wanglab/gogpt-training-data huggingface dataset:
Protein: NAC domain-containing protein 72 (ANAC072) (Protein RESPONSIVE TO DESICCATION 26) (Q93VY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factors that bind specifically to the 5'-CATGTG-3' motif and with bipartite regions with 5'-CGTr-3' and 5'-YACG-3' as cores. Involved in the regulation of metabolic reprogramming during senescence by promoting the chloroplast protein degradation and the catabolism of lysine, phytol and free fatty acids via the induction of CV, LKR/SDH and PES1 expression. Triggers also the degradation of starch and the accumulation of mono- and disaccharides during senescence by enhancing the expression of AMY1, SFP1 and SWEET15.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:16581911, ECO:0000269|PubMed:29659022}.
Interaction partners:
- Zinc-finger homeodomain protein 11
- Low-temperature-induced 65 kDa protein
- Low-temperature-induced 78 kDa protein
- Dehydration-responsive element-binding protein 2A
- Probable peroxygenase 3
- Protein BRASSINAZOLE-RESISTANT 2
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- ABSCISIC ACID-INSENSITIVE 5-like protein 7
- Transcription factor MYC2
- ABSCISIC ACID-INSENSITIVE 5-like protein 6
Sequence:
MGVREKDPLAQLSLPPGFRFYPTDEELLVQYLCRKVAGYHFSLQVIGDIDLYKFDPWDLPSKALFGEKEWYFFSPRDRKYPNGSRPNRVAGSGYWKATGTDKIITADGRRVGIKKALVFYAGKAPKGTKTNWIMHEYRLIEHSRSHGSSKLDDWVLCRIYKKTSGSQRQAVTPVQACREEHSTNGSSSSSSSQLDDVLDSFPEIKDQSFNLPRMNSLRTILNGNFDWASLAGLNPIPELAPTNGLPSYGGYDAFRAAEGEAESGHVNRQQNSSGLTQSFGYSSSGFGVSGQTFEFRQ
Protein: Methyl-CpG binding domain protein 1 (A0A8I6AS94)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEAWQDCPALGPGWKRREAFRKSGASCGRSDIYYRSPTGEKIRSKIELTRYLGPACDLTLFDFRQGILCHPVPKTHPLAVPSKKKKKTSKPAKAKKQQVGPQRSEVRKETPREGNKVAPATALLPVTASAPAPVPVPVSAPAPAPAPLCCENCGIHLSWDGIKRERRRTLCKDCRAQRIAFNREQRMFKRVGCGECTACLVKEDCGVCSICCLQLPNDVASGLFCKCEQRRCLRIVEKNRGCGVCRGCQTQEDCGHCRICLRFPRPGLKRQWRCLQRRCFWGKYDHSKRGPRVASRRHSRAPPLPPHAASQHPEPTELHISDQTPTAPAEFVYDCVEEDELQPYTNQRQNRKCGACAACLRRMDCGHCDFCCDKPKFGGSNQKRQKCRWRQCLQFAMKRLLPSIGPGSEEEARLLPHHTHQKRSASTRQLQLSSPLKAPLAVVTTPPGPVQDSGKRQAGSGFVLPQPDTDLVYLQEGTSSLMQVPGPAAASTENPAQETQGSAPGWVVALPQVKQEKADAPEEWTAVTTFLTSSTVQPGFLSKASGLDPPPVKREPPGPEEDGEENKEDDVSESAPAEEIGGIGTPVITEIFSLGGTRLRDAEAWLPRCAPYS
Protein: Cytochrome P450 monooxygenase aba1 (EC 1.-.-.-) (Abscisic acid biosynthesis cluster protein 2) (Q6H9H9)
Organism: Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Interaction partners:
Sequence:
MSNSILNLGSFACLLSLGSIVLWYTISAVLAWYPLRKIPAPSFLATFSYLWLAKTTYSGKQYWIQRDLHKKYGPLVRIGPTDIITDDPEIIKKISSARSSHRRGDWYLTGRFNPYYDNMFTMLEPGPHAKAKARTAAAYSGRDMPDLEVGVNAQLQTLIGLMRSKYASNTVKPHQPLLDLGQVSCFFTMDVITRLAFGEEFGYLKEETDQYGFLGEVRELWPRMSTSADTPWIRKFLFSPPFLKVLGPKPTDKTGFGALMAVAEHHVGKRFAPDAKKKEDMLGSFIRHGLNQQECEVEGLFMIVAGTESTASAIRSTLVHVMTCPRVYQKLKTEINLAVEEGKVSSPIKLEEAKLLPFLQAVIYEGIRMRPPLLGLFPKIVPDGGEEFHGMFIPAGTAICMNTSSLLRSTALFGDDAEVYRPERFMELEKSKRGEMERNVELAFGYGQYMCVGKTVAFMELNKSIFEILRAFDLQLLSPAKPCDVLSYGIFLESNMLVKVTESEGTEYK
Protein: Sharpin (Shank-associated RH domain-interacting protein) (Q9EQL9)
Organism: Rattus norvegicus (Rat)
Function: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11178875}. Synapse {ECO:0000269|PubMed:11178875}. Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1. {ECO:0000269|PubMed:11178875}.
Interaction partners:
- RBR-type E3 ubiquitin transferase
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor superfamily member 1A
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
- Receptor-interacting serine/threonine-protein kinase 1
- SH3 and multiple ankyrin repeat domains protein 1
- ubiquitinyl hydrolase 1
- TNF receptor-associated factor
Sequence:
MSPPAGGAAAAADPASPVVLLAVQAAVRLLGAGHEDEAQLRKLQLKADPERPGRFRLGLLGIEPGAVSLEWPLESICYTIRGPNQHELQPPPGGPGTFSVHFLNSEEAQQWAALVRDATAEGQNGNDSTAPVPTPAMCPTSPPCSSVTPTPKATQPEMDLPQGSGNLKKEELATHLAQAIAGGDEKAAAQVAAILAQHHVALNVQLLEAWFPRGPIRLQVTVEDATSVLSSSSSAHVSLQIHPHCSIAALQEQVFSEFGFPPAVQRWVIGRCLCMPERSLASYGVSQDGDPAFLYLLSAPREVSGHSPQHSKMDRKLGCLFPQSLELPHNLQASSSSLPSPPQPGWSCPSCTFINASNRPGCEMCSTQRPCAWDPLTATST
Protein: AP-4 complex subunit mu-1 (AP-4 adaptor complex mu subunit) (Adaptor-related protein complex 4 subunit mu-1) (Mu subunit of AP-4) (Mu-adaptin-related protein 2) (mu-ARP2) (Mu4-adaptin) (mu4) (Q9JKC7)
Organism: Mus musculus (Mouse)
Function: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (By similarity). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. Within AP-4, the mu-type subunit AP4M1 is directly involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos. The adaptor protein complex 4 (AP-4) may also recognize other types of sorting signal (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O00189}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00189}. Early endosome {ECO:0000250|UniProtKB:O00189}. Note=Found in soma and dendritic shafts of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}.
Interaction partners:
- AP-4 complex subunit beta-1
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit sigma-1
- AP-5 complex subunit mu-1
- AP-2 complex subunit beta
- AP-4 complex accessory subunit Tepsin
- AP-1 complex subunit sigma-1A
- AP-1 complex subunit gamma-1
- AP-2 complex subunit alpha-1
- AP-1 complex subunit gamma-like 2
Sequence:
MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGGESPVVMYHGDRHFIHIRHSGLYLVATTLENVSPFSLLELLSRLATLLGDYCGSLNEGTISRNVALVYELLDEVLDYGYVQTTSTEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQNKVAPSSAASRPVLSSRSDQSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEICIGLTEEFCVGKSELRGYGPGIRVDEVSFHSSVNLDEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFPSVQWDQGSGRLQVYLKLRCDLPPKSQALNIHLHLPLPRGVISLSQELSSPDQKAELGEGALHWDLPRVQGGSQLSGLFQMDVPGLQGLPNHGPSPLGLGPASLSFELPRHTCSGLQVRFLRLSFSACGNANPHKWVRHLSHSNAYVIRI
Protein: Ephrin type-A receptor 8 (EC 2.7.10.1) (EPH- and ELK-related kinase) (EPH-like kinase 3) (EK3) (hEK3) (Tyrosine-protein kinase receptor EEK) (P29322)
Organism: Homo sapiens (Human)
Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system also plays a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O09127}; Single-pass type I membrane protein {ECO:0000255}. Cell projection {ECO:0000250|UniProtKB:O09127}. Early endosome membrane {ECO:0000250|UniProtKB:O09127}. Note=Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes. {ECO:0000250|UniProtKB:O09127}.
Interaction partners:
- Ephrin-A5
- Ephrin-A2
- Ephrin-A1
- Ephrin-A3
- Tyrosine-protein kinase ABL1
- Ephexin-1
- Ephrin-A4
- Ras GTPase-activating protein 1
- Ephrin-B3
- Ephrin-B1
Sequence:
MAPARGRLPPALWVVTAAAAAATCVSAARGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSMPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACVACELGFYKSAPGDQLCARCPPHSHSAAPAAQACHCDLSYYRAALDPPSSACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNYSFWIEAVNGVSDLSPEPRRAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLHHPPGKLPEPQFYAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGDSGEVCYGRLRVPGQRDVPVAIKALKAGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDTFLRTHDGQFTIMQLVGMLRGVGAGMRYLSDLGYVHRDLAARNVLVDSNLVCKVSDFGLSRVLEDDPDAAYTTTGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNRDVISSVEEGYRLPAPMGCPHALHQLMLDCWHKDRAQRPRFSQIVSVLDALIRSPESLRATATVSRCPPPAFVRSCFDLRGGSGGGGGLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLTSTQGPRRHL
Protein: Immunodominant surface protein gp47 (Q2GHU2)
Organism: Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
Interaction partners:
- histidine kinase
Sequence:
MQVDVGSEPDHGYHILFKNNGHVISDFRGVQAENFVFDIKNHNLRASFLVDPMAPFTELDNSQHPHFVVNMHTANECGSDCVHHNEHDHDAHGRGAASSVAEGVGSAISQILSLSDSIVVPVLEGNASVSEGDAVVNAVSQEAPAASVSEGDAVVNAVSQETPAASVSEGDAVVNAVSQETPAASVSEGDAVVNAVSQETPAASVSEGDAVVNAVSQETPAASVSEGDAVVNAVSQETPAASVSEGDAVVNAVSQETPATQPQSRDSLLNEEDMAAQFGNRYFYF
Protein: Geranylgeranyl pyrophosphate synthase 12, chloroplastic (GGPP synthase 12) (GGPS12) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 12) (Dimethylallyltranstransferase 12) (EC 2.5.1.1) (Farnesyl diphosphate synthase 12) (Farnesyltranstransferase 12) (EC 2.5.1.29) (Geranyltranstransferase 12) (EC 2.5.1.10) (Q9LHR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Dehydrodolichyl diphosphate synthase 2
- Phytoene synthase 1, chloroplastic
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Isopentenyl phosphate kinase
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Ent-copalyl diphosphate synthase, chloroplastic
- Farnesyl pyrophosphate synthase 2
Sequence:
MANTVHLSSSSLFIQTRGRKYNSILSFNNLQKRTVLSLSCALTSQGGKDMIPPKGKSNDRNFAFDFKSYMIRKAESVSMALNVSVPPQDPLAIQEAVRYSLLAGGKRVRPLLCIAACELVGGDEATAMSAACAVEMIHTSSLIHDDLPCMDDADLRRGKPTNHKVFGEHMAVLAGDALLALAFEHMTVVSSGLVAPERMIRSVTELAKAIGTKGLVAGQVSDLCSQGLNPYDVGLERLEFIHLHKTAALLEAAAVLGAIIGGGTEEEIQKLRKYGRCIGLLFQVVDDIIDVTESTEELGKTAGKDVMARKLTYPRLIGLERSREVAEKLRREAAEQLLGFDSNKVAPLVALASYIACRHN
Protein: RabGAP/TBC domain-containing protein (Q54UM5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSYTLLPTDNSNNNNNMTVSTSTPIKSNTNNRNNSNSSNSNNSNNSNGIDTTTTTPTKKPTRDRQLFSFSELAGTNLTLLLDSEILIRIFSKLEYSDLFIVKRVCSRWKPLCEHKSLFNSLDMQSFILYCRILPMTILNNFLQTLSMDKDEIDALKMVCREMPKITITNTPNIYLDTPPPTISNQQVPLNTQYITSSSSSSSTTTVTTTINTSNSSNTATTFITNTPIGGSTTPPIKNSFVNAFTATTSSLKSFLNTSGSGIATTLNGSNGSISSPPSPNLNSNNNNNNNSQNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSQNGHLRVSSLDDTLSISSTSSNGSLSSLDSLTINNSNNSSSNNNNNNSNNNSINGNSGNTPISNRRNVFGQSLTLNEKEQKKKDKNRKERERRMEESLKIWNEDMIPNWDKRKGTKKCREMVLQGIPSLVRSKVWPLLIGNDLNITPELFSIFGARAERAKQKSEARSLGREKTVSLIHLDLPRTFPMLSIFQDEGPLHQSLANVLEAYVCYRPDVGYVQGMSYLAAVFLLILDEFNSFVCLSNFLNNPCYMTFYTMNLDQMAVYMNTMDQLMAQNLPKIQKHLKELGIQPDIFMIDWVLTVFSKALPLDVASHVWDTIFLDGEVVIFQTALGILKMYSKDLEFGDFDVCMTLLTHLPTDIDEDELFQHINSFQINQKLLNKMLNK
Protein: Tropomyosin 4 (Tropomyosin 4a isoform 2) (Q7T3F0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTGVTSLDAVKRKIQCLQQQADDAEDRALGLQRELDNERELREKAEGDVAALNRRIQLVEEELDRAQERLGTALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVAECKASDLEEELKNVTNNLKSLEAQAEKYSEKEDKYEEEIKVLSDKLKEAETRAEFAERTVAKLEKSIDDLEEKLSSAKEENLGMHQVLDQTLQELNSL
Protein: Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (Q92456)
Organism: Hypocrea jecorina (Trichoderma reesei)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTPHSIDRAARPSVWSGLALLLSTAHAIVMPDGVTGKVPSLGWNSWNAYHCDIDESKFLSAAEVIVSSGLLDAGYNYVNIDDCWSMKDGRVDGHIAVNTTRFPDGIDGLAKKVHDLGLKLGIYSTAGTATCAGYPASLGYEDVDAADFADWGVDYLKYDNCNVPSDWQDEYVACAPDAVQTGPNGTCSTALEPNLAPPGYDWSTSKSAERFNAMRNALAKQSREIVLSLCIWGVADVFSWGNETGISWRMSGDISPEWGSVTHIINMNSFKMNSVGFWGHNDADILEVGNGNLTAAETRTHFALWAAMKSPLLIGTDLAQLSQENIELLKNKHLLAFNQDSVYGQPATPYKWGVNPDWTFNYTNPAEYWAGPSSKGHLVLMMNTLDHTVRKEAKWSEIPGLSAGRYEVRDVWTDKSLGCLSSYKTAVAAHDTAVILVGKKCRNW
Protein: Probable coatomer subunit epsilon (Epsilon-coat protein) (Epsilon-COP) (O74767)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Putative coatomer subunit alpha
- Probable coatomer subunit beta'
- Coatomer subunit delta
- Probable coatomer subunit zeta
- Coatomer subunit beta
- Probable coatomer subunit gamma
- ADP-ribosylation factor 1
- Protein transport protein sec13
- Protein rer1
- ADP-ribosylation factor GTPase-activating protein glo3
Sequence:
MFSWEASLSNELYFVRQYFYSGNYTKLFEIDTTSMSEKGLELTEIYMARAKLALGESLESIQSILTQKTPGSAAILALAGEGNMELIIDQHGNSDSVVQTLGAIFQIKNGSFDDAMDLLKKSVENLEAVALQVYIHLREHKIEAAEQTLKQALDWADEEIVLQLAQSWIKIVSGGVESYNDAFYVFEELNGTDSNPMTLTGMACADICLLRPEEALSSLKTALDSQPNYEEALSNMTTAITDLGPDAPSQAKNILSSFTNSSTLKLNDHLNEKAQEFDTFSTQFLSTA
Protein: Pab1p-dependent poly(A) ribonuclease subunit, putative (Q382E0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Exonuclease domain-containing protein
- Mitochondrial DNA polymerase I protein B, putative
- RNA-binding protein, putative
- Polyadenylate-binding protein
- RNA-binding protein, putative
- Polyadenylate-binding protein
- NUDIX hydrolase, conserved
- mRNA export factor MEX67
Sequence:
MDSKGRGSKANALGCANVVGTAANAVTNNNGSNSNQHPYARRHVNNSGGAFVNAFLASPTSLYNTPQPVDPYRQALSNPFPSAPYTTVGHLFMSSAVRNARPNVSFRSRSPARNTTVVTSPKFAHYTTIYNIENEASPSSMNPKVRTQVYQTTTRMAGTSMALRRLVKMSTTAEECAAVSELFRQYRHPNLVPLTNVLVTDEFVMGSADVIMEYKFITGAKSLNEAFINEGKATEGLLWSFACQMVSLMRAFHETSTPLRGLHWTKILFVPVSSRFYFSGVGFMDVMEPKGSAHQSAALMKHDIQSLGLLLLQLSTGNSNAKPEDFTAQPAKGYSGIFWLLVKACIDGTADVVTLCRALGERMSMEVAHQEGHADRLISQCGKEAHNGRIMRLMIKLNFVLESLHDFPEHSAEANNRYALRLFSQYVFNQVDERHRTRLDWGHVFHSLNKLDCGSEELVQLIGNDESNTILVISYRDLRDTLERAFEQLQPPPNEGDVQPFTVTVGTTSATL
Protein: 17 kDa gas vesicle protein (P81002)
Organism: Dactylococcopsis salina (strain PCC 8305) (Myxobactron salinum)
Function: May confer stability to the gas vesicle membranes. Gas vesicles are small, hollow, gas filled protein structures that are found in several microbial planktonic microorganisms. They allow the positioning of the organism at the favorable depth for growth.
Subcellular location: Gas vesicle {ECO:0000269|PubMed:1527496}. Note=Binds to the external surface of the gas vesicle. {ECO:0000269|PubMed:1527496}.
Interaction partners:
Sequence:
MVSLREQWNEQARERQREISARKTETVALLQEANQERVRVAQQQKALAIELKNQLAQFHEQLETSVGNWRQETQEQLINLEETRTANAQQQREALFNFRRQLTADVWGETESDSLKVEENTPFVA
Protein: Sodium/calcium exchanger 1 (Na(+)/Ca(2+)-exchange protein 1) (Solute carrier family 8 member 1) (P70414)
Organism: Mus musculus (Mouse)
Function: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for normal embryonic heart development and the onset of heart contractions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8659820}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- Sodium/calcium exchanger 2
- cAMP-dependent protein kinase catalytic subunit alpha
- cGMP-dependent protein kinase 1
- cGMP-dependent protein kinase 2
- Sodium/calcium exchanger 3
- Ryanodine receptor 2
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Sequence:
MLRLSLPPNVSMGFRLVALVALLFSHVDHITADTEAETGGNETTECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVSSPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPASKTEIEMDGKVVNSHVDNFLDGALVLEVDERDQDDEEARREMARILKELKQKHPEKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNMEMAENDPVSKIFFEQGTYQCLENCGTVALTIMRRGGDLSTTVFVDFRTEDGTANAASDYEFTEGTVIFKPGETQKEIRVGIIDDDIFEEDENFLVHLSNVRVSSDVSEDGILESNHASSIACLGSPSTATITIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIIPYKTIEGTARGGGEDFEDTCGEPEFQNDEIVKTISVKVIDDEEYEKNKTFFIEIGEPRLVEMSEKKALLLNELGGFTLTGKEMYGQPIFRKVHARDHPIPSTVITISEEYDDKQPLTSKEEEERRIAEMGRPILGEHTKLEVIIQESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSSLFVLLWLLYIFFSSLEAYCHIKGF
Protein: DNA repair protein RadA (EC 3.6.4.-) (Branch migration protein RadA) (DNA repair protein Sms) (P9WHJ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Interaction partners:
- DNA integrity scanning protein DisA
- Regulatory protein RecX
- Protein RecA
- Thiamine-monophosphate kinase
- DNA 3'-5' helicase
- Putative bifunctional exonuclease/endonuclease protein Rv2191
- Probable ATP-dependent helicase Lhr
- Cullin, a subunit of E3 ubiquitin ligase
- DNA repair protein RecN
- TIGR04338 family metallohydrolase
Sequence:
MANARSQYRCSECRHVSAKWVGRCLECGRWGTVDEVAVLSAVGGTRRRSVAPASGAVPISAVDAHRTRPCPTGIDELDRVLGGGIVPGSVTLLAGDPGVGKSTLLLEVAHRWAQSGRRALYVSGEESAGQIRLRADRIGCGTEVEEIYLAAQSDVHTVLDQIETVQPALVIVDSVQTMSTSEADGVTGGVTQVRAVTAALTAAAKANEVALILVGHVTKDGAIAGPRSLEHLVDVVLHFEGDRNGALRMVRGVKNRFGAADEVGCFLLHDNGIDGIVDPSNLFLDQRPTPVAGTAITVTLDGKRPLVGEVQALLATPCGGSPRRAVSGIHQARAAMIAAVLEKHARLAIAVNDIYLSTVGGMRLTEPSADLAVAIALASAYANLPLPTTAVMIGEVGLAGDIRRVNGMARRLSEAARQGFTIALVPPSDDPVPPGMHALRASTIVAALQYMVDIADHRGTTLATPPSHSGTGHVPLGRGT
Protein: Metallophosphoesterase, isoform E (EC 3.1.3.-) (A0A0B4LF50)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Alpha-mannosidase 2
Sequence:
MASLRVVNRNRLVCRGFVALTLLLVFFNEFIVYYMAQSSWQPIDCKLDNCTRLLLIADPQILGNSYDRSSHSPLARYDSDRYLAKTFERALAFTQPHIIVFLGDLLDEGNIATAQEYKQYVQRFRRIYQNKNYKKFRMISAFFQRVHVPGDNDIGGENGDYISNSNQRRFENEFMSEDLFDYDNRLRFFKINRMLLDFSNPDRDNNADRLRIGVSHAPLLIGGGPLLRAIISDLDPHIIFSGHWHESRIFIYPSTKVINFYENSVRHFDLKALKEQEHSYLEIMVPTCSYRMGKSKIGLGYAVLENYNLSYTVLWQPNRFILLFTYVFWGLFVVCGFVVFKMMTRCPFRVAKRQTLYNRVSTIPQF