wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein P2A (P2A) (60S acidic ribosomal protein P2-alpha) (A2) (L12eIB) (L44) (YP2alpha) (P05319)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein P1B
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein P1A
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein P2B
Sequence:
MKYLAAYLLLNAAGNTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASAGGAAAASGDAAAEEEKEEEAAEESDDDMGFGLFD
Protein: Protein cereblon (Q56AP7)
Organism: Rattus norvegicus (Rat)
Function: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (By similarity). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16045448}. Nucleus {ECO:0000250|UniProtKB:Q96SW2}. Membrane {ECO:0000269|PubMed:16045448}; Peripheral membrane protein {ECO:0000269|PubMed:16045448}.
Interaction partners:
- Cullin-4A
- DNA damage-binding protein 1
- E3 ubiquitin-protein ligase RBX1
- Cullin-4B
- IKAROS family zinc finger 1
- IKAROS family zinc finger 3
- E3 ubiquitin-protein ligase ZFP91
- G1 to S phase transition 1
- Bromodomain containing 4
- DDB1 and CUL4 associated factor 15
Sequence:
MAGEGDHQDAAHNMGNHLPLLPADSEDEDDEIEMEVEDQDSKEARKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPEVMMILIPGQTLPLQLSHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQEFGIEVVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPISWEDQYSCKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKEDSLPANPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKASNLNLIGRPSTVHSWFPGYAWTIAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPETEDEISPDKVILCL
Protein: Jen1p (A0A1D8PKH9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEEKARADHISITNSNELNYDDYSNSYKNQPELDDELFNEKPDLSLSSISRYFATRLTTLLDLPLYHTHKKWYEVINPIPGLKSMSKSDWNFYCLGFFAWALDAMDFFCVSVAAPEIANTLNISVTDVTWGVTLVLMLRSVGAVIFGIASDYFGRKWTYISIVTLFVVVEVGTGFVQTYQQFLGVRAIFGILMGAMYPIAMVTALEGQPIAARSVLSGLFLPGYCFGYIMAMVWYRAFAGTYKEGEGWRSLIWFSGGLSLILIVWRLFTPESPDYIKMKIKKEKFNQQQRLKEQEQNGGVAVKEKKFWQKIDKSILVTFKTEWLIFSYLVLLYAGWNFTTHGSQDLYVTMITKQYHVGLDKKTVIIVVSNIGGIIGGIIMGQASELLGRRLTVVISIVCAGAFLYPSFFNPDRNWPAYIFLNAFVFGSFSVGPAYLLELVNSTHRTLLSGVAYQLGNLVSSASATIEAKIGERFPLKDQPGMFDYGKVMCIFCGAIFAYMIFIIFLGPERFHRDLQIHDTDEIEELQQDSSSNNESVKERV
Protein: Hepatocyte nuclear factor 1-beta (Transcription factor 2) (A0A087WZC2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MVSKLTSLQQELLSALLSSGVTKEVLVQALEELLPSPNFGVKLETLPLSPGSGAEPDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQTVQSSGNMTDKSSQDQLLFLFPEFSQQSHGPGQSDDACSEPTNKKMRRNRFKWGPASQQILYQAYDRQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSSNQTHSLNPLLSHGSPHHQPSSSPPNKLSGVRYSQQGNNEITSSSTISHHGNSAMVTSQSVLQQVSPASLDPGHNLLSPDGKMISVSGGGLPPVSTLTNIHSLSHHNPQQSQNLIMTPLSGVMAIAQSLNTSQAQSVPVINSVAGSLAALQPVQFSQQLHSPHQQPLMQQSPGSHMAQQPFMAAVTQLQNSHMSSTSLVMPTHHLLRAQQQGPCFPHHHPLGSCHGKAQ
Protein: FERM domain containing 7 (X6R7S7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVSHILQSELGDFHEETDRKHLAQTRYLPNQDCLEGKIMHFHQKHIGRSPAESDILLLDIARKLDMYGIRPHPASDGEGMQIHLAVAHMGVLVLRGNTKINTFNWAKIRKLSFKRKHFLIKLHANILVLCKDTLEFTMASRDACKAFWKTCVEYHAFFRLSEEPKSKPKTLLCSKGSSFRYSGRTQRQLLEYGRKGRLKSLPFERKHYPSQYHERQCRSSPDLLSDVSKQVEDLRLAYGGGYYQNVNGVHASEPVLESRRRNSALEVTFATELEHSKPEADPTLLHQSQSSSSFPFIYMDPVFNTEPNPNPDPRDIFSERSSLSSFQTSCKFSGNHMSIYSGLTSKVRPAKQLTYTDVPYIPCTGQQVGIMPPQVFFYVDKPPQVPRWSPIRAEERTSPHSYVEPTAMKPAERSPRNIRMKSFQQDLQVLQEAIARTSGRSNINVGLEEEDPNLEDAFVCNIQEQTPKRSQSQSDMKTIRFPFGSEFRPLGPCPALSHKADLFTDMFAEQELPAVLMDQSTAERYVASESSDSESEILKPDYYALYGKEIRSPMARIRLSSGSLQLDEEDEDAYFNTPTAEDRTSLKPCNYFLA
Protein: NAC domain containing protein 58 (Q9LS50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Type IV inositol polyphosphate 5-phosphatase 11
- Putative pentatricopeptide repeat-containing protein At3g18840
Sequence:
MEENLPPGFRFHPTDEELITHYLCRKVSDIGFTGKAVVDVDLNKCEPWDLPAKASMGEKEWYFFSQRDRKYPTGLRTNRATEAGYWKTTGKDKEIYRSGVLVGMKKTLVFYKGRAPKGEKSNWVMHEYRLESKQPFNPTNKEEWVVCRVFEKSTAAKKAQEQQPQSSQPSFGSPCDANSSMANEFEDIDELPNLNSNSSTIDYNNHIHQYSQRNVYSEDNTTSTAGLNMNMNMASTNLQSWTTSLLGPPLSPINSLLLKAFQIRNSYSFPKEMIPSFNHSSLQQGVSNMIQNASSSSQVQPQPQEEAFNMDSIW
Protein: Myozenin-1 (Calsarcin-2) (Filamin-, actinin- and telethonin-binding protein) (Protein FATZ) (Q9NP98)
Organism: Homo sapiens (Human)
Function: Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.
Subcellular location: Nucleus. Cell projection, pseudopodium. Note=Localized to the nucleus and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2, FLNC and MYOT at the Z-lines of skeletal muscle.
Interaction partners:
- Alpha-actinin-2
- Myotilin
- Telethonin
- Filamin-C
- Synaptopodin 2-like protein
- LIM domain-binding protein 3
- Troponin C, skeletal muscle
- Alpha-actinin-3
- Myosin regulatory light chain 11
- Myosin-7
Sequence:
MPLSGTPAPNKKRKSSKLIMELTGGGQESSGLNLGKKISVPRDVMLEELSLLTNRGSKMFKLRQMRVEKFIYENHPDVFSDSSMDHFQKFLPTVGGQLGTAGQGFSYSKSNGRGGSQAGGSGSAGQYGSDQQHHLGSGSGAGGTGGPAGQAGRGGAAGTAGVGETGSGDQAGGEGKHITVFKTYISPWERAMGVDPQQKMELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLSNRPSFNRTPIPWLSSGEPVDYNVDIGIPLDGETEEL
Protein: At3g05625 (Tetratricopeptide repeat (TPR)-like superfamily protein) (Q8GUK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSLTQIVNPIIYPSRTIPRRFTAISPFKTLSPQFSRHPPHALSRRLFLPSVSSIWDAITGGGDSNPREAIAAVRRGMQLFRQGDVAGSVAEFDRAIILDPRQKAYLWQRGLSLYYVDRFEEGAEQFRIDVAQNPNDTEESIWCFICEARLHGVDVARTQFLEVGRDSRPVMREAYNLFKNGGDPEKLVNDFSSGQASEYFYASLYAGLYYEAEGKSENAKFHLTAACGSPYGQRSDDYMASLAKVHCLCRNWSSGIL
Protein: Decaprenyl-diphosphate synthase subunit 2 (P91093)
Organism: Caenorhabditis elegans
Interaction partners:
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Farnesyl pyrophosphate synthase
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Atypical kinase coq-8, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein coq-4, mitochondrial
- Alkyl transferase
- Diphosphomevalonate decarboxylase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Sequence:
MGVLPKINIVARQFRKCSMAATSTSTSSSDNSVASTAFVQEHVRQMQNDIMVQLIPQDESGAVENLADLNVTSNLGRMTHYYFQQGGKMLRPTVSLLMGNACNSAANRSISEEYLAMLSTERSGIAAHLSVCQNQYKIGMIAEMIHTASLVHDDVIDEANTRRGSASVNAVWGNKMSVLVGDFILARATQILCSIGKPNIISVMASIIEDLVLGEFMQMSTTPTDATPVDRMKAYIEKTHRKTASLFASSCRSAAILADGSDLKLHEIAFEYGRNLGIAFQLADDLLDFIATADEMGKPVAADLKLGLATAPVLYACEQYPELNTMLLRKFKHDGDAEKAREIVVNSDGMDKTRRLIDSYSQKAVEMASSLPNRNESTEHLIKLAMSQSDRKF
Protein: AIR1A-like protein (At4g12530) (Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein) (Protease inhibitor/seed storage/lipid transfer protein family protein) (Q9SU32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Germin-like protein subfamily T member 3
- Bidirectional sugar transporter SWEET9
- Protein DETOXIFICATION 32
- Auxin efflux carrier component 6
- Bidirectional sugar transporter SWEET12
Sequence:
MSMAPKTSTTLALFLVTNILFLNLITLSCADNTCPRDVLKLSTCSNVLNLINLKLGAPAMRPCCSILFGLIDLDVAVCLCTALKLSLLGITIDTPIHLNLALNACGGTLPDGFRCPT
Protein: E3 ubiquitin-protein ligase TRIM37 (EC 2.3.2.27) (Mulibrey nanism protein) (RING-type E3 ubiquitin transferase TRIM37) (Tripartite motif-containing protein 37) (O94972)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication. Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes. Also acts as a positive regulator of peroxisome import by mediating monoubiquitination of PEX5 at 'Lys-472': monoubiquitination promotes PEX5 stabilitation by preventing its polyubiquitination and degradation by the proteasome. Has anti-HIV activity.
Subcellular location: Chromosome {ECO:0000269|PubMed:25470042}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15885686}. Peroxisome membrane {ECO:0000269|PubMed:11938494, ECO:0000269|PubMed:28724525}; Peripheral membrane protein {ECO:0000269|PubMed:28724525}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000269|PubMed:15885686}.
Interaction partners:
- TNF receptor-associated factor 6
- Peroxisomal targeting signal 1 receptor
- PEX5-related protein
- Gamma-butyrobetaine dioxygenase
- Peroxisomal ATPase PEX1
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Peroxisomal targeting signal 2 receptor
Sequence:
MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR
Protein: ATPase inhibitor, mitochondrial (ATP synthase F1 subunit epsilon) (Inhibitor of F(1)F(o)-ATPase) (IF(1)) (IF1) (O35143)
Organism: Mus musculus (Mouse)
Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- Eukaryotic translation initiation factor 5B
- Oocyte-secreted protein 1
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- ATP synthase F
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- ATP synthase F
Sequence:
MAGSALAVRARFGVWGMKVLQTRGFVSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (A0A8I5ZWZ4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGDLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQSSKNPTIPIQKLQDIQRAMELLSACQGPARNIDEATKRRYQFWDTQPVPKLNEVITSHGAIEPDKDNIRQEPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIRAVRELINVYLKQFHLAPVMGDEEVAHWFLPREHIIDTFVVESPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
Protein: RIC3 acetylcholine receptor chaperone (B0B1T9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
- Protein unc-50 homolog
- 5-hydroxytryptamine receptor 3A
- Lymphocyte antigen 6 family member H.
- Protein disulfide-isomerase TMX3
Sequence:
MAYSTVQRVALASGLVLAVSLLLPKAFLSRGKRPEPPPGPEGKLGRFPPMMHHHTAPSDGQTPGAHFQRSHLAEAFAKAKGAGGGAGGGGSGRGLMGQIIPIYGFGIFLYILYILFKLSKGKTAEDRNCSTAPPGNTHRKITNFELVQLQEKLKETEEAMEKLINRVGPNGESRAQTVTSDQEKRLLHQLREITRVMKEGKFIDTSPEKEAEEAPYMEDWEGYPEETYPIYDLSDGIKRRQETILVDYPDPKEPSAEETAEQMGALDEESSEHLSWDRLPTDPGVQRDNSVTLCDPKPESCSCCFHEDEDPAVLAENAGFSADGYSEQEEATKENLPQDFTDEGLGTSTDNTHVGGMLRKRSPQGFE
Protein: Peptidyl-prolyl cis-trans isomerase (Q57XM6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
Sequence:
MVTSTGLLSRVAAVEKAAEIAKPPPPKVVELTEAAKQLPQHIIGVTDPTKLNAQVSYFQCPPWAALPSVACHLQCTRDGLPLPALGLHRFPFYLFGRSKVCDYVLEHPSISSVHAVLVFHGGQRCFVLMDLGSTNGVKLNGNRIEKRRPLPAPVGSSIQFGFSSRVYKVQLGPPSSSKRLREEQERQEAEEGKRKCVEEDQQNGTLGDTRVSPSTSGAVSNEERIEGNVVVDRTVVESVAAETKEVVTCDGVLETSVQAGAPPPTERHFYHVLVKHKDVRRPSSLAPRNKGEKITRSRADAINLAQAILAQHKERKTWSLDEFVQVVRDFSECGSAKRDGDLGMVESGTYTEGFDTVAFSLKSGEVSAPVETELGVHLIYRVE
Protein: Antitoxin RelF (O33347)
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 toxin RelE2.
Interaction partners:
- Toxin RelG
- Toxin RelE
- Toxin RelK
- Antitoxin RelJ
Sequence:
MRILPISTIKGKLNEFVDAVSSTQDQITITKNGAPAAVLVGADEWESLQETLYWLAQPGIRESIAEADADIASGRTYGEDEIRAEFGVPRRPH
Protein: Protein MICRORCHIDIA 6 (AtMORC6) (EC 3.6.-.-) (Protein CRT1-homolog 6) (CRT1-h6) (Protein DEFECTIVE IN MERISTEM SILENCING 11) (Q56Y74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. Together with SUVH2 and SUVH9, regulates the silencing of some transposable elements (TEs). Exhibits ATPase activity. May also be involved in the regulation of chromatin architecture/condensation to maintain gene silencing. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair (By similarity). Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:22555433}. Note=Present in nuclear bodies near chromocenters. {ECO:0000269|PubMed:22555433}.
Interaction partners:
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- Histone-lysine N-methyltransferase family member SUVH9
- Protein RDM1
- Helicase protein MOM1
- Histone-lysine N-methyltransferase family member SUVH2
- SWI/SNF complex subunit SWI3D
- Protein CHROMATIN REMODELING 35
- SWI/SNF complex subunit SWI3B
- Protein INVOLVED IN DE NOVO 2
- DNA-directed RNA polymerase V subunit 1
Sequence:
MSHDRSVNVSHDAVIAKPERGTMLQSFSPRSHGSKGYSLPQDSEENRGSVGQSAGQSSTSVVDQVRSPADDAGVTSSSTICPAPVCRQFWKAGSYNDELSSKSQQPNGKNYLHVHPMFLHSNATSHKWAFGAVAELLDNAVDEIQNGATFVIVDKTTNPRDGATALLIQDDGGGMDPQAMRHCMGFGFSDKKSDSAIGRYGNGFKTSTMRLGADVIVFSRHSKNQTLTQSIGLLSYTYLTRTGHDRIVVPILDYEFNASAGEFKTLQDREHFISSLSILLEWSPFSTEAELLQQFDDVGPHGTKVIIYNMWLNSDAKLELDFDSVAEDILIEGSIKKTGSKIVNDHIASRFSYSLRVYLSILYLRIPETFKIILRGKVVEHHNVADDLMHPQYILYKPQAAGSEEALVVTTIGFLKEAPKVNLHGFCVYHKNRLIMPFWQVINYSSSRGRGVVGVLEANFVEPTHNKQDFEKTVLLQKLENRLKEMTVEYWSCHCVLIGYQVNKKPRLQIPQKVQPAGRQALSPPPGFQAVFPQGNTTSLPRVSTQPVLLEKRKEHPDSVASAALKRKVGNDDFTVPGHIRVEQFIHGSASQSQDIETVKLMEENKKLRAKCLDRKVRSQNLEVKAMNLRSELENYKSEYERLMVELQALDLVKDEHRRNVNT
Protein: Ral GTPase activating protein catalytic subunit alpha 2 (H7C1F9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLDIPHLRPKPVYITTTRDNENIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAVQERAPELDGGGPTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRMVYEMVQRILLSTRGYVNFVNEVFHQAFLLPSCEIAVTRKVVQVYRKWILQDKPVFMEEPDRKDVAQEDAEKLGFSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEENTNVKAGVQALLQVFLTNSANIFLLEPCAEVPVLLKEQVDACKAVLIIFRRMIMELTMNKKTWEQMLQILLRITEAVMQKPKDKQIKDLFAQSLAGLLFRTLMVAWIRANLCVYISRELWDDFLGVLSSLTEWEELINEWANIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCVLDPQKGTTVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNIVRQKATEVEECQQSENAPAAGSGHLTVGQQQQVLRSSSTSDIPEPLCSDSSQGQKAENTQNSSSSEPQPIQENKGHVKREHEGITILVRRSSSPAELDLKDDLQQTQGKCRERQKSESTNSDTTLGCTNEAELSMGPWQTCEEDPELNTPTDVVADADARHWLQLSPTDASNLTDSSECLTDDCSIIAGGSLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHARVFCYLYELWYKLAKIRDNLAISLDNQSSPSPPVLIPPLRMFASWLFKAATLPNEYKEGKLQAYRLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDILNTIIRHCPPRFFSLGFPGFSMLVGDFITAAARVLSTDILTAPRSEAVTVLGSLVCFPNTYQEIPLLQSVPEVNEAITGTEDVKHYLINILLKNATEEPNEYARCIAVCSLGVWICEELAQCTSHPQVKEAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETSLPRKMAEILVATVAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSVLLHPVSTAVLEEQHSARAPLLDYIYRVLHCCVCGSSTYTQQSHYILTLADLSSTDYDPFLPLANVKSSEPVQYHSSAELGNLLTVEEEKKRRSLELIPLTARMVMAHLVNHLGHYPLSGGPAILHSLVSENHDNAHVEGSELSFEVFRSPNLQLFVFNDSTLISYLQTPTEGPVGGSPVGSLSDVRVIVRDISGKYSWDGKVLYGPLEGCLAPNGRNPSFLISSWHRDTFGPQKDSSQVEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSLTPCGMNYDQEKEIIEVILRQNAQEDEYIQSHNFDSAMKVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILSNERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFIAITKKPEVPFFGPLFDGAIVSGKLLPSLVCATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSLSGTGALASSLSADLEEPLSEEETEHPLLPLPRATKPRISRKFRCCTSALSRSSH
Protein: Mating-type-like protein ALPHA2 (MTLalpha2 protein) (Q9UW22)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that acts in conjunction with A1 to repress transcription both of homozygote-specific genes and of genes necessary for the white-opaque switch, a prerequisite for mating.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MNSHSEALFEINQRLSSHIRTMSNFPVFDPQKITNDVEANIKRMTSILKSKRLTREDEDLMKMINDCSKVLHEMLLERIMLQQDSIQFFTEKEASDSPFSNSADTIDEDDDKKIKSRRLTKKQLLVLEGWFQKHKNHPYSQKDQTNLLIKSTKLSKSQVQNWISNRRRKEKNTKVSPELAALLLTG
Protein: Uncharacterized protein Rv1708 (P9WLT1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May play a role in septum formation.
Interaction partners:
- Segregation and condensation protein A
- Probable chromosome-partitioning protein ParB
- Possible segregation and condensation protein ScpB
- Cytidylate kinase
- Uncharacterized RNA pseudouridine synthase Rv1711
- GTPase Der
- Uncharacterized protein Rv3660c
- Chromosomal replication initiator protein DnaA
- Cell division protein FtsZ
- Probable conserved transmembrane protein
Sequence:
MPAGLPGQASVAVRLSCDVPPDARHHEPRPGMTDHPDTGNGIGLTGRPPRAIPDPAPRSSHGPAKVIAMCNQKGGVGKTTSTINLGAALGEYGRRVLLVDMDPQGALSAGLGVPHYELDKTIHNVLVEPRVSIDDVLIHSRVKNMDLVPSNIDLSAAEIQLVNEVGREQTLARALYPVLDRYDYVLIDCQPSLGLLTVNGLACTDGVIIPTECEFFSLRGLALLTDTVDKVRDRLNPKLDISGILITRYDPRTVNSREVMARVVERFGDLVFDTVITRTVRFPETSVAGEPITTWAPKSAGALAYRALARELIDRFGM
Protein: PLAT domain-containing protein 1 (AtPLAT1) (PLAT domain protein 1) (O65660)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of abiotic stress tolerance involved in the regulation of plant growth. May be a downstream target of the abscisic acid (ABA) signaling pathway.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:25396746}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653}. Note=Localizes to rod shaped ER structures that resemble ER bodies. {ECO:0000269|PubMed:25396746}.
Interaction partners:
- MD-2-related lipid recognition domain-containing protein
- GDSL esterase/lipase At1g29660
- Phosphatidylinositol N-acetyglucosaminlytransferase subunit P-like protein
- Lipoxygenase 6, chloroplastic
- Lipoxygenase 4, chloroplastic
- Lipoxygenase 3, chloroplastic
- Thioredoxin-like 2-2, chloroplastic
- Major latex homologue type2
- Lipoxygenase 2, chloroplastic
Sequence:
MARRDVLLPFLLLLATVSAVAFAEDDPDCVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNNCPVKLRDSVSRVGSEIRKKLSWVV