDSLKKKITSDRFVYIQKRVEENSIKLSPITLHSHNLSKNRQTSTSNSTDLVSNLLTKRKEDALCAVNSRESSPDESEGANCQDECSSTVIVGGNLSARNSVRPIRLPEVATLPPYTTWIFLDRNQRMQEDQSVLGRRRIYYDTNCGEALICSDSEDEAVEDEEEKKEFKDSEDCIIRMTIQECGMSDAVLETLARDIERAPDDIKARYEILQGEKPEGSSKKVSELNVKMEDVYGDKDLDAALDSFDNLFCRRCLVFDCKLHGCSQDLVFPTEKQAPLCSSDEGTPCGIHCYKLVSKPDAIMEIDSHLLVDVEEPTSDNLKDQIGSNKKKLGSSGQKTKSQQSESSSTARVSSESSESEVQLLSNKSPQHSPGLSKNKLGAKGGIKKSTNRRIAERILMSVKKGQQEMSPDSNSIVNGCHWPRDMKLRSDTRSGIKDSVVSSQCNSPSTRSFRKKGTLQMENNSSFVDAQSDSMEDTNNEHSATDGCDSSRKEECVDESICRQEAHGRSWKVIEQGLLLKGLEIFGKNSCLIARNLLGGMKTCTDVFQYMNYIENSSASGALSGVDSLVKGYMKGNELRTRSRFVRRRGRVRRLKYTWKTAGYHFIRKRITERKDQPCRQYTPCGCQSACGKQCPCLTNGTCCEKYCGCPKMCKNRFRGCHCAKSQCRSRQCPCFAADRECDPDVCRNCWVGCGDGTLGVPNQRGDNYECRNMKLLLKQQQRVLLGRSDVSGWGAFLKNSVGKHEYLGEYTGELISHKEADKRGKIYDRENSSFLFNLNNEYVLDAYRMGDKLKFANHSPDPNCYAKVIMVAGDHRVGIFAKERISAGEELFYDYRYEPDRAPAWARKPEGPGAKDDAQPSTGRAKKLAH
Protein: Uncharacterized protein KIAA0408 (Q6ZU52)
Organism: Homo sapiens (Human)
Interaction partners:
- ABI gene family member 3
- Microtubule cross-linking factor 3
Sequence:
MDLHKQWENTETNWHKEKMELLDQFDNERKEWESQWKIMQKKIEELCREVKLWRKININESAKIIDLYHEKTIPEKVIESSPNYPDLGQSEFIRTNHKDGLRKENKREQSLVSGGNQMCKEQKATKKSKVGFLDPLATDNQKECEAWPDLRTSEEDSKSCSGALSTALEELAKVSEELCSFQEEIRKRSNHRRMKSDSFLQEMPNVTNIPHGDPMINNDQCILPISLEKEKQKNRKNLSCTNVLQSNSTKKCGIDTIDLKRNETPPVPPPRSTSRNFPSSDSEQAYERWKERLDHNSWVPHEGRSKRNYNPHFPLRQQEMSMLYPNEGKTSKDGIIFSSLVPEVKIDSKPPSNEDVGLSMWSCDIGIGAKRSPSTSWFQKTCSTPSNPKYEMVIPDHPAKSHPDLHVSNDCSSSVAESSSPLRNFSCGFERTTRNEKLAAKTDEFNRTVFRTDRNCQAIQQNHSCSKSSEDLKPCDTSSTHTGSISQSNDVSGIWKTNAHMPVPMENVPDNPTKKSTTGLVRQMQGHLSPRSYRNMLHEHDWRPSNLSGRPRSADPRSNYGVVEKLLKTYETATESALQNSKCFQDNWTKCNSDVSGGATLSQHLEMLQMEQQFQQKTAVWGGQEVKQGIDPKKITEESMSVNASHGKGFSRPARPANRRLPSRWASRSPSAPPALRRTTHNYTISLRSEALMV
Protein: MMS19 nucleotide excision repair protein (Q581B2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367072}.
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1 homolog
- MIP18 family-like domain-containing protein
- MIP18 family-like domain-containing protein
- DNA 5'-3' helicase
Sequence:
MSVEEVDTLLQGVVTCGTNADEVALEKLREIPLLQLSRMMGKYLTGEEHVVNAVRVLGLATVNRRDRTIEEVDVMLRFFSRKLSSMQTIAVAVESTALLVRELSSEGPCTSDVFNVLHTEFLQSFSLQALPTNVRSWGYDVLRFTVTKETATWFTTPFLQVVLKSMDEENEPELLMRALELHHIIASYAREDAMQPLLEEYFDSISSYFPVVFSQPPGCKVSKEDLRRVLSACMTHPLYLNICVPFLLSRMASPSSVVKQESTNALLNIFSLDSSHTTESLCPHVVSVTNHIRNEVVRAVSLGSGECEPYVKDCVHVLKFISKRAQDVSLSIVRSWLEPMTSGALASLRSGPAVCSAYATMFYHLVSSSTCCGAATVQCFLLQLLSNTREDSFEVDDAVLIISAILSGIFDAGNGGECGKRPPPQRDVKEGLETVSEKLFQLVEKLTLSLQKADASSVHVRCELLASLVTLAAWLPHWMPDDTVLLIYKRLIALCLCGDEEVGNRVVKHISRIGSVEGNLLNVALLDMPADINPTAAGILTLYKGLLGSQASLSLAATKSLLECPEGLFGFTLTERDVFSLCRSSLSAHADYSTEDIRCLLLLTKKRNSVASFDYLCDLLLLLPIAFVPSVLQEVGGEQWGVLTASLVSCFDMDVLGVSDHIEHWMCEVLDAVRSTPTDVLTMQSVSSLCARVPGVAGRFLEAAKRLNPTTQLAARAAVARGLLACGVAEGGIIELIIEEITNSLRSGYVQDCYVDILTGVFVFCYQGCRKTTTLILPLVHAATRGSKPVSLELLRVVAKLLQDVSPTCGLEWGDIVEFSRRVSKPLNEEFVNELVELLDLALSQMDPKNVLVEALLGTDDLLPLVLSGVRSPLLKVRCTSLRLLSEAALFVMQFSSENGDSGNSYMSSALQVRDEVLHVSQVALSDHKRMVRRSAAQCRHQWYKLK
Protein: Protein NRT1/ PTR FAMILY 8.5 (AtNPF8.5) (Peptide transporter PTR6) (Q93Z20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Secretory carrier-associated membrane protein 5
Sequence:
MVNSNEEDERRILDVEESLLTQEEVNNHLTGLSSTAEDGSIDIYGNPPSKKKTGNWKACPFILGNECCERLAYYGIAKNLITYYTSELHESNVSAASDVMIWQGTCYITPLIGAVIADSYWGRYWTIASFSAIYFIGMALLTLSASLPVLKPAACAGVAAALCSPATTVQYAVFFTGLYLIALGTGGIKPCVSSFGADQFDDTDPRERVRKASFFNWFYFSINIGSFISSTLLVWVQENVGWGLGFLIPTVFMGVSIASFFIGTPLYRFQKPGGSPITRVCQVLVAAYRKLKLNLPEDISFLYETREKNSMIAGSRKIQHTDGYKFLDKAAVISEYESKSGAFSNPWKLCTVTQVEEVKTLIRMFPIWASGIVYSVLYSQISTLFVQQGRSMNRIIRSFEIPPASFGVFDTLIVLISIPIYDRFLVPFVRRFTGIPKGLTDLQRMGIGLFLSVLSIAAAAIVETVRLQLAQDFVAMSIFWQIPQYILMGIAEVFFFIGRVEFFYDESPDAMRSVCSALALLNTAVGSYLSSLILTLVAYFTALGGKDGWVPDDLNKGHLDYFFWLLVSLGLVNIPVYALICVKHTKKKAL
Protein: Syntaxin PEP12 (Carboxypeptidase Y-deficient protein 12) (Vacuolar protein sorting-associated protein 6) (Vacuolar protein-targeting protein 13) (P32854)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in the sorting and targeting of vacuolar proteases.
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Synaptobrevin homolog 2
- Synaptobrevin homolog YKT6
- Vacuolar v-SNARE NYV1
- t-SNARE VTI1
- Protein transport protein SEC22
- Vacuolar morphogenesis protein 7
- Golgi SNAP receptor complex member 1
- Protein transport protein SFT1
- Syntaxin-8
- Vacuolar protein sorting-associated protein 45
Sequence:
MSEDEFFGGDNEAVWNGSRFSDSPEFQTLKEEVAAELFEINGQISTLQQFTATLKSFIDRGDVSAKVVERINKRSVAKIEEIGGLIKKVNTSVKKMDAIEEASLDKTQIIAREKLVRDVSYSFQEFQGIQRQFTQVMKQVNERAKESLEASEMANDAALLDEEQRQNSSKSTRIPGSQIVIERDPINNEEFAYQQNLIEQRDQEISNIERGITELNEVFKDLGSVVQQQGVLVDNIEANIYTTSDNTQLASDELRKAMRYQKRTSRWRVYLLIVLLVMLLFIFLIMKL
Protein: Bisanhydrobacterioruberin hydratase (EC 4.2.1.161) (A0A0A1GNF2)
Organism: Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1)
Function: Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR). Catalyzes the reaction that introduces hydroxyl groups to C3'' and C3''' of bisanhydrobacterioruberin (BABR) to generate BR.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSGKDRTLAGWTLPETKTDATAQFDRFVTENRFTIAVVFPLVGAVTLLASAEGLLPDPLAFNPYFVLFGTFVMRLPLVAGIFPLVDRRAGLALVALTLYSYGIELVGVRTGWPYGEFTYGVDLGPMLLGDVPFGLPVFFFPLVLNAYLLVLLLLGNRAASTTVRLLSTLATVMLVDLVLDPGAVAIGFWIYEMPQFYGVPWQNYAGWLLSGSVAVLLFDFGFDRAGLRRRLRDCPFMLDDLVSFVLLWGGINLFYTNWVPFGLAALLGAGLLWTDRFDFDLSETRLGRAVWR
Protein: UBA domain-containing protein (Q57XK3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCASFQKCSAVSQENVIAQPYTWLLASSMLSKPISSFQFFTILVHTICFTCIRQNIIYIQRIYITCAVSIMLRRMEDCYIDYVAGLLARGNIDMNVVRTTLVSLGFDDRSIDIMLGEALNLRWTSGSSSTTLTASEPASETASRTSLEKGAVPFLCGDNAVKLSRSYPLGEVPEGTGSVDTSQQRLPVDFRDKIISLSSTGSHSCMCQEDPSSSCTTGMGYEPEVGLPPFINAEGCQQDRGNVPGERYKRHLEALEELLGVVWFPSNEVVDRCVPLRVRNELCRSRLKKLIMCGKGPDKILLPLPQYLYEAEREDWGTPQKSYDDRAVRFFRHLDTCDRHHSSIQRRRSRSPRQRRPCDGALGHCELCRTLSYRFLLSCKGEQRSRPQTTSAAAGGACHVKMRPLSVNTVGCGRINVKAVATTLPRREDRVGKALAYRAAWSRFGLWPAI
Protein: Ubiquinol oxidase 3, mitochondrial (EC 1.10.3.11) (Alternative oxidase 3) (Q8LEE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:25732537}; Multi-pass membrane protein {ECO:0000305}. Note=Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane.
Interaction partners:
- Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' gamma isoform
- External alternative NAD
- Internal alternative NAD
- External alternative NAD
- External alternative NAD
- Internal alternative NAD
- Glutathione S-transferase U3
- External alternative NAD
- NAC domain-containing protein 17
Sequence:
MSYRSIYRTLRPVLSSSVQSSGLGIGGFRGHLISHLPNVRLLSSDTSSPVSGNNQPENPIRTADGKVISTYWGIPPTKITKPDGSAWKWNCFQPWDSYKPDVSIDVTKHHKPSNFTDKFAYWTVQTLKIPVQLFFQRKHMCHAMLLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALLEEAENERMHLMTFIELSQPKWYERAIVFTVQGVFFNAYFLAYVISPKLAHRITGYLEEEAVNSYTEFLKDIDAGKFENSPAPAIAIDYWRLPKDATLRDVVYVIRADEAHHRDINHYASDIQFKGHELKEAPAPIGYH
Protein: Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1-alpha) (PPAR-gamma coactivator 1-alpha) (PPARGC-1-alpha) (Q9QYK2)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (By similarity). Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O70343}. Nucleus, PML body {ECO:0000250|UniProtKB:O70343}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-1
- Nuclear respiratory factor 1
- Forkhead box protein O1
- Peroxisome proliferator-activated receptor alpha
- Peroxisome proliferator-activated receptor gamma
- Steroid hormone receptor ERR1
- Hepatocyte nuclear factor 4-alpha
- Cyclic AMP-responsive element-binding protein 1
- Transcription factor A, mitochondrial
- Transcription factor YY2
Sequence:
MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSVLSRGHEERKTKRPSLRLFGDHDYCQSVNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSSQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPSQAVFDDKVDKTSELRDGNFSNEQFSKLPVFINSGLAMDGLFDDSEDENDKLSYPWDGTQSYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEANEHERLKRDEYRREYEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR
Protein: Lecithin retinol acyltransferase (EC 2.3.1.135) (Phosphatidylcholine--retinol O-acyltransferase) (O95237)
Organism: Homo sapiens (Human)
Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (Probable). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}.
Interaction partners:
- Retinoid isomerohydrolase
- Retinol dehydrogenase 12
- Retinol dehydrogenase 5
- Cytochrome P450 26A1
- Retinol dehydrogenase 10
- Retinol dehydrogenase 11
- Retinol dehydrogenase 8
- Retinol-binding protein 1
- Short-chain dehydrogenase/reductase 3
- All-trans-retinol 13,14-reductase
Sequence:
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
Protein: Probable manganese efflux pump MntP (P76264)
Organism: Escherichia coli (strain K12)
Function: Probably functions as a manganese efflux pump.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Transcriptional regulator MntR
- Divalent metal cation transporter MntH
- Small protein MntS
Sequence:
MNITATVLLAFGMSMDAFAASIGKGATLHKPKFSEALRTGLIFGAVETLTPLIGWGMGMLASRFVLEWNHWIAFVLLIFLGGRMIIEGFRGADDEDEEPRRRHGFWLLVTTAIATSLDAMAVGVGLAFLQVNIIATALAIGCATLIMSTLGMMVGRFIGSIIGKKAEILGGLVLIGIGVQILWTHFHG
Protein: Trihelix transcription factor GT-3b (Transcription factor GT-1-like) (Trihelix DNA-binding protein GT-3b) (O80450)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may play a role in the induction of CAM4 in response to pathogen and salt.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- Heat shock 70 kDa protein BIP3
- Mediator of RNA polymerase II transcription subunit 7a
- DNA gyrase subunit A, chloroplastic/mitochondrial
- Mediator of RNA polymerase II transcription subunit 30
- Small RNA degrading nuclease 3
- Mediator of RNA polymerase II transcription subunit 19a
- Mediator-associated protein 2
- Mediator of RNA polymerase II transcription subunit 14
- Mediator-associated protein 3
Sequence:
MDGHQHHHLHQLQYLNKHHLHTQSQTPEIASPVAVGDRFPQWSVEETKELIGIRGELDQTFMETKRNKLLWEVISNKMRDKSFPRSPEQCKCKWKNLVTRFKGCETMEAETARQQFPFYDDMQNIFTTRMQRMLWAESEGGGGGTSGAARKREYSSDEEEENVNEELVDVSNDPKILNPKKNIAKKRKGGSNSSNSNNGVREVLEEFMRHQVRMESEWREGWEAREKERAEKEEEWRRKMEELEKERLAMERMWRDREEQRRSREEMRAEKRDSLINALLAKLTRDGSL
Protein: Gdap1, isoform C (X2JAP0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSEQTKEIEALPPTLQDFKAPDLPANKPVLFFHPYNFHAQKVLMVFYEKKIDFFPYVVDLCNGEQYSNWFLNLNPKGDVPVLQDGALVIPSSTHIINYVESKFRGDRSLKPAHNSKEFDQMLIFEQAMARLPVGTLSLGSFIHDDLKLVPKAPFIGPVRQSCLKNNEKVLDLLRHSVDEQATKKAALQHKLDIQLRRHELASSREEFQKVLDAVRHFLLYVEQELTAQAPRVEWLTGDELSVADISLGLLLHRLYQLGFENQFWTFGKLPQVEAYFLRFRQRESFHRLQPSNFAILREMWTRTPGNYKLGAGAGFLVGHI
Protein: Cocaine- and amphetamine-regulated transcript protein (Q18744)
Organism: Caenorhabditis elegans
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- ShKT domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MKLLVLCILITISSSLFIEDSRINEIECSIVAILTDQIEESTACNLKHLLRNDPLFKPLIQTNVHKKRSAYEIIGVHTCEENEPCRIGRTRSCLCQEDFVCDKTPANKNVHLCTKLGYFRLFEANKK
Protein: Actin-related protein 2-A (Actin-like protein 2-A) (Q7ZTP2)
Organism: Xenopus laevis (African clawed frog)
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 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 (Probable). 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) (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17178911}. Cell projection {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
Sequence:
MDSQGKKVVVCDNGTGFVKCGYAGSNFPEHIFPALVGRPVIRSTAKVGNIEIKDLMVGDEASELRSMLEVNYPMENGIVRNWDDMKHLWDYTFGPEKLNIDTRDCKILLTEPPMNPTKNREKIVEVMFETYQFSGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFSLPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRMIKEKLCYVGYNIEQEQKLALETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGVGVAELLFNTIQAADIDTRAEFYKHIVLSGGSTMYPGLPSRLERELKQLYLERVLKGDVEKLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDNFWMTRQEYQEKGTRVLEKLGVTVR
Protein: Transcription cofactor HES-6 (Hairy and enhancer of split 6) (Q9JHE6)
Organism: Mus musculus (Mouse)
Function: Does not bind DNA itself but suppresses both HES1-mediated N box-dependent transcriptional repression and binding of HES1 to E box sequences. Also suppresses HES1-mediated inhibition of the heterodimer formed by ASCL1/MASH1 and TCF3/E47, allowing ASCL1 and TCF3 to up-regulate transcription in its presence. Promotes cell differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAPSQAPSRDRAGQEDEDRWEARGDRKARKPLVEKKRRARINESLQELRLLLAGTEVQAKLENAEVLELTVRRVQGALRGRAREREQLQAEASERFAAGYIQCMHEVHTFVSTCQAIDATVSAELLNHLLESMPLREGSSFQDLLGDSLAGLPGGSGRSSWPPGGSPESPLSSPPGPGDDLCSDLEEIPEAELNRVPAEGPDLVSTSLGSLTAARRAQSVWRPW
Protein: N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC 3.1.4.45) (Mannose 6-phosphate-uncovering enzyme) (Phosphodiester alpha-GlcNAcase) (Q9UK23)
Organism: Homo sapiens (Human)
Function: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12058031}; Single-pass type I membrane protein {ECO:0000269|PubMed:12058031}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12058031}. Note=Cis/medial Golgi.
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunit gamma
- N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Sequence:
MATSTGRWLLLRLALFGFLWEASGGLDSGASRDDDLLLPYPRARARLPRDCTRVRAGNREHESWPPPPATPGAGGLAVRTFVSHFRDRAVAGHLTRAVEPLRTFSVLEPGGPGGCAARRRATVEETARAADCRVAQNGGFFRMNSGECLGNVVSDERRVSSSGGLQNAQFGIRRDGTLVTGYLSEEEVLDTENPFVQLLSGVVWLIRNGSIYINESQATECDETQETGSFSKFVNVISARTAIGHDRKGQLVLFHADGQTEQRGINLWEMAEFLLKQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCHGHGTCVDGHCQCTGHFWRGPGCDELDCGPSNCSQHGLCTETGCRCDAGWTGSNCSEECPLGWHGPGCQRPCKCEHHCPCDPKTGNCSVSRVKQCLQPPEATLRAGELSFFTRTAWLALTLALAFLLLISTAANLSLLLSRAERNRRLHGDYAYHPLQEMNGEPLAAEKEQPGGAHNPFKD
Protein: Proteasome subunit alpha type (C1BFT7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
Sequence:
MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSHSHAVLVALKRAQSELAAHQKKILHVDSHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVTLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCKAMSIGARSQSARTYLERHMDTFLDCELNDLVQHGLRGLRETLPAEQDLTTKNVSIGIVGKDMEFTIYDDGDVASFLEGLEERPQRRVAQPDDEVAAEKPEEPMEL
Protein: Voltage-gated purine nucleotide uniporter SLC17A9 (Solute carrier family 17 member 9) (Vesicular nucleotide transporter) (VNUT) (Q9BYT1)
Organism: Homo sapiens (Human)
Function: Involved in vesicular storage and exocytosis of ATP. May accumulate ATP and other nucleotides in secretory vesicles such as adrenal chromaffin granules and synaptic vesicles.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:Q8VCL5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:23467297}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8VCL5}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to mucin granules and vesicles. {ECO:0000269|PubMed:23467297}.
Interaction partners:
Sequence:
MQPPPDEARRDMAGDTQWSRPECQAWTGTLLLGTCLLYCARSSMPICTVSMSQDFGWNKKEAGIVLSSFFWGYCLTQVVGGHLGDRIGGEKVILLSASAWGSITAVTPLLAHLSSAHLAFMTFSRILMGLLQGVYFPALTSLLSQKVRESERAFTYSIVGAGSQFGTLLTGAVGSLLLEWYGWQSIFYFSGGLTLLWVWYVYRYLLSEKDLILALGVLAQSRPVSRHNRVPWRRLFRKPAVWAAVVSQLSAACSFFILLSWLPTFFEETFPDAKGWIFNVVPWLVAIPASLFSGFLSDHLINQGYRAITVRKLMQGMGLGLSSVFALCLGHTSSFCESVVFASASIGLQTFNHSGISVNIQDLAPSCAGFLFGVANTAGALAGVVGVCLGGYLMETTGSWTCLFNLVAIISNLGLCTFLVFGQAQRVDLSSTHEDL