wanglab/gogpt-training-data huggingface dataset:
Protein: Protein PARTING DANCERS (AtPTD) (EC 3.1.-.-) (F4IDW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for chromosome segregation during meiosis. During diakinesis and prometaphase I, essential for the formation of class I meiotic crossovers and homologous recombination.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nucleic acid-binding, OB-fold-like protein
- E3 ubiquitin-protein ligase At1g12760
- Protein POOR HOMOLOGOUS SYNAPSIS 1
- Pentatricopeptide repeat-containing protein At1g12775
- Tetratricopeptide repeat
- Pentatricopeptide repeat
- F3F19.7
- Uncharacterized protein At1g63310
- At1g63230
- Crossover junction endonuclease MUS81
Sequence:
MATAGSSYSVSTDHQVSSPLVNLGNVAGVCIMSNAWKVEQEPSLINFISAFLSANSFRLNFVSIPPDLIFNCGGVSIAFVFVTKWDFSNVASIFSRVKRLKGQFAQLYVVATLSTKEQSDSFMRSYFQYEMEFGKPAFVQVTDAEMGFEKIVKIAHSRGVCKQQKVASKLKVERKRTVQDTNIFIRFVTSIPNINKHDANTLYQAIGSIEAIAKASKEDILANTDLSSKKADTLTRFFQDPEFYLSPKFN
Protein: Protein STIP1 homolog (Q54DA8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Heat shock cognate 90 kDa protein
Sequence:
MSENAQKATEFKNQGNAAFSSKDYNSAVKCFDQAIELDPSNHILYSNRSASLLALDKNEDALTDAKKAIELKPDWSKGYLRETNALYKLGRFEEAEKSAEAGLKIDPTNQQLEDALEDAQYATTGAKDPASAMANLFSAQNLTKLRFNPKTAPFFQQPDFVAIMDQISKNPSLFSQYIADQRFSTCLGVLLGVDINQGPGAPPQSQQPTPQQPTPTPQQPTPTPQQPKPTEAPKKPEAPPMTESQKERDLGNKAYAKKEFEQAIVHYDKAVELDSSDILAMNNKAAVLIEQQKLDEAIETCKKALEKAQEIRADYRVKSKVYTRLGNIYLKKNQLDDAYKAYSSAVLEDKNADTTANMKKIEKLKKQRDDEAYLSVDQSIIEKNKGVEHFKKGEFPEAIKCFEEAIRRNPKDHTIYSNRSAAYSKLLEYKLAIKDADKCIELEPTFIKGYIRKGTALFAMREYQQALEVYDQGLRIEANNPELLDLSRKTVAALTKLQSTLTDEERLQQAAKDPEIQKILSDPIMNQILKDMSENPAAAQDHLKNPLIMAKFQKLVNAGIVKLG
Protein: Ankyrin repeat domain 23 (D3ZVB9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Myopalladin
Sequence:
MVSGERVGRKALEFGRGVPDPGGWPSGWTLGPQEAVAWEKLKLEEEKRKKLERFNSSRLTLDNLTDLENLIQRRRKKRQRHKVPPREPESGAEPQPQVPLEPVGLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLARDWQRGIREALQAHVGHPRTRC
Protein: Plasma protease C1 inhibitor (C1 Inh) (C1Inh) (C1 esterase inhibitor) (C1-inhibiting factor) (Serpin G1) (P97290)
Organism: Mus musculus (Mouse)
Function: Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein.
Subcellular location: Secreted.
Interaction partners:
- Complement C1s-1 subcomponent
- Complement C1s-1 subcomponent
- Complement C1r-B subcomponent
- Complement C1r-A subcomponent
- Mannan-binding lectin serine protease 1
- Mannan-binding lectin serine protease 2
- Mannose-binding protein A
- Complement C1q subcomponent subunit B
- Mannose-binding protein C
- Kallikrein 1-related peptidase b8
Sequence:
MASRLTPLTLLLLLLAGDRAFSDPEATSHSTQDPLEAQAKSRESFPERDDSWSPPEPTVLPSTWPTTSVAITITNDTMGKVANESFSQHSQPAAQLPTDSPGQPPLNSSSQPSTASDLPTQATTEPFCPEPLAQCSDSDRDSSEAKLSEALTDFSVKLYHAFSATKMAKTNMAFSPFSIASLLTQVLLGAGDSTKSNLESILSYPKDFACVHQALKGFSSKGVTSVSQIFHSPDLAIRDTYVNASQSLYGSSPRVLGPDSAANLELINTWVAENTNHKIRKLLDSLPSDTCLVLLNAVYLSAKWKITFEPKKMMAPFFYKNSMIKVPMMSSVKYPVAQFDDHTLKAKVGQLQLSHNLSFVIVVPVFPKHQLKDVEKALNPTVFKAIMKKLELSKFLPTYLTMPHIKVKSSQDMLSVMEKLEFFDFTYDLNLCGLTEDPDLQVSAMKHETVLELTESGVEAAAASAISFGRSLPIFEVQRPFLFLLWDQQHRFPVFMGRVYDPRG
Protein: AUGMIN subunit 1 (F4IK01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in microtubules reorganization during spindle and phragmoplast development.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21750235}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21750235}. Note=Preferentially localizes to microtubules minus ends. {ECO:0000269|PubMed:21750235}.
Interaction partners:
- AUGMIN subunit 3
- AUGMIN subunit 6
- AUGMIN subunit 4
- AUGMIN subunit 2
- Putative RRM-containing protein family protein)
- LYR motif protein
- AUGMIN subunit 7
- Tubulin gamma-2 chain
- AUGMIN subunit 5
- Ribonucleases P/MRP protein subunit POP1
Sequence:
MSDVTGDLAAVSEAKGGSDAARISEVKAWLTSQFEAVGKEVPNFEYTHRSITHLYNLATASQAKSQAATIVANDFRLKASEYRAQAARIREILESAGMSQESLPSNVVSSAQVLANVANLLNIRDTELSSFLVAMGDISLRKTGVEEKRAKAQKESNALLDYTRKAIQRLTYLKKILAQLEDDVVPCESQMENWKTNLEVMAVKEEQYIQQYKKYEQMLLNRVGYTPKISHRELVEMAEHRKELDKMTKPVLDTLRSYQDLPPDKALAALAIEDKKRQFTAAEKYLEEVLQSALETNDE
Protein: Chromobox protein homolog 5 (Heterochromatin protein 1 homolog alpha) (HP1 alpha) (Q61686)
Organism: Mus musculus (Mouse)
Function: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P45973}. Chromosome {ECO:0000250|UniProtKB:P45973}. Chromosome, centromere {ECO:0000250|UniProtKB:P45973}. Note=Colocalizes with HNRNPU in the nucleus (By similarity). Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase. Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:P45973}.
Interaction partners:
- Histone H3.1
- Histone H3.3
- Histone H3.2
- Histone-lysine N-methyltransferase SUV39H1
- Transcription intermediary factor 1-beta
- Histone-lysine N-methyltransferase SETDB1
- CCAAT/enhancer-binding protein alpha
- Delta
- Chromatin assembly factor 1 subunit A
- Proline-rich protein 14
Sequence:
MGKKTKRTADSSSSEDEEEYVVEKVLDRRMVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSEGNKRKSSFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKESAKS
Protein: Sporulation-regulated protein 28 (Q04921)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Septins are GTPases involved in cytokinesis that assemble into filaments and form a ring at the cleavage site. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation (By similarity).
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Bud neck {ECO:0000250}. Note=Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate (By similarity). Localizes to ring-like structures around each of the four nuclear lobes at the onset and during meiosis II. Concentrated initially at the leading edge of the developing prospore wall. {ECO:0000250, ECO:0000269|PubMed:8885406}.
Interaction partners:
- Cell division control protein 11
- Sporulation-regulated protein 3
- Cell division control protein 10
- Cell division control protein 3
- Cell division control protein 12
- GTPase-GDP dissociation stimulator BEM4
- Spore-specific protein YSW1
Sequence:
MFPMKDHSALEQHTLSRDELRRRKGYKKGLQLSILLLGEKGSGKSTFLNNLCGQDISLSDGDYDDDDDKVTNNVTPENGNAIEDIDPGYKTAHLSPGLKLVTRRVYLNDELGVPITLDIILFPGCGDNVDNSQSSVVIKNYLDQQFANVLKEEVRIKRNTKETDGRPHVCLYFLKSTPRGVKKFDIELMKTICDKVNLIPIIPKADGLTETELNLHKDIVRQEISQNNIRVFDFKSDTLGETLALYDMDIDSSSAKSKYDNDTKIKEISPFAIVCSKTFNKNSENRVEHIRTYEWGSLVVEDQNTSDFIYLKAILLGSHLQELKDVTNNVLYENYRAKVLTEKKNNYDIPNYSYIDETSRGSVSNVSTRRNSASRTLGNPDTNDENAYQIHKEIDEKNRIIEDYQRKIDLLEKMLAAPHQNKV
Protein: HIG1 domain family member 2A (Q9CQJ1)
Organism: Mus musculus (Mouse)
Function: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May be involved in cytochrome c oxidase activity. May play a role in the assembly of respiratory supercomplexes (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}. Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- Cytochrome c oxidase assembly protein COX14
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Ragulator complex protein LAMTOR2
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase assembly factor 3 homolog, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MAAPGPVSPEAPFDPSKPPVIEGFSPTVYSNPEGFKEKFIRKTRENPMVPIGCLGTAAALTYGLYCFHRGQSHRSQLMMRTRIAAQGFTVVAILLGLAASAMKSQA
Protein: Nuclear receptor binding SET domain protein (EC 2.1.1.357) (Maternal-effect sterile 4 homolog) (Probable histone-lysine N-methyltransferase Mes-4) (Q8MT36)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable histone methyltransferase. Histone methylation gives specific tags for epigenetic transcriptional activation or repression (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase
- Calmodulin-lysine N-methyltransferase
Sequence:
MKLSTDAHSEIEGDAAHGNVLCNSASDSLTATDEVAAGNDESVATEGDDVEIPRDTNNSTPVRLLDKPGQNPVQNGAQPAAEESELESQRQTPVQKQQQQRVSMVNRKRDLINLQSALSPKYIGYANANSPTPLSDSDDTIRTTRRRVNQAAALNNSSAGETLAHDNASPRTPGGGGGGGGDDSANQLLSKTYMSPIEKLLIKNGASSPNSTGFEAGSEDLGIRPIVRKHVKRKMKRVPKAKVTLELDEKNQQEVDEKSVKTEPIDEEVDRTDEAPTQEAQTTAISIKSETEAEHKAAVDVHIKQEDTIRLDIVNNPVESTSIVITEEPKDLEKSTEELAFALPLASSTEVDLKSPPDLSSTALATSIKSPSSVSIDSAKGLSIVTDPGWPTYQVGDLFWGKVFSYCFWPCMVCPDPLGQIVGNMPSHPQRSSLDNANVPIQVHVRFFADNGRRNWIKPENLLTFAGLKAFDDMREELRIKHGPKSAKYRQMVPKRTKVVIWRQAIEEAQAMTQIPYSDRLEKFYQTYENVVTLNRQKRKRTKYMMQDTSDVGSSLYDSTDNLHNKQGTQLLAVKRERSESPFSPAFSPVKSKNEKRAKRRKLSNGTEADTGSNSMAVTPSQTETTVDSSAYENPEFRQLLSAVMEYVMMNRSDEKVEKVLLSVVSNIWSLKQIQLRELERDLASGEIEEPLGSSVVGRGSGVGTIKRLSNRLMTMMVRRSMTPVVTPSTTPAPSEPDRRLSEPPKTKKPVNRPIEEVIEDILQLDSKYLFRGLSREPICKYCYQAGSDLVRCSRTCSSWLHADCLERKVTGAPMPKIGSRKALVIPPTSKSPSPDEDHVTADAKEVVAVGTSLVCHECNVGEPEGCVICHQVESPAVPSTPRKEDSSSHTPIEDKLLTCSQPMCGKRFHTSCCKYWPQASSSKHSARCPRHVCHTCVSDDPSGKFQQLGSSKLAKCVRCPATYHQLSKCIPAGTQMLNTTNIICPRHNIAKADAHVNVLWCYICVKGGELVCCETCPIAVHAHCRNIPIKTNESYICEECESGRLPLYGEIVWAKFNNFRWWPAIILPPTEVPSNILKKAHGENDFVVRFFGTHDHGWISRRRVYLYIEGDTGDGHKTKSQLFRNYTTGVEEASRFLPIIKARRQEQDMERQSGNKLHPPPYVKIKTNKAVPPLRFSQNLEDLSTCNCLPVDEHPCGPEAGCLNRMLFNECNPEYCKAGSLCENRMFEQRKSPRLEVVYMNERGFGLVNREPIAVGDFVIEYVGEVINHAEFQRRMEQKQRDRDENYYFLGVEKDFIIDAGPKGNLARFMNHSCEPNCETQKWTVNCIHRVGIFAIKDIPVNSELTFNYLWDDLMNNSKKACFCGAKRCSGEIGGKLKDDAVKAHAKLKQMRRAKASAVRIHVKPKKTPKVKHISADDEPMDAKDE
Protein: Immunoglobulin lambda constant 7 (Ig lambda-7 chain C region) (A0M8Q6)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
GQPKAAPSVTLFPPSSEELQANKATLVCLVSDFNPGAVTVAWKADGSPVKVGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCRVTHEGSTVEKTVAPAECS
Protein: Speedy protein 1-B (Spy1-B) (Protein Ls27) (Rapid inducer of G2/M progression in oocytes B) (RINGO-B) (XSpy1-B) (p33 ringo-B) (xRINGO-B) (Q9YGL1)
Organism: Xenopus laevis (African clawed frog)
Function: Stimulates oocyte maturation by promoting meiotic G2/M progression in resting oocytes, via activation of the MAPK cascade and cdc2-cyclin B. Also activates the kinase activity of cdk2; this activation does not appear necessary for oocyte maturation. Necessary for polyadenylation in oocytes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5MJ70}.
Interaction partners:
Sequence:
MRHMQSATRATLVCGSGVKQIIAKGHPNTRVFGARKARIPEREVLAAKPKITRITHLNLQPQERQAFYRLLENELIQEFLSMDSCLKISDKYLIAMVLAYFKRAGLYTGEYTTMNFFVALYLANDMEEDEEDYKYEIFPWALGDSWREFFPQFLRLRDNFWAKMNYRAVVSRRCCDEVMAKDPTHWAWLRDRPIHHSGALRGYLRNEDDFFPRGPGLTPASCALCHKASVCDSGGVAHDNSSPEQEIFHYTNREWSQELLILPPELLLDPESTYDIHIFQEPLVGLEPDGAALEWHHL
Protein: Oxidoreductase NdmD (EC 1.-.-.-) (H9N291)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the oxidation of NADH and transfers electrons to NdmA and NdmB, which catalyze the N-demethylation reactions.
Interaction partners:
Sequence:
MNKLDVNQWFPIATTEDLPKRHVFHATLLGQEMAIWRDDSGSVNAWENRCPHRGLRLTLGANTGNELRCQYHGWTYESGTGGCTFVPAHRDAPPPNAARVNTFPVREKHGFIWTTLGQPPGEPISILDDAQLVNAVKTNLHSVVIDADIDGVVSVLRQNLSAFIDVFGAASAEDLHLKSMLQDRGILVTRSGSIAIHFYMQRSTISKCVVHAQVLTPGRPGYELQKNYSYAMNVIRRAAEAVATDLISITDISDQTIEKLEVVRENMTKAPPTHYICEVVTRTQETGDINSYWLKPIGYPLPAFSPGMHISITTPEGSIRQYSLVNGPDERESFIIGVKKEIQSRGGSRSMHEDVKVGTQLKVTLPRNGFPLVQTRKHPILVAGGIGITPILCMAQALDQQGSSYEIHYFARAFEHVPFQDRLTALGDRLNVHLGLGPDETRAKLPDIMEIHNAQDVDVYTCGPQPMIETVSAVALAHGIAEESIRFEFFSKKNDVPVSDEEYEVELKKTGQIFTVSPGSTLLQACLDNDVRIEASCEQGVCGTCITPVVSGDLEHHDTYLSKKERESGKWIMPCVSRCKSKKIVLDL
Protein: RE57622p (Q6AWN8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAIITSAFFSSMSFAGLFSGSLFQRFGMRQVGVTGGILYFLGTGMQLFATSTLHLIMAFSVVQGFAFGLMVPTCYTTFNHYFVKNRVMWMSFAQTLIGLGSMLYPIVMQKLMSWYGFRGCLLILTGLNAHAVFGMLVMHPVEWHMRRVPIQPEEQEELKELSPTVVIRVQPETPLKATREEPNFHTADPGARKLSHAEEQMLKVLSSRASSITSLGNWSGPVVVSDASPQMMHSLQTSRRPSTIAGASGAVAPAHATKKSWVRTIVDFLDLTLLKKPIFVNIVLGITFALYSDITFFTMQPVYLFELGYSRPDTATIIAIGAAADLASRIFLAITAVCIQVPSRYIYLAGAVFTVFARFGRRTLPWAPRTPFLPLISLIFPQPSTESHSLWAWPASRRSLDFCAPGSTFHCLWSLPTTCPRKGSPLAMAFSCSSKAMPCSSSVPLLGLFGTRPGITFSSFTS
Protein: Tubulin alpha-3D chain (EC 3.6.5.-) (Alpha-tubulin 3D) [Cleaved into: Detyrosinated tubulin alpha-3D chain] (P0DPH8)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY
Protein: DNA-directed RNA polymerase II subunit RPB11-a (RNA polymerase II subunit B11-a) (RPB11a) (DNA-directed RNA polymerase II subunit J-1) (RNA polymerase II 13.3 kDa subunit) (P52435)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9852112}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB7
Sequence:
MNAPPAFESFLLFEGEKKITINKDTKVPNACLFTINKEDHTLGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDYSPQEAFTNAITDLISELSLLEERFRVAIKDKQEGIE
Protein: Type IV pilin secretion protein (Q4QNP5)
Organism: Haemophilus influenzae (strain 86-028NP)
Interaction partners:
Sequence:
MTSYALLHTQRVTAQNGEIFTISPDLWERNQQQQSLLLRYFALPLKEENNRLWLGVDSLSNLSACETIAFITGKPVEPILLESSQLKELLQQLTPHQMQVEEQVKFYQHQETHFEQEDDEPVIRLLNQIFESALQKNASDIHLETLADQFQVRFRIDGVLQPQPLISKIFANRIISRLKLLAKLDISENRLPQDGRFQFKTTFSDILDFRLSTLPTHWGEKIVLRAQQNKPVELSFAELGMTENQQQAFQRSLSQPQGLILVTGPTGSGKSISLYTALQWLNTPDKHIMTAEDPIEIELDGIIQSQINPQIGLDFSRLLRAFLRQDPDIIMLGEIRDEESARIALRAAQTGHLVLSTLHTNDAISAISRLQQLGIQQHEIENSLLLVIAQRLVRKICPKCGGNLINSCDCHQGYRGRIGVYQFLHWQQNGYQTDFENLRESGLEKVSQGITDEKEIERVLGKNS
Protein: Spike protein P5 (Protein P5) (P22536)
Organism: Enterobacteria phage PRD1 (Bacteriophage PRD1)
Function: In association with P31 and P2, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity.
Subcellular location: Virion.
Interaction partners:
Sequence:
MANQQIGGSTVTYNGAIPMGGPVAINSVIEIAGTEVLVDLKLDYATGKISGVQTLYIDLRDFLGDVTVTMPDTGQRITARAGTQGYYPVLSTNLMKFIVSATIDGKFPMNFINFPIALGVWPSGIKGDKGDPGAPGPAGGTVVVEDSGASFGESLLDTTSEPGKILVKRISGGSGITVTDYGDQVEIEASGGGGGGGGVTDALSLMYSTSTGGPASIAANALTDFDLSGALTVNSVGTGLTKSAAGIQLAAGKSGLYQITMTVKNNTVTTGNYLLRVKYGSSDFVVACPASSLTAGGTISLLIYCNVLGVPSLDVLKFSLCNDGAALSNYIINITAAKIN
Protein: Histone deacetylase 2 (HD2) (EC 3.5.1.98) (Protein deacylase HDAC2) (EC 3.5.1.-) (YY1 transcription factor-binding protein) (P70288)
Organism: Mus musculus (Mouse)
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity (By similarity). May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A. In addition to protein deacetylase activity, also acts as protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92769}. Cytoplasm {ECO:0000250|UniProtKB:Q92769}.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein 4
- Histone-binding protein RBBP7
- DNA helicase
- DNA
- Paired amphipathic helix protein Sin3a
- Lysine-specific histone demethylase 1A
- Histone deacetylase 1
- Histone deacetylase complex subunit SAP30
- Histone-binding protein RBBP4
- Histone-lysine N-methyltransferase EZH2
Sequence:
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVAKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDPKGAKSEQLSNP
Protein: Origin recognition complex subunit 5 (Origin recognition complex 53 kDa subunit) (P50874)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. This subunit is a candidate for the mediation of ATP-dependent binding of ORC to origins. May also be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ORC5).
Subcellular location: Nucleus.
Interaction partners:
- ATP-dependent DNA helicase RRM3
- Origin recognition complex subunit 1
- Cell division cycle protein CDT1
- DNA replication licensing factor MCM6
- Origin recognition complex subunit 2
- Origin recognition complex subunit 4
- Cell division control protein 6
- DNA replication licensing factor MCM4
- Origin recognition complex subunit 6
- Nucleolar complex-associated protein 3
Sequence:
MNVTTPEVAFREYQTNCLASYISADPDITPSNLILQGYSGTGKTYTLKKYFNANPNLHAVWLEPVELVSWKPLLQAIARTVQYKLKTLYPNIPTTDYDPLQVEEPFLLVKTLHNIFVQYESLQEKTCLFLILDGFDSLQDLDAALFNKYIKLNELLPKDSKINIKFIYTMLETSFLQRYSTHCIPTVMFPRYNVDEVSTILVMSRCGELMEDSCLRKRIIEEQITDCTDDQFQNVAANFIHLIVQAFHSYTGNDIFALNDLIDFKWPKYVSRITKENIFEPLALYKSAIKLFLSTDDNLSENGQGESAITTNRDDLENSQTYDLSIISKYLLIASYICSYLEPRYDASIFSRKTRIIQGRAAYGRRKKKEVNPRYLQPSLFAIERLLAIFQAIFPIQGKAESGSLSALREESLMKANIEVFQNLSELHTLKLIATTMNKNIDYLSPKVRWKVNVPWEIIKEISESVHFNISDYFSDIHE