wanglab/gogpt-training-data huggingface dataset:
Protein: Protein-arginine deiminase type-2 (EC 3.5.3.15) (Peptidylarginine deiminase II) (Protein-arginine deiminase type II) (P20717)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2J8}.
Interaction partners:
Sequence:
MLRERTVRLQYGSRVEAVYVLGTQLWTDVYSAAPAGAKTFSLKHSEGVKVEVVRDGEAEEVVTNGKQRWALSPSTTLRLSMAQASTEASSDKVTVNYYEEDGSAPIDQAGLFLTAIEISLDVDADRDGEVEKNNPKKASWTWGPEGQGAILLVNCDRDTPWLPKEDCSDEKVYSKQDLQDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRQKLYHVVKYTGGSAELLFFVEGLRFPDESFSGLVSIHVSLLEYMAEDIPLTPIFTDTVTFRIAPWIMTPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYMNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKDFPIKQLLGPDFGYVTREPLFETVTSLDSFGNLEVSPPVTVNGKAYPLGRILIGSSFPLSGGRRMTKVVRDFLQAQQVQAPVELYSDWLTVGHVDEFMTFVPIPGKKEFRLLMASTSACYQLFREKQKEGHGEAIMFKGLGGMSSKRITINKILSNESLTQENQYFQRCLDWNRDILKKELALTEKDIIDLPALFKMDEDRQARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLETHVRGLLEPLGLACTFIDDISAYHKFLGEVHCGTNVRRKPFTFKWWHMVP
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) (P04406)
Organism: Homo sapiens (Human)
Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250|UniProtKB:P04797}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions (PubMed:12829261). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:12829261}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Large ribosomal subunit protein uL13
- Fructose-bisphosphate aldolase A
- Phosphoglycerate kinase 2
- Phosphoglycerate kinase 1
- Heterogeneous nuclear ribonucleoprotein Q
- Triosephosphate isomerase
- Alpha-enolase
- E3 ubiquitin-protein ligase SIAH1
- Glucose-6-phosphate isomerase
Sequence:
MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE
Protein: EF-hand calcium-binding domain-containing protein 12 (Q6NXP0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDDDYEAYHSLFLSLLGLCPSKTPINENAPVFDPEPVIAHCFKQFQQKDFRLPQTRRRIIMVPRKEDQTPLNPASQPQAPPKPIPSFKVLEARDIQEQPEDRKTWLSQRSKLRQELESFGDVKRWLENKPSITPSEAKVLHMIHEEQSAQPNASQATTRTTRKKAPRLSRLSRQMVPQLQLPEPPALSVMYSYLHSRKIKILEIFHKVGQGENQRITREEFIAAVKAVGVPLKNQEVEDIVIYLSSLGKHNTITMDILANTYKQWSMAQQRSSLATAREHYILAKHRDSLKGPLKKQEVDSAPQLPKVDLLTVPAVDTQMETRPMTLEEMEEVGKRYRERQRQHKLTIPSIQYTEQCHLVRCGNRHFDEHCLPSTIHGDMRELIDSARRHNFLVYLQCWKLCKSYGLPLTEDILMKALLYPGDKIIFQMDKVCPIRQPGGYYSDWKVFSPNLALLRSQGPGKSKRTDKKTPKKSKKMRFKEFEEFTRKLKVKRSSGLQQTHPNSFWPGHLLDKLQLYLPTVATDRSLALFSCVQHQPHVYPATYHPDHWWPLRNKNYMTHAHYDAAKVYYIN
Protein: Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3) (Q6TRW4)
Organism: Rattus norvegicus (Rat)
Function: Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:12072405}.
Interaction partners:
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1A
- Nipped-B protein
- Cohesin subunit SA
- RAD21 cohesin complex component
- Cohesin subunit SA
- Cell division cycle-associated 5.
- Structural maintenance of chromosomes protein
- Sister chromatid cohesion protein PDS5 homolog A
Sequence:
MAHSKTRTNDGKITYPPGVKEISDKISKEEMVRRLKMVVKTFMDMDQDSEEEKELYLNLALHLASDFFLKHPDKDVRLLVACCLADIFRIYAPEAPYTSPDKLKDIFMFITRQLKGLEDTKSPQFNRYFYLLENIAWVKSYNICFELEDSNEIFTQLYRTLFSVINNGHNQKVHMHMVDLMSSIICEGDTVSQELLDTVLVNLVPAHKNLNKQAYDLAKALLKRTAQAIEPYITNFFNQVLMLGKTSISDLSEHVFDLILELYNIDSHLLLSVLPQLEFKLKSNDNEERLQVVKLLAKMFGAKDSELASQNKPLWQCYLGRFNDIHVPIRLECVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVSIVTAAKKDILLVNDHLLNFVRERTLDKRWRVRKEAMMGLAQIYKKYALQSAAGKDAAKQICWVKDKLLHIYYQNSIDDRLLVERIFAQYMVPHNLETTERMKCLYYLYATLDLNAVKALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKVMVITRNLPDPGKAQDFMKKFTQVLEDDEKIRKQLEALVSPTCSCKQAEGCVREITKKLGNPKQPTNPFLEMIKFLLERIAPVHIDTESISALIKQVNKSIDGTADDEDEGVPTDQAIRAGLELLKVLSFTHPISFHSAETFESLLACLKMDDEKVAEAALQIFKNTGSKIEEDFPHIRSALLPVLHHKSKKGPPRQAKYAIHCIHAIFSSKETQFAQIFEPLHKSLDPSNLEHLITPLVTIGHIALLAPDQFAAPLKSLVATFIVKDLLMNDRLPGKKTTKLWVPDEEVSPETMVKIQAIKMMVRWLLGMKNNHSKSGTSTLRLLTTILHSDGDLTEQGKISKPDMSRLRLAAGSAIVKLAQEPCYHEIITLEQYQLCALAINDECYQVRQVFAQKLHKGLSRLRLPLEYMAICALCAKDPVKERRAHARQCLVKNITVRREYLKQHAAVSEKLLSLLPEYVVPYTIHLLAHDPDYVKVQDIEQLKDVKECLWFVLEILMAKNENNSHAFIRKMVENIKQTKDAQGPDDTKMNEKLYTVCDVAMNIIMSKSTTYSLESPKDPVLPARFFTQPDKNFSNTKNYLPPEMKSFFTPGKPKTANVLGAVNKPLSSAGKQSQTKSSRMETVSNASSSSNPSSPGRIKGRLDSTEMDHSENEDYTMSSPLPGKKSDKREDSDLVRSELEKPRSRKKASVTDPEEKLGMDDLSKLVQEQKPKGSQRGRKRGHAASESEEQQWPEEKRHKEELLGNEDEQNSPPKKGKRGRPPKPLGGTSKEEPVVKTSKKGNKKKPAPPVVDEDEEEERQMGNTEQKSKSKQQRTSKRAQQRAESPETSAVESTQSTPQKGRGRPSKTPSPSQPKKNIRVGRSKQVATKENDSSEEMDVLQASSPVSDDTTQEGAEEEDISAGNVRRRSSKRERR
Protein: TRF-like 10 (C0SVN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription factor bHLH168
- AT-rich interactive domain-containing protein 2
- Transcription factor bHLH155
- Transcription factor bHLH109
- Transcription factor GTE1
- COP1-interacting protein 7
- SHUGOSHIN 1
Sequence:
MIEKKLSKMKMRTKSIPVRSSRKSLDSLLDDEANENTQCDERDVPHKKRRCLGTSETTDRGGSVEPLLDLDACIVCEVSDERVSRCCGVDCLLSFHGECLYADLGSTSSSSSSSSEDVSNPFCPYCWLKIVALKSKTLREKTVEAEKAVCKYLDKEMKSRDEDITLSGDEIGNQEQSTDIVSDHELQGEKDGCSSKPDADQGKVGTGKVIDEVGASEKVATEKFQDAEDDETAKDQGTRILNTGAGKKREVSSFLSMQESFSAKEQDQVQQNEKRRRRGLKIIDSDISSKGSSNERNGEDVTEQVTSSVQVTSPSGRMRNQQATTKVVAKSKTVRDISFFKMDQRRRLLWTYEEEEMLKVGVEKFAAEANKNMPWRKILEMGEKVFHETRTPADLKDKWRSMVKIMNKNEQGSTLTPTAM
Protein: KIN14B-interacting protein At4g14310 (F4JUQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might be involved in division plane determination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20706207}. Note=Localizes at the pre-prophase band. {ECO:0000269|PubMed:20706207}.
Interaction partners:
- Bromodomain testis-specific protein
- Cyclin-dependent kinases regulatory subunit 2
- Putative cyclin-A3-1
- Cyclin-A3-4
- Kinesin-like protein KIN-14B
- Thylakoid lumenal 17.9 kDa protein
- Glycine-rich protein family
- Gamma-tubulin complex component 3
- DEAD-box ATP-dependent RNA helicase 55
- Protein SAMBA
Sequence:
MSASTNRRRLKDINTGAGENPSSGKKPLRSVTPLPISSKNSNPALQKSLSSKENPNPKLSHRSFGSTQKPVLRPVPRIDKSAVSGEGRVTRSTSSGLRGRSSSPSDLIRVFSDLRKRNESRVIGEKGESGQDKKSGLKSSGFKQGTSEIKVEPSSVCEKADEGSSCPVNSSKFEGSSVARNSISDPKAHALVGSGEKSTVALKSDSKIEKTGKGTSVALRRKSLDNVGKAMEMSKDIRGNEGSSNSTAKYPSKLHEKLAFLEGKVKKIASDIKKTKDMLDLNNPDSSKVIISDIHQKITGIEKSMSHVIDGPEKNKTTKAKSSVKGLNKEELEDRLLPHQRLLRSRTQSKTSSHVSKGHDSVESNKAVNAEEKPSAPVEENAIALEFLASLDKEKVTFMSDQNALENLEVQEMDTEEPSKENDVSKDVNLTSNLTEILRANEALEEIDDEENREEMELEEIDDGCMYQLNDIGSKTSTGGWFVSEGEAVILAHDDGSCSYYDVANSEFMVNECNSLSIWVRLYEVTGVFGFVHYVKSVYSPPDGISPNTWRDCWVVRAPGADGCSGRYVVAASAGNTLESGFCSWDFYTKDIKALHIEDGSSRVSRTALAPLPNNTSHGRNTPACAVVPETQQWWYRPCGPLIASTGSFQSIVKVFDIRDGEQIMKWGVQNPVSALDYSSPLQWRNRGKLVIAETEAISVWDVNSLHPEAQHTISSSGRKISAFHINNTDAEVGGGVRQRVSSLDAEGNDGVFCTSDSINILDFRNPSGIGAKIPKLGVNAQCVSSRGDSVFLGCTNQKSTVKKQMASSSQVQQFSIRKQRLVSTYSLPDSNSHPHHSAITQVWGNSNFVMATSGMGLFVFDTAKEETLQQQPLTSDYGSVQTVREIIGPNDMYCPSFDYSGCRVLLISRDRPALWRYLL
Protein: F-box only protein 11 (Protein arginine N-methyltransferase 9) (Vitiligo-associated protein 1) (VIT-1) (Q86XK2)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53.
Subcellular location: Nucleus {ECO:0000269|PubMed:16487488, ECO:0000269|PubMed:17098746, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:25827072}. Chromosome {ECO:0000269|PubMed:23892434}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Denticleless protein homolog
- B-cell lymphoma 6 protein
- DNA mismatch repair protein Msh6
- F-box/LRR-repeat protein 14
- Ubiquitin-like protein NEDD8
- Cellular tumor antigen p53
- NEDD8-activating enzyme E1 catalytic subunit
Sequence:
MNSVRAANRRPRRVSRPRPVQQQQQQPPQQPPPQPPQQQPPQQQPPPPPQQQQQQQPPPPPPPPPPLPQERNNVGERDDDVPADMVAEESGPGAQNSPYQLRRKTLLPKRTACPTKNSMEGASTSTTENFGHRAKRARVSGKSQDLSAAPAEQYLQEKLPDEVVLKIFSYLLEQDLCRAACVCKRFSELANDPILWKRLYMEVFEYTRPMMHPEPGKFYQINPEEYEHPNPWKESFQQLYKGAHVKPGFAEHFYSNPARYKGRENMLYYDTIEDALGGVQEAHFDGLIFVHSGIYTDEWIYIESPITMIGAAPGKVADKVIIENTRDSTFVFMEGSEDAYVGYMTIRFNPDDKSAQHHNAHHCLEITVNCSPIIDHCIIRSTCTVGSAVCVSGQGACPTIKHCNISDCENVGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQAGVLISTNSHPILRKNRIFDGFAAGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIEKAVSRGQCLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAGEPTHDTDTLYDSAPPIESNTLQHN
Protein: CDGSH iron-sulfur domain-containing protein 3, mitochondrial (MitoNEET-related protein 2) (Miner2) (Mitochondrial inner NEET protein) (MiNT) (P0C7P0)
Organism: Homo sapiens (Human)
Function: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17376863}.
Interaction partners:
- CDGSH iron-sulfur domain-containing protein 1
- CDGSH iron-sulfur domain-containing protein 2
- Large ribosomal subunit protein uL24m
Sequence:
MRGAGAILRPAARGARDLNPRRDISSWLAQWFPRTPARSVVALKTPIKVELVAGKTYRWCVCGRSKKQPFCDGSHFFQRTGLSPLKFKAQETRMVALCTCKATQRPPYCDGTHRSERVQKAEVGSPL
Protein: Frizzled 7a (Frizzled 7b) (Frizzled class receptor 7b) (Frizzled-7b precursor) (Q8QFM3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Tyrosine-protein kinase RYK
- Glypican 4
- E3 ubiquitin-protein ligase znrf3
- Protein Wnt-5b
- Protein Wiz isoform X1
- Protein Wnt
- Protein Wnt-11
- Protein Wnt
- Low density lipoprotein receptor-related protein 5
- Protein Wnt
Sequence:
MMAVREVGPCVYKTYCVFITTLLFGLSSAQYHGEKGISVPEHGFCQPISIPLCTDIQYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSQDLKFFLCSMYAPVCTVLEQAIPPCRTLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNKSDPDVPTTNPTPYIPEPFSPRIHTPRQNQAFTCPLQLTVPSYLNYHFLGAKNCGAPCEHKQPYGLMYFKEEEVRFGRLWVGIWSILCCVSTLFTVLTYLVDMRRFHYPERPIIFLSGCYFMVAVAYAAGFLLEDKVVCIDKFRDDAFKTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLSAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILALGQVDGDLLTGVCYVGIYNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFREQWEKTWHMQTCKRFAVPCPNNNFAPMTPDFTVFMIKYLMTMIVGITSGFWIWSGKTLQSWRRFYKRLGNNQGETTV
Protein: Junctional sarcoplasmic reticulum protein 1 (Junctional-face membrane protein of 45 kDa homolog) (JP-45) (Q96MG2)
Organism: Homo sapiens (Human)
Function: Involved in skeletal muscle excitation/contraction coupling (EC), probably acting as a regulator of the voltage-sensitive calcium channel CACNA1S. EC is a physiological process whereby an electrical signal (depolarization of the plasma membrane) is converted into a chemical signal, a calcium gradient, by the opening of ryanodine receptor calcium release channels. May regulate CACNA1S membrane targeting and activity.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Colocalizes with ryanodine receptors at the sarcoplasmic reticulum triad membranes. {ECO:0000250}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Calsequestrin-1
- Triadin
Sequence:
MSMTTRAWEELDGGLGSCQALEDHSALAETQEDRASATPRLADSGSVPHDSQVAEGPSVDTRPKKMEKEPAARGTPGTGKERLKAGASPRSVPARKKAQTAPPLQPPPPPPALSEELPWGDLSLNKCLVLASLVALLGSAFQLCRDAVPGEAALQARVPEPWVPPSSAPREPSSPLPKFEAQAPPSAPPAPRAEAEVRPKIPGSREAAENDEEEPGEATGEAVREDRVTLADRGPKERPRREGKPRKEKPRKEERPKKERPRKEERPRAAREPREALPQRWESREGGHRPWARDSRDAEPRKKQAWVSPRRPDEEQRPGSRQKLRAGKGRD
Protein: Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.11.23) (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (MP86) (Protein kinase minibrain homolog) (MNBH) (Q61214)
Organism: Mus musculus (Mouse)
Function: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Exhibits a substrate preference for proline at position P+1 and arginine at position P-3 (By similarity). Plays an important role in double-strand breaks (DSBs) repair following DNA damage (By similarity). Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR) (By similarity). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A (By similarity). May play a role in a signaling pathway regulating nuclear functions of cell proliferation (By similarity). Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits p53/TP53 activity and apoptosis. Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434'.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:9070862}.
Interaction partners:
- DDB1- and CUL4-associated factor 7
- Forkhead box protein M1
- Protein lin-54 homolog
- Protein lin-52 homolog
- Calcipressin-1
- E3 ubiquitin-protein ligase RNF169
- Phosphorylated adapter RNA export protein
- Protein lin-37 homolog
- Protein lin-9 homolog
- Protein FAM53C
Sequence:
MHTGGETSACKPSSVRLAPSFSFHAAGLQMAAQMPHSHQYSDRRQPSISDQQVSALPYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWSLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFAAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLAMRQGADREESPMTGVCVQQSPVASS
Protein: Protein PHOSPHATE STARVATION RESPONSE 2 (OsPHR2) (Q6Z156)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor involved in phosphate starvation signaling. Binds to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to promote the expression of inorganic phosphate (Pi) starvation-responsive genes. Functionally redundant with PHR1 and PHR3 in regulating Pi starvation response and Pi homeostasis. Involved in both systematic and local Pi-signaling pathways. Regulates several Pi transporters. Regulates the expression of PT2. Directly up-regulates SPX1 and SPX2 expression, but PHR2 binding to DNA is repressed redundantly by SPX1 and SPX2 in a PI-dependent manner. The DNA-binding activity is also repressed by SPX4. Involved in root growth under Pi deprivation. Involved in the modulation of Pi response and homeostasis together with RLI1; promotes RLI1 expression in response to nitrate availability, thus triggering the nitrate-induced phosphate response (NIPR).
Subcellular location: Nucleus {ECO:0000269|PubMed:18263782, ECO:0000269|PubMed:24692424}. Cytoplasm {ECO:0000269|PubMed:24692424}. Note=Interaction with SPX4 trap PHR2 within the cytoplasm and affects the nuclear localization. {ECO:0000269|PubMed:24692424}.
Interaction partners:
- SPX domain-containing protein 1
- SPX domain-containing protein 2
- SPX domain-containing protein 4
- Os01g0314700 protein
- Kinesin-like protein KIN-14I
Sequence:
MERISTNQLYNSGIPVTVPSPLPAIPATLDENIPRIPDGQNVPRERELRSTPMPPHQNQSTVAPLHGHFQSSTGSVGPLRSSQAIRFSSVSSNEQYTNANPYNSQPPSSGSSSTLNYGSQYGGFEPSLTDFPRDAGPTWCPDPVDGLLGYTDDVPAGNNLTENSSIAAGDELAKQSEWWNDFMNYDWKDIDNTACTETQPQVGPAAQSSVAVHQSAAQQSVSSQSGEPSAVAIPSPSGASNTSNSKTRMRWTPELHERFVDAVNLLGGSEKATPKGVLKLMKADNLTIYHVKSHLQKYRTARYRPELSEGSSEKKAASKEDIPSIDLKGGNFDLTEALRLQLELQKRLHEQLEIQRSLQLRIEEQGKCLQMMLEQQCIPGTDKAVDASTSAEGTKPSSDLPESSAVKDVPENSQNGIAKQTESGDR
Protein: DnaJ homolog subfamily C member 2 (Gliosarcoma-related antigen MIDA1) (Zuotin-related factor 1) (Q7TQ20)
Organism: Rattus norvegicus (Rat)
Function: Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99543}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99543}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 14
- Zinc finger protein ZPR1
- Heat shock 70 kDa protein 1-like
- Heat shock-related 70 kDa protein 2
- Heat shock 70 kDa protein 1A
- Heat shock cognate 71 kDa protein
- Stress-70 protein, mitochondrial
Sequence:
MLLLPSAAEGQGTAITHALTSASAVCQVEPVGRWFEAFVKRRNRNASTSFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKENFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKLCDRLELASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEKSTGGSGSGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVAPQADSAAPSERFEGPCIDSIPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMRRYKELVEMVKAKKAAQEQVLNASRARK
Protein: tRNA(Ile)-lysidine synthetase (EC 6.3.4.19) (F4J7P7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g49350
- TTF-type zinc finger protein with HAT dimerization domain-containing protein
- Cytoplasmic tRNA 2-thiolation protein 2
Sequence:
MARGLSLCSNGRKSSTLLSNSIPRVSISFSPKTLFTCSYPLQSRHPKFSQRLFCNHACVPETVDETRYKELFNKRMDMAGLKPHNRIALGVSGGPDSMALCVLTAKWKTEGLSCVNKTDGFIDGLVAIVVDHGLRQESKDEAELVCSRVSQMGIRCEIASCDWVDGRPKLGHLQEAAREMRYEMISNVCFRQQIEVLLIAHHADDQAELFILRLSRSSGVLGLAGTAFASEIFSRNLQLDAKHMKNQSIRLVRPLLDLWKEDMYKICQWGRQDWVEDPTNRSQLFVRNRIRTSIGNLESGSFKSELQAVISECRRTRSFVDKVCTDLIHQTVTVTDKGYAILDLERLNPSGVKDICLSKYLFAVLQFISQRQRPIRGNTSKLLLNYIRAIPCRTSLTAAGCYLSPAPGSKGTKIIVSCSVDCPLPSKTELLNISFNETPSDDLGQIIADAKSFSDHVAPTSLFEVQFLDVASESVLSKARELNLLSESTYTTIGLLQRDETKRFLTKTEEKSVELEHGTNIAASSDKVHLCLGQNLYFMNRFLIRWNLSDHQCNEADCRNCPVSTATSMEVRHMVEPDWLYLAELSKCSTSNHSISSSQKALRSLKLIPAAARKSLPVLVNHCGLLLCIPAIGFSYCSCLEASAVFLPRIPLGGGHSSFL
Protein: Mannosyltransferase (EC 2.4.1.-) (Q586R8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}.
Interaction partners:
- Mannosyltransferase
- Alpha-1,3-mannosyltransferase, putative
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MTVLSFFSFLFLLACVISVEIVCPYTKVEESFGMQAMHDFLLCGKRACFDHLSSPGVVPRTFTGPWFVASLAMLPFLCDVNYVVRFLLEPLKYVVAGDVAWFVRLVEDVGLVGSSEELFALFPMLASNMCRVTLGVVTCCALGYVGCGIDSAAKWEKFKSTSSRVAAARCPVSMRHVSSVFYLLCLSQFHLVFYATRPLPNTYGLIMCTLACGATCRGKYYWAIALLSATSALFRCDVLVLLAPYSLFLLLRGDITLLRGVAAGICSVAAVVIFSIGMDSYLWGRLVWPEAVVLLFNTAENQSWRWGRLPVYWYVLVALPRSLLFLYPLWLTLVCMGWGNIYFALHRLSGAGRREGTTSEEPSPAAAHCALWVFLDTSERYADLLVPSSLFIVLYSLLPHKEVRFLMIVFPWLLVPLAAAGTRLWDECFARPLSSCTLEVTKGKGIVQGRATLVKWRNEGANLRSRGDGKGGFNVRPRWFLACLTRRSVIASLIVLLYTVQLATVLLSVYLSADNYPGSEALRRLHHAVEKDVRNSSSCLSRRLTTRTNRSNSISVFIDAYAAMTGISRFQKVHKIQRRNPTNSTFATAGASQQVSDRFVKLLTFPFRALMSVGRSIVVGDTGLHDEELFGTGNVPSPAVVSGGDSSRTEVSDAFSLSILLQRRGLEMQYIKEEIRFDETNDLYNSEGIDYVISRYSQRELHRKHGEYNEIAVVHESNRLHMLKLRLMQLFWLRKRHEVADQADPEGKPFLIALGPRC