wanglab/gogpt-training-data huggingface dataset:
Protein: HCG41426, isoform CRA_c (Transforming acidic coiled-coil containing protein 2) (Q4VXL4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPLRRPKMKKTPEKLDNTPASPPRSPAEPNDIPIAKGTYTFDIDKWDDPNFNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPLKTDTFRVKKSPKRSPLSDPPSQDPTPAATPETPPVISAVVHATDEEKLAVTNQKWTCMTVDLEADKQDYPQPSDLSTFVNETKFSSPTEELDYRNSYEIEYMEKIGSSLPQDDDAPKKQALYLMFDTSQESPVKSSPVRMSESPTPCSGSSFEETEALVNTAAKNQHPVPRGLAPNQESHLQVPEKSSQKELEAMGLGTPSEAIEIREAAHPTDVSISKTALYSRIGTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGKS
Protein: tRNA-dihydrouridine(20/20a) synthase (EC 1.3.1.-) (EC 1.3.1.91) (DusA-like U20-specific dihydrouridine synthase) (U20-specific Dus) (Q5SMC7)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.
Interaction partners:
Sequence:
MLDPRLSVAPMVDRTDRHFRFLVRQVSLGVRLYTEMTVDQAVLRGNRERLLAFRPEEHPIALQLAGSDPKSLAEAARIGEAFGYDEINLNLGCPSEKAQEGGYGACLLLDLARVREILKAMGEAVRVPVTVKMRLGLEGKETYRGLAQSVEAMAEAGVKVFVVHARSALLALSTKANREIPPLRHDWVHRLKGDFPQLTFVTNGGIRSLEEALFHLKRVDGVMLGRAVYEDPFVLEEADRRVFGLPRRPSRLEVARRMRAYLEEEVLKGTPPWAVLRHMLNLFRGRPKGRLWRRLLSEGRSLQALDRALRLMEEEVGEEGEKEKPGPRGQREAAPGPAREGV
Protein: Protein CADMIUM TOLERANCE 1 (Cd tolerant 1) (OsCDT1) (Q5VSB5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Confers resistance to heavy metal ions (e.g. cadmium (CdCl(2)) and copper (CuCl(2))) by chelating them at the plasma membrane of root cells, thus stopping their entry and reducing their accumulation. Binds to aluminium (Al).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19017626}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19017626}.
Interaction partners:
Sequence:
MYNAPMAQDMSYYEHVQRRHEEKGCLYACIFTALCCFCCYETCECCLDCLCCCCN
Protein: Bip1 protein (Q9XZU6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNTITTLRICQAVSLNPSANGPEPVLPPSSRICLMGCQDVKPNDLRRFPVHDTDRCNHWLRHFGVSYKLVDQLGGLQKLRICSRHFSQRQEMAKTRIKMTPLRKSSSSKGIVLPINTAGGSVIAGALAGGGGAGTGSGAVKSAVANSTTIELVESPNRHQAKKPNTGIMPMPQRSHSISSSASSDVLSINSDYEASLPLSALEDSQNGLNRLENGQAKKRKLYVITEKSDETKGQTLETNGQPKKRKMFVVVEQDKDVAGKKLMIMADKPQTNLTQHLEKLLPELLNRIQDKEQKQIKPAPVVTKAKPVVNNPRPHITLPPKKNPTNFAKITSTPSSVPSSIQMPLPIQNTKILKSENSELTMNSDEIETNINLSPDFRFLMKILPKLEQLPEPHKQNVKRSIQIFVEKSYSIYGNKD
Protein: Silencing boundary-establishment protein FUB1 (Function of boundary protein 1) (Proteasome inhibitor PI31-like protein FUB1) (P25659)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in the establishment of transcriptional silencing boundaries, preventing the propagation of heterochromatic silencing.
Interaction partners:
- Proteasome subunit beta type-3
- Proteasome subunit beta type-5
- Proteasome subunit beta type-2
- Proteasome subunit beta type-7
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-2
Sequence:
MIENKVELVAELVLESIGKTEVVSRHTEGTKSCQVSFRIKDSPSEKGSTSFLSELVVIQTLDDNDKYTVVIRHGTSITMACVVGYSDFKLPTELKWPLERESLPVEPDLKPIMTQLKRQTAGSADMPKFDDEYQAQARQNQGTAPLNPYPGLTVTEPSFANPAGGYADGDLYPVGTSHPDWSGGLPNPLGNPSSQGGMIFDPNRRPAPRREDMPPGWMPGSKYDEPFGPGSGGFGGSGSGGFGGSGSGFI
Protein: Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain) (Q8IX12)
Organism: Homo sapiens (Human)
Function: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation. In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12816952}.
Interaction partners:
- Pre-mRNA-processing factor 40 homolog A
- Transcription elongation regulator 1
- RNA-binding protein 5
- RNA-binding protein 25
- RNA-binding protein 39
- Serrate RNA effector molecule homolog
- ATP-dependent RNA helicase A
- Probable ATP-dependent RNA helicase DDX5
- Serine/arginine repetitive matrix protein 2
- 17S U2 SnRNP complex component HTATSF1
Sequence:
MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAAAAALQQQYSQPQQALYSVQQQLQQPQQTLLTQPAVALPTSLSLSTPQPTAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPPAVLQPIAPQTTFGVQTQPQPQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSRERERERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKNMAILDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQELRDGFQHPARLVKFLVGMKGKDEAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKEADGEQDEEEKDDGEAKEISTPTHWSKLDPKTMKVNDLRKELESRALSSKGLKSQLIARLTKQLKVEEQKEEQKELEKSEKEEDEDDDRKSEDDKEEEERKRQEEIERQRRERRYILPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKKEKDKKSKKDERKDKKEERDDETDEPKPKRRKSGDDKDKKEDRDERKKEDKRKDDSKDDDETEEDNNQDEYDPMEAEEAEDEEDDRDEEEMTKRDDKRDINRYCKERPSKDKEKEKTQMITINRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLLNKVVLRESCFYRKLTDTSKDEENHEESESLQEDMLGNRLLLPTPTVKQESKDVEENVGLIVYNGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKENGASV
Protein: Signal recognition particle 54 kDa protein (Q8ISC7)
Organism: Trypanosoma brucei
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MVLAELGQKIGAAISKMSSKSFVGEDDVKEFXNEVARALLQADVNVKTVKELQQNVRAEVAITAEAAGLNKRKMLQTAVFNGIKKMLDPGVKPFIPAKGKTSIVMFVGLQGSGKTTSCTKYAAYFQRKGLKTGLVCADTFRAGAYDQLRQNATKAKVRFYGSLTEADPVIIAKEGVLELKKEKYDLIIVDTSGRHKQESALFEEMKQVQQAVKPNDIVFVMSATDGQGIEEQARQFKEKVPIGSVIVTKLDGQAKGGGALAAVAMTKSPIVFIGTGEHFDDFELFQPESFVSRMLGMGDMRALVDSMKDANIDTDSELYKRFQDGQFTLRDMYEHLQNVLKMGSVSKIMDMIPGMSGFTGNAGDAGDVTLKTFIHMMDSMTAAELDDSRVKKTMTPTRIHRIARGSGHTILEVHNLITSYTKFEDVVKKMGKVNFKAMTQDSSTAFSGKMGQQQVLQLAKALNPTMLRQIGGLTGLQDIMKQLQSIK
Protein: Delta-aminolevulinic acid dehydratase (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) (Q58DK5)
Organism: Bos taurus (Bovine)
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10518}.
Interaction partners:
- Porphobilinogen deaminase
- Uroporphyrinogen-III synthase
- 5-aminolevulinate synthase, non-specific, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Ferrochelatase, mitochondrial
- Ornithine aminotransferase, mitochondrial
- Beta-alanine-activating enzyme
Sequence:
MHPQSVLHSGYFHPLLRNWQTAATSLSASNLIYPIFVTDVPDDKQPIASLPGVARYGVNRLEEMLKPLVEEGLRCVLIFGVPSRVPKDERGSAADSEDSPAIEAIRLLRKNFPSLLVACDVCLCPYTSHGHCGLLSENGSFQAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGFGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADLLMVKPGTPYLDIVREVKNKHPELPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEVMTAFRRAGADVIITYYTPQLLQWLKE
Protein: Tubulin-specific chaperone A (B5G0F0)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU364030}.
Interaction partners:
Sequence:
MYEKEAKQQEEKIEKMKAEACDDYGIKKQIEILQESRMMIPDCQRRLEVAHAELTQLLENEKELEEAEEYKEARSILESVKLEA
Protein: Transposase (Q5F769)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Interaction partners:
Sequence:
MKITHCKLKKEVQKEPLRSFVPEVTARSAADILGIHPDSAALFYRKIRTVANHRLALAADGVFEGPAGPGGSCFGGRRKGRRGRGAAGKAVVFGIPKRNGRAYTVAADNAEPETLPPAVKKKIMPDGIVYADSPGSRGKSDAGGFTRCRINRSEEFADRRNHINGIGNFWNQAKRALRKYNGIDRKPFPPLLRECEFRLNFGTPSRQLKILRDRCGI
Protein: L-iditol 2-dehydrogenase (A0A1D8PUB4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Xylulose kinase
- D-xylose reductase [NAD
- Adh5p
- Phosphotransferase
- Phosphotransferase
- Transketolase
- ATP-dependent 6-phosphofructokinase
- 5-aminolevulinate synthase, mitochondrial
- Trehalose 6-phosphate synthase/phosphatase complex subunit
Sequence:
MTNPSLVLNKIDDISFEDYESPEITSPRDVIVEVKKTGICGSDIHYYAHGSIGPFVLRKPMVLGHESAGVVVAVGDDVTNLKVGDKVAIEPGVPSRYSDEYKSGNYHLCPHMAFAATPPVNPDEPNPPGTLCKYYKAPADFLFKLPDHVSLELGAMVEPLTVGVHACKLANLKFGENVVVFGAGPVGLLTAAVAKTIGAKNIMVVDIFDNKLQMAKDMGAATHTFNSKTGDDLVKAFDGIEPSVVLECSGAKQCIYTGVKILKAGGRFVQVGNAGGDVNFPIADFSTRELTLYGSFRYGYGDYQTSIDILDKNYINGKENAPINFELLITHRFKFKDAIKAYDLVRGGNGAVKCLIDGPE
Protein: FACT complex subunit pob3 (Facilitates chromatin transcription complex subunit pob3) (O94529)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q04636}. Chromosome {ECO:0000250|UniProtKB:Q04636}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q04636}.
Interaction partners:
- FACT complex subunit spt16
- Uncharacterized protein C13E7.08c
- Transcription elongation factor spt5
- Tetratricopeptide repeat protein 1
- RNA polymerase-associated protein C651.09c
- Cell division control protein 73
- Transcription elongation factor spt6
- Transcription elongation factor spt4
- RNA polymerase II-associated protein 1 homolog
- Non-histone chromosomal protein 6
Sequence:
MAAKTVQYDNIYLNLSEKPGKLRIAPSGLGWKSPSLAEPFTLPISEIRRFCWSRFARGYELKIILKSKDPVSLDGFSQEDLDDLINVIKQNFDMGIEQKEFSIKGWNWGEANFLGSELVFDVNSRPAFEIPISAVTNTNLSGKNEVALEFSTTDDKQIPSAQVDELVEMRLYVPGTTAKEDAADGEEVEQNAANLFYESLKERADIGQAAGDAIVSFSEILLLTPRGRYDIDMYETCMRLRGKTYDYKVEYSSINSLFLLPKPDEQHVVFVIGLEPPLRQGQTRYPFLVTQFVRDEDMEVDLNIEETVLKEKYADKVKASYDQPAFEVVSQIFRGLTGRKVTTPAEFLSHEGHAAVKCSYKANEGQLYCLDKSFLFIPKPTLLMNTSDITRVTLSRVGMSVSAARTFDLTFTLRSGTSYQFSNINRVEQSALVAFLESKQIKIHNDLADETQQTLLTSALDDEDEEGDEEMEEALSEDEDFQAESESDVAEEYDENAESSDEEGASGAEGSE
Protein: Bifunctional autolysin (EC 3.2.1.96) (EC 3.5.1.28) (Q9AIS0)
Organism: Staphylococcus caprae
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTKKFNYKLPSMVALTLFGTAFTAHHAHAAEETQDQTKNSNVLDDQATLKQAEQAKNEVTQSAQNVSGTQTYQDPTKVQSKQDTTSNNYDASLDELNDSSSKASQQEQSNNSNQPTDSKETNTSSVNTYQDSTKDIKNNEISKDAVTSEDNETSKVDNTNKEVSETEQQESTVENVNKDENSNNNIQASSNQTNNLNDQEKQEATSNQASNNKTSQQATTDSTEKSNNKVSQTNSSGYNFDDDEDDVDTTNAQSKNTKADQPQVASLSAQNNVNTKSESNPTIKNSTNSTNTSKSATQNTKVSNTQANNTTTESNNKVSTFSSVAKPRMMYAVNKKTTSSLPKYTPQVKSSINDYIRKKNYKAPQIEENYTSYFPKYGYRNGVGRPEGIVVHDTANDNSTIDGEINYMKNNYQSAFVHAFVDGNRIVETAPTDYLSWGAGPQGNERFINVEIVHTHDYDSFARSMNNYADYAATQLQYYGLKPDSAENDGQGTVWTHYAISRYLGGTDHTDPHQYFRSHNYSYAELYDLIYEKYLIKTGQVAPWGTSSTSPSKPSKPSDSSNNNKLTVSANSGVAQIKPSNSGLYTTVYDEKGHSTDQAQKTLSVTKSATLGNNKFYLVEDYNTGKKYGWVKQGDVVYNTAKSPVKVNQTYNVKAGSTLYTVPWGTPSQVASKVSGSGNQTFKATKQQQIDKAIYLYGTVNGKSGWISKYYLTTPSSSNTKPSKPSTDNSSSNNKLTVSANSGVAQIKAKNNGVYTTVYDKKGKTTDQVQRTLSVTKSATLGNDKFYLVEDYNTGKKYGWVKQDDVVYNTAKSPVKVNQNYSIKPGVKLYTVPWGTYNQVASTVSGSGNQTFKATKQQQIDKATYLYGTVNGKSGWVSKYYLTTPTQSKVAVSKPKTSTKAVSTNSKATTADRAAITQTSAKASNTNSTQTINKIAQVKANNSGIRASVFDKKAKSGAKYGNRTYIITKQRTEGNNTYVLLQDSTRNTPLGWVNVKDVTSQNIGNQTKATGQYKVSQTNNGLYSIAWGTKNQQLLPSNTIASKTFNASKSLYVGKDLYLYGTVNNRTGWIAAKDLIQSNKDVQARPYNYTFVISNSNSYYYEDLGKNARYSLKPYYDKTFVVSKQKNINGVTWYYGKLTNGKYVWIKSTDVAKESVKYVNTGYTLAHAAEIQNDLYDTPQIQKVPGQWTNANYNEIKDAMDPNKLTKDSGARYQFLRLDQPQSLSVAALNELLKGQGVLEGQGAAFSEAAKKYGINEIYLVAHALVETGNGTSQLAKGGDIVNGKFSDKTKTKYHNVFGIGAYDSSPLIEGIKYAKNAGWDSVSKAIIGGAKFIGQSYIKAGQNTLYKMRWNPSNPGTHQYATDIHWATVNAQTIKGFYDKIGEVGKYYEIPKYK
Protein: Mixed lineage kinase domain like pseudokinase (I3L2T9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENLKHIITLGQVIHKRCEEMKYCKKQCRRLGHRVLGLIKPLEMLQDQGKRSVPSEKLTTAMNRFKAALEEANGEIEKFSNRSNICRFLTASQDKILFKDVNRKLSDVWKELSLLLQVEQRMPVSPISQGASWAQEDQQDADEDRRAFQMLRRDNEKIEASLRRLEINMKEIKETLRQYLPPKCMQEIPQEQIKEIKKEQLSGSPWILLRE
Protein: Proteasome subunit alpha 1 (20S proteasome alpha subunit 1) (Proteasome core protein PrcA 1) (Q53080)
Organism: Rhodococcus erythropolis (Arthrobacter picolinophilus)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
Sequence:
MTMPYYASAEQIMRDRSELARKGIARGRSVVVLTFRDGVLFVAENPSTALHKVSELYDRLGFAAVGKYNEFENLRRAGIVHADMRGYSYDRRDVTGRSLANAYAQTLGTIFTEQPKPYEVEICVAEVGRVGSPKAPQLYRITYDGSIVDEQHFVVMGGTTEPIATAMRESYRADLDLEAAVGIAVNALRQGGAGEGEKRNVDVASLEVAVLDQSRPRRAFRRIAGTALEQLVPAEPAAASESAPEPKPDTETKPADTQD
Protein: Chaperonin CPN60, mitochondrial (HSP60) (P29197)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- 10 kDa chaperonin 2, chloroplastic
- 10 kDa chaperonin, mitochondrial
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 10, mitochondrial
- Heat shock protein 90-5, chloroplastic
- T-complex protein 1 subunit theta
- Heat shock 70 kDa protein 9, mitochondrial
- Heat shock protein 90-1
- GrpE protein homolog
Sequence:
MYRFASNLASKARIAQNARQVSSRMSWSRNYAAKEIKFGVEARALMLKGVEDLADAVKVTMGPKGRNVVIEQSWGAPKVTKDGVTVAKSIEFKDKIKNVGASLVKQVANATNDVAGDGTTCATVLTRAIFAEGCKSVAAGMNAMDLRRGISMAVDAVVTNLKSKARMISTSEEIAQVGTISANGEREIGELIAKAMEKVGKEGVITIQDGKTLFNELEVVEGMKLDRGYTSPYFITNQKTQKCELDDPLILIHEKKISSINSIVKVLELALKRQRPLLIVSEDVESDALATLILNKLRAGIKVCAIKAPGFGENRKANLQDLAALTGGEVITDELGMNLEKVDLSMLGTCKKVTVSKDDTVILDGAGDKKGIEERCEQIRSAIELSTSDYDKEKLQERLAKLSGGVAVLKIGGASEAEVGEKKDRVTDALNATKAAVEEGILPGGGVALLYAARELEKLPTANFDQKIGVQIIQNALKTPVYTIASNAGVEGAVIVGKLLEQDNPDLGYDAAKGEYVDMVKAGIIDPLKVIRTALVDAASVSSLLTTTEAVVVDLPKDESESGAAGAGMGGMGGMDY
Protein: Complement factor H-related protein (Q61408)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGFCSMLLLSNILLTAWLSTAKGEVKSCEFPQFKYGRLYFEEILRPNFPVSIGNKYSYKCDNGFSPPSGLFWDYLRCTVQGWKPEVPCVRKCVFHYVENGEFAYWEKIYVQGQSLKVQCYNGYSLQNGQDTMTCTENGWSPPPKCIRIKTCSVSDIEIENGFFSESFRTYALNRETSYRCKQGYVTNTGETSRSITCLQNGWSPQPSCIKSCERPVFENSVTKNNSTWFKLNDKLDYECLIGHENEYKHTKGSITCTYYGWSDTPSCYEIECSVPILDRKLVVSPRKEKYRVGDLLEFSCRSGHRVGPDSVQCYHFGWSPSFPTYKGQVASCAQPPEIPNGEINGAKRVEYSHGEVVGYDCKPRFLLKGPNKIQCVDGMWTTLPVCVEEERTCGDIPELEHGSVKFSVPPYHHGDSVEFTCAETFTMIGLGSVSCLSGKWTQLPKCVATDQLEKCRVLKSTDIEAIKPKRNEFQHNSTMYYKCRDKQEYEHSICINGKWNPEPNCTRKTSCPPPPQIPNTLVIETTVKYLDGEKLSVLCQDNYLTQDPEEMMCKDGRWQSLPHCIGLPCGPPPSILRGTVSLELESYQHGEEVTYHCSTGFGIDGPAFIKCEGGKWSDPPKCIKTNCDVLPTIENAIIRGKKKKSYRTGEQVTFRCQSPYQMNGSDTVTCVNSRWIGKPVCKDSRGKCGPPPPIDNGDITSLSLPEYEPFSSVDYQCQKYYLLKGKKTITCRNGKWSEPPTCLHACIIPENIMEARKIILKWRHTENIYSHSGEDIEFECKYGYHKARGSPPFRTKCISGTINYPTCE
Protein: Cellulose synthase A catalytic subunit 7 [UDP-forming] (EC 2.4.1.12) (OsCesA7) (Q9AV71)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation (By similarity). Involved in the secondary cell wall formation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cellulose synthase A catalytic subunit 9
- Zinc finger CCCH domain-containing protein 43
- Eukaryotic translation initiation factor isoform 4G-2
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor isoform 4G-1
- Cellulose synthase A catalytic subunit 4
- Os04g0682400 protein
- Os05g0185800 protein
- Polyadenylate-binding protein
- Os04g0405700 protein
Sequence:
MDTASVTGGEHKGKEKTCRVCGEEVAAREDGKPFVACAECGFPVCKPCYEYERSEGTQCCPQCNTRYKRHKGCPRVEGDEDDGGDMDDFEEEFQIKSPTKQKPPHEPVNFDVYSENGEQPAQKWRPGGPALSSFTGSVAGKDLEQEREMEGGMEWKDRIDKWKTKQEKRGKLNRDDSDDDDDKNDDEYMLLAEARQPLWRKVPIPSSKINPYRIVIVLRLVVLCFFLKFRITTPAMDAVPLWLASVICELWFALSWILDQLPKWSPVTRETYLDRLALRYERDGEPCRLAPIDFFVSTVDPLKEPPIITANTVLSILAVDYPVDRVSCYVSDDGASMLLFDTLSETAEFARRWVPFCKKFTIEPRAPEFYFSQKIDYLKDKVQPTFVKERRAMKREYEEFKVRINALVAKAQKKPEEGWVMQDGTPWPGNNTRDHPGMIQVYLGSQGALDVEGSELPRLVYVSREKRPGYNHHKKAGAMNSLVRVSAVLTNAPFILNLDCDHYVNNSKAVREAMCFLMDKQLGKKLCYVQFPQRFDGIDRHDRYANRNTVFFDINMKGLDGIQGPVYVGTGTVFNRQALYGYDPPRPEKRPKMTCDCWPSWCCCCCCFGGGKRGKSHKNKKGGGGGEGGGLDEPRRGLLGFYKKRSKKDKLGGGAASLAGGKKGYRKHQRGFELEEIEEGLEGYDELERSSLMSQKSFEKRFGQSPVFIASTLVEDGGLPQGAAADPAALIKEAIHVISCGYEEKTEWGKEIGWIYGSVTEDILTGFKMHCRGWKSVYCTPARAAFKGSAPINLSDRLHQVLRWALGSVEIFMSRHCPLWYAYGGRLKWLERFAYTNTIVYPFTSIPLLAYCTIPAVCLLTGKFIIPTLNNLASIWFIALFLSIIATGVLELRWSGVSIEDWWRNEQFWVIGGVSAHLFAVFQGLLKVLGGVDTNFTVTSKAAADETDAFGELYLFKWTTLLVPPTTLIIINMVGIVAGVSDAVNNGYGSWGPLFGKLFFSFWVILHLYPFLKGLMGRQNRTPTIVVLWSILLASIFSLVWVRIDPFIPKPKGPVLKPCGVSC
Protein: Tachykinin-related peptide 2 (TKRP-2) (P86564)
Organism: Banasa dimiata (Banasa stink bug) (Pentatoma dimiata)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APAAGFFGMR
Protein: ADAMTS-like protein 2 (ADAMTSL-2) (TSP1-repeat-containing protein 1) (TCP-1) (Q7TSK7)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Latent-transforming growth factor beta-binding protein 1
- Fibrillin-1
- GDP-fucose protein O-fucosyltransferase 2
- Beta-1,3-glucosyltransferase
Sequence:
MDGRRQHPHWAWSLLAVAVVAGGAAPTEASDNSPTSNSLEGGADTTAYWWGEWTKWTACSRSCGGGVTSQERHCLQQRRKSVPGTGNRTCVGTSKRYQLCRVQECPPDGRSFREEQCVSFNSRVYDGRAYQWKPLYPDDYVHISSKPCDLHCSTVDGQRQLTVPARDGTSCKLTDLRGVCVSGKCEPIGCDGVLFSTHTLDKCGVCQGDGSSCTHVTGNYRKGNNHLGYSLVTHIPAGARDIQIVERKKSADVLALADEAGFYFFNGNYKVDSPKNFNIAGTVVKYRRPMDVYETGIEYIVAQGPTNQGLNVMVWNQNGKSPSITFEYTLLQSPHMHHLPPVYYSFSEAASQSTESTERQELDSARLLGFMQHNGSLYRQTSSERLGLNSQLFQPPAPEVELGPSRGQESNEVCKQASGGVCEGPPRGKGFQDHNATGRAFSADKDDREISAHFTSHELLSANTISDQLLGTGSESEEFSLNETMNSIFAQGAPRSSPAESLYVDYEENEGPAAYLINGSYLELSSDRINTSSEAPFPNTSASPPNLAGNRTHKARTRPKARKQGVSPADMYRWKLSSHEPCSATCTTGVMSTYAMCVRYDGVEVDDSYCDALTRPEPVHEFCAGRECQPRWETSSWSECSRTCGEGHQFRIVRCWKMLSPGFDSSVYSDLCEATEAVRPEERKTCRNPACGPQWEMSEWSECTAKCGERSVVTRDIRCSEDEKLCDPSTKPVGEKNCTGPPCDRQWTVSDWGPCSGSCGQGRTIRHVYCKTSDGRVVPESQCQTETKPLAIHPCGDKNCPAHWLAQDWERCNTTCGRGVKKRLVLCMELANGKPQIRSGPECGLARKPPEESTCFERPCFKWYTSPWSECTKTCGVGVRMRDVKCYQGTDIVRGCDPLVKPVGRQACDLQPCPTEPPDDSCQDQPGTNCALAIKVNLCGHWYYSKACCRSCRPPHS
Protein: Voltage-dependent calcium channel gamma-4 subunit (Neuronal voltage-gated calcium channel gamma-4 subunit) (Transmembrane AMPAR regulatory protein gamma-4) (TARP gamma-4) (Q8VHW9)
Organism: Rattus norvegicus (Rat)
Function: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (By similarity). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs), including GRIA1 and GRIA4. Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization.
Subcellular location: Cell membrane {ECO:0000305|PubMed:17880894}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 4
- Glutamate receptor 1
- Glutamate receptor 3
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel gamma-7 subunit
- Protein cornichon homolog 2
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, NMDA 1
- Voltage-dependent R-type calcium channel subunit alpha-1E
Sequence:
MVRCDRGLQMLLTTAGAFAAFSLMAIAIGTDYWLYSSAHICNGTNLTMDDGPPPRRARGDLTHSGLWRVCCIEGIYKGHCFRINHFPEDNDYDHDSSEYLLRIVRASSVFPILSTILLLLGGLCIGAGRIYSRKNNIVLSAGILFVAAGLSNIIGIIVYISSNTGDPSDKRDEDKKNHYNYGWSFYFGALSFIVAETVGVLAVNIYIEKNKELRFKTKREFLKASSSSPYSRMPSYRYRRRRSRSSSRSTEASPSRDASPVGLKITGAIPMGELSMYTLSREPLKVTTAASYSPDQDAGFLQMHDFFQQDLKEGFHVSMLNRRTTPV
Protein: Putative antitoxin VapB19 (P95006)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC19.
Interaction partners:
- Ribonuclease VapC19
- Putative antitoxin VapB18
- Putative antitoxin VapB44
- Ribonuclease VapC18
Sequence:
MRTQVTLGKEELELLDRAAKASGASRSELIRRAIHRAYGTGSKQERLAALDHSRGSWRGRDFTGTEYVDAIRGDLNERLARLGLA