wanglab/gogpt-training-data huggingface dataset:
Protein: Histone-lysine N-methyltransferase, H3 lysine-79 specific (Q6XZL8)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037123, ECO:0000256|RuleBase:RU271113}.
Interaction partners:
- Protein AF-10
- Protein AF-9
- Btk-PH-domain binding protein translocated to, 1)
- Histone H3.1
- Histone H3.2
- Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 6
- NAD-dependent protein deacetylase sirtuin-1
- Histone-lysine N-methyltransferase 2A
- AF4/FMR2 family member 1
- Histone H3.3
Sequence:
MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSNGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRENKSNATTPTKVPESKAAATEAPADSGAEEEKSGVATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMSAASAERKSKKSQSTLDLLHSPPPAPPSASPQDAYRAPHSPFYQLPPSTQLHSPNPLLVAPTPPALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEADAGRLRLELDCAKISLPHLSSMSPELSMNGHAASYELCNAASRPSSKQNTPQYLASPLDQEVVPCTPSHSGRPRLEKLSGLALPDYTRLSPAKIVLRRHLSQDHTGASKAATSEPHPRPEHPKESSLPYQSPGLSNSMKLSPQDPPLASPATSPLTSEKGSEKGVKERAYSSHGETITSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSATLEKQTGASAHGAGGAGAGSRSLAVAPTGFYAGSVAISGALASSPAPLASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSPLNLNSMVSNINQPLEITAISSPESSLKSSPTPYQDHDQPPVLRKERPLGLTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFSPISDLGLAKAVDSPLQAGSALSHSPLFSFRPSLEEPAAEAKLPTHPRKSFAGSLGAAEGPSPGTNPPNGLAFSGGLAADLGLHSFNDGASLSHKGPDVTGLSASLSFPSQRGKDSTTEANPFLSRRQPEGLGGLKGEGNANKESGESLPLCGPSDKASLPHGSRASKGRDRELDFKGGHNLFISAAAVPPGGLLGGPGLVTVASSAGSATPTAQAPRPFLSTFAPGPQFTLGPMSLQANLGSVAGSSVLQSLFSTVPAAAGLVHVSSTATRLTNSHTMGSFSSGVAGGTVGGN
Protein: DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.38) (Deoxycytidine deaminase) (Q7YR24)
Organism: Pan troglodytes (Chimpanzee)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also against simian foamy virus (SFV). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. May inhibit the mobility of LTR retrotransposons.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9HC16}. Nucleus {ECO:0000250|UniProtKB:Q9HC16}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9HC16}. Note=Mainly cytoplasmic, small amount are found in the nucleus. {ECO:0000250|UniProtKB:Q9HC16}.
Interaction partners:
- single-stranded DNA cytosine deaminase
- single-stranded DNA cytosine deaminase
- Cullin-5
- Elongin-B
- Tripartite motif-containing protein 5
- Cytidine deaminase
- Core-binding factor subunit beta
- Cytochrome c1, heme protein, mitochondrial
- Elongin-C
- T-cell surface glycoprotein CD4
Sequence:
MKPHFRNPVERMYQDTFSDNFYNRPILSHRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSKLKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLHQDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLAKAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLEEHSQALSGRLRAILQNQGN
Protein: Probable arylsulfatase AtsB (Aryl-sulfate sulphohydrolase) (Sulfatase) (O65931)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- RNA pseudouridylate synthase
- Formylglycine-generating enzyme
- Phosphate-specific transport system accessory protein PhoU homolog 1
- Possible esterase lipoprotein LpqC
- Conserved hypothetical Mce associated alanine and valine rich protein
Sequence:
MMSEDNALVLVAGYQDLDSARHDFQTLVDAAKDKSIPLQGAVLIGKDAEGSPVLVDTGNRLGRRGAAWGAGVGLAIGLFSPALLASAALGAATGALAGTFAHHRIKTGLADKIGQALAAGRAVVIAVTEAQGRLEAGQALASSPMKSVAELSRSTLRSLGAALREAMGKFNPDRTRLPLPQRRFGGVVGRTMAESVGDWSIVPGPFPPDDAPNVLIVLIDDAGFGGPDTFGGAIRTPTLSRLAQNGLIYNRFHVTAVCSPTRAALLTGRNHHRVGFGSVCEFPGPYPGYSAVRPRSCAALPRILRDNGYVTGAFGKWHLTPDNVQGAAGPFDNWPLGWGFDHFWGFPSGAAGQYDPIISQDNSVIGIPEGSGEDGRPYYFPDDLTDKAIEWLHTVRAQNATKPWMLYYATGATHAPHHVFKEWADKYRGEFDDGWDVYRQKTFERQKRLGIIPPDAELTERPDLFPAWDSMSEAQKRLFARQMEVFAGFSENADWNVGRLLDAIEDLGESDNTLVFYIWGDNGASMEGTNTGSFNEMTFLNGLDLDAERQLELIEQYGGIAALGDEFTAPHFASAWAHASNTPLQWGKQMASHLGGTRDPLVVAWPARIRPDGRVRSQFTHCIDIAPTVLAAIGLPEPTHVDGFEQEPMDGTSFVRTFDDAEAEDRHTVQYFENFGSRAIYKDGWWACARLDKAPWDLSPETMRRFAPGTYDPDQDVWELYYLPDDFSQAKNLAAEHPDKVAELTQLWWQEAERNRVLPLLGGLAVMFGDLPPLPTTARFSFKGDVQNIQRGMVPRICGRSYAIEARLHIPDGGAQGVIVANADFMGGFALWVDEQRHLHHTYSFLGVETYRQVSSEPLPTGDVTVRMLFDSHQPVAASGGRVTLWADDRLIGEGELPQTVPLAFTSYAGMDIGRDNGLVVDRGYEDKAPYAFTGTVTEVIFDLKPVHPEAARALHEHASVQAVGQGAAG
Protein: 3'-5' exoribonuclease Rv2179c (EC 3.1.13.-) (P9WJ73)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Exonuclease that cleaves single-stranded 3' overhangs of double-stranded RNA. Has no activity with 5' overhangs. Has negligible endonuclease activity. Can bind ATP, dATP and AMP (in vitro); the nucleotide occupies the predicted substrate binding site.
Interaction partners:
- Probable conserved integral membrane protein
- Polyprenol-phosphate-mannose-dependent alpha-
- Phospho-2-dehydro-3-deoxyheptonate aldolase AroG
- PspA protein
- Intracellular chorismate mutase
- Uncharacterized protein Rv2468c
- Probable conserved secreted protein
- Uncharacterized protein Rv3412
- Possible conserved membrane protein
- GCN5-like protein acetyltransferase Rv2170
Sequence:
MRYFYDTEFIEDGHTIELISIGVVAEDGREYYAVSTEFDPERAGSWVRTHVLPKLPPPASQLWRSRQQIRLDLEEFLRIDGTDSIELWAWVGAYDHVALCQLWGPMTALPPTVPRFTRELRQLWEDRGCPRMPPRPRDVHDALVDARDQLRRFRLITSTDDAGRGAAR
Protein: Phenylalanine ammonia-lyase (EC 4.3.1.24) (B2J528)
Organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Function: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Histidinol-phosphate aminotransferase
- Histidinol-phosphate aminotransferase
- Aminotransferase
- Imidazoleglycerol-phosphate dehydratase
- Prephenate dehydratase
- Arginase/agmatinase/formiminoglutamase
- Glycoside hydrolase family 42 N-terminal domain-containing protein
Sequence:
MNITSLQQNITRSWQIPFTNSSDSIVTVGDRNLTIDEVVNVARHGTQVRLTDNADVIRGVQASCDYINNAVETAQPIYGVTSGFGGMADVVISREQAAELQTNLIWFLKSGAGNKLSLADVRAAMLLRANSHLYGASGIRLELIQRIETFLNAGVTPHVYEFGSIGASGDLVPLSYITGALIGLDPSFTVDFDGKEMDAVTALSRLGLPKLQLQPKEGLAMMNGTSVMTGIAANCVYDAKVLLALTMGVHALAIQGLYGTNQSFHPFIHQCKPHPGQLWTADQMFSLLKDSSLVREELDGKHEYRGKDLIQDRYSLRCLAQFIGPIVDGVSEITKQIEVEMNSVTDNPLIDVENQVSYHGGNFLGQYVGVTMDRLRYYIGLLAKHIDVQIALLVSPEFSNGLPPSLVGNSDRKVNMGLKGLQISGNSIMPLLSFYGNSLADRFPTHAEQFNQNINSQGYISANLTRRSVDIFQNYMAIALMFGVQAVDLRTYKMKGHYDARTCLSPNTVQLYTAVCEVVGKPLTSVRPYIWNDNEQCLDEHIARISADIAGGGLIVQAVEHIFSSLKST
Protein: Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G (EC 7.2.1.2) (Rnf electron transport complex subunit G) (H6LC30)
Organism: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with electrogenic movement of Na(+) out of the cell. Involved in caffeate respiration.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000269|PubMed:19222539}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00479}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- Ion-translocating oxidoreductase complex subunit C
- Propanediol utilization protein PduS
- Pyruvate:ferredoxin oxidoreductase
- Hydrogenase large subunit-like protein
- 5,10-methylene-THF reductase small subunit MetV
Sequence:
METKEKVQIDWKVVFKLGLILFVISAVAACALALTNYVTAGTIEEMNVQTNTVARQEVLPKAADFEAVPAKDVEKIASEIGMEKPEELLEVYIGKSNGEVVGYTVKTGPTSGYAGEVQVLTGISADGVITGITIIKSNETPGLGAKASGVWNDQFTGKSAKEELVVVKGTTKEGSNEIQAITGSTITSKAVTSGVNMSIQVYQNLSK
Protein: Galanin peptides [Cleaved into: Galanin; Galanin message-associated peptide (GMAP)] (P10683)
Organism: Rattus norvegicus (Rat)
Function: Endocrine hormone of the central and peripheral nervous systems that binds and activates the G protein-coupled receptors GALR1, GALR2, and GALR3. This small neuropeptide may regulate diverse physiologic functions including contraction of smooth muscle of the gastrointestinal and genitourinary tract, growth hormone and insulin release and adrenal secretion.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P07480, ECO:0000250|UniProtKB:P22466}.
Interaction partners:
- Galanin receptor type 1
- Galanin receptor type 3
- Galanin receptor type 2
- Pro-neuropeptide Y
- Protachykinin-1
- Somatostatin
- Oxytocin-neurophysin 1
- Neurotensin/neuromedin N
- Galectin-2
- Cholecystokinin
Sequence:
MARGSVILLAWLLLVATLSATLGLGMPTKEKRGWTLNSAGYLLGPHAIDNHRSFSDKHGLTGKRELPLEVEEGRLGSVAVPLPESNIVRTIMEFLSFLHLKEAGALDSLPGIPLATSSEDLEQS
Protein: Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratase) (P0A9G6)
Organism: Escherichia coli (strain K12)
Function: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
Interaction partners:
- Malate synthase A
- Malate synthase G
- Isocitrate dehydrogenase kinase/phosphatase
- Aconitate hydratase B
- Glyoxylate/hydroxypyruvate reductase A
- Aconitate hydratase A
- Glyoxylate/hydroxypyruvate reductase B
- Glyoxylate carboligase
- Citrate synthase
- KHG/KDPG aldolase
Sequence:
MKTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAAKMWRLLHGESKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANLAASMYPDQSLYPANSVPAVVERINNTFRRADQIQWSAGIEPGDPRYVDYFLPIVADAEAGFGGVLNAFELMKAMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVTGVPTLLVARTDADAADLITSDCDPYDSEFITGERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARRFAQAIHAKYPGKLLAYNCSPSFNWQKNLDDKTIASFQQQLSDMGYKFQFITLAGIHSMWFNMFDLANAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVTTIIQGGTSSVTALTGSTEESQF
Protein: Calmodulin-6 (CaM-6) (Q03509)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Interaction partners:
- Mitogen-activated protein kinase 8
- Plasma membrane-associated cation-binding protein 1
- Kinesin-like protein KIN-14E
- Calmodulin-binding transcription activator 3
- Two pore calcium channel protein 1
- CDPK-related kinase 1
- Calreticulin-1
- ATMYB2
- Calreticulin-2
- Heat shock 70 kDa protein 4
Sequence:
MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLSDEEVDEMIREADVDGDGQINYEEFVKVMMAK
Protein: Zinc finger protein 32 (C2H2-546) (Zinc finger protein KOX30) (P17041)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein FRA10AC1
Sequence:
MFGFPTATLLDCHGRYAQNVAFFNVMTEAHHKYDHSEATGSSSWDIQNSFRREKLEQKSPDSKTLQEDSPGVRQRVYECQECGKSFRQKGSLTLHERIHTGQKPFECTHCGKSFRAKGNLVTHQRIHTGEKPYQCKECGKSFSQRGSLAVHERLHTGQKPYECAICQRSFRNQSNLAVHRRVHSGEKPYRCDQCGKAFSQKGSLIVHIRVHTGLKPYACTQCRKSFHTRGNCILHGKIHTGETPYLCGQCGKSFTQRGSLAVHQRSCSQRLTL
Protein: Keratin, type II cytoskeletal 79 (Cytokeratin-79) (CK-79) (Keratin-6-like) (Keratin-6L) (Keratin-79) (K79) (Type-II keratin Kb38) (Q5XKE5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSSVSRQTYSTKGGFSSNSASGGSGSQARTSFSSVTVSRSSGSGGGAHCGPGTGGFGSRSLYNLGGHKSISVSVAGGALLGRALGGFGFGSRAFMGQGAGRQTFGPACPPGGIQEVTVNQSLLTPLHVEIDPEIQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGQNLGVTRNNLEPLFEAYLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAYMGRMDLHGKVGTLTQEIDFLQQLYEMELSQVQTHVSNTNVVLSMDNNRNLDLDSIIAEVKAQYELIAQRSRAEAEAWYQTKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLESEESRMSGECPSAVSISVTGNSTTVCGGGAASFGGGISLGGSGGATKGGFSTNVGYSTVKGGPVSAGTSILRKTTTVKTSSQRY
Protein: Type 1 phosphatases regulator YPI1 (Q59ZW4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Type 1 protein phosphatase-activating protein
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Protein phosphatase regulator
Sequence:
MSQQRENQRGIVSQTTTTTASPILKLRAQERQARDVSWDANVVDNEHLNKKKTKICCIFHPSDRNCDEEDSSSSSDSSSDSSDNEEDDKNTKIAPKSNNNKKKSKPNAYEVQPHYKNQSKVPGK
Protein: RNA-binding protein, putative (Q584Q1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C3H1-type domain-containing protein
- Small nuclear ribonucleoprotein E
- Sm protein G
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Small nuclear ribonucleoprotein Sm D2
- Sm protein F
- Small nuclear ribonucleoprotein SmD1
- Sm protein B
- RNA-binding protein, putative
- U2 small nuclear ribonucleoprotein B, putative
Sequence:
MPPGFKAPPMPPGFKMPPRPPMPPGFKMPPGGPRPPGPPMPPHAQQGSYPNYPTPPGAPPMPPGGRYAPAPPRPPSGGSDQENGQGYMMHSGAVHGQYDAYAREDYNYGVPPGPDSRGYSSYHPSQQYHQGYYGAPAAHGGENRGNRRDEEAREPTNTVWVGNLDVQRHSDDFLRQEFREFGRVVRIAKVPDKSYCFVHFRYVEEARNAVETLSARGSLGGARFSYGKMFDYSQDEGGMQQDGGMSNQGMRPPRRPREEERHEHEERRRRPRRDEEPMEPTNVLWIGDLPPTITNEELNENFKVFGTILNISRLDCKNMAFIHFENIESCTQALDLMRDQLICGARVALNYGRAQRNPVSQTTGLSPDGIPLSETPTNVIFVGQFATDVTEEDIEALFEPFEGFINSKFIHSSCIAFGHFDTVDHARAARVALNNTLLKGAPARISFGKTNHTLTMADRMRRGRPAPLVDGVEVIPETAAGAPGRGSLDGVSGALVAGPGLSGASENGAVVMIPAMGAAVTATSPPQAHASFTRERPAPDMTLDARLQSLLGATYNSCGEAEKSLSPSVIQTICDLIDDCVDEGSEKRLDDAIFLYTPLNSAHVFGILAKRMQSFFNDDPHKKLYIAYAATRVLLAAKTDYVFFTKAAMNAYLMVLFVTSQGQTPDGMEQLVAIIESVRRHPFIEKQRLDAEYTEIFRGQLEEILGRAKEEQDLTSLITKKRRR
Protein: Periostin (A0A0G2K692)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MVPLLPLSALLLLFLCDVDPANANSYYDKVLAHSRIRGRDQGPNVCALQQILGTKKKYFSSCKNWYQGAICGKKTTVLYECCPGYMRMEGMKGCPAVMPIDHVYGTLGIVGATTTQHYSDVSKLREEIEGKGSYTYFAPSNEAWDNLDSDIRRGLENNVNVELLNALHSHMVNKRMLTKDLKHGMVIPSMYNNLGLFINHYPNGVVTVNCARVIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDELSSFRAAAITSDLLESLGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSEAITGGAVFETMEGNTIEIGCEGDSISINGIKMVNKKDIVTKNGVIHLIDEVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASSLKPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLSDLYNGQILETIGGKQLRVFVYRTAICIENSCMVRGSKQGRNGAIHIFREIIQPAEKSLHEKLRQDKRFSIFLSLLEAADLKDLLTQPGDWTLFAPTNDAFKGMTNEEREILIGDKNALQNIILYHLTPGVYIGKGFEPGVTNILKTTQGSKIYVKGVNETLLVNELKSKESDIMTTNGVIHVVDKLLYPADIPVGNDQLLELLNKLIKYIQIKFVRGSTFKEIPMTVYRPAMTKIHIEGEPDFRLIKEGETVTEVIHGEPVIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLQKFLQKEVSKVTKFIEGGDGHLFEDEAIKRLLQGDTPAKKIQANKRVQGSRRRSREGRSQ
Protein: Protein Tat (Transactivating regulatory protein) (P04608)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:19888548}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:19888548, ECO:0000269|PubMed:23501106}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079, ECO:0000269|PubMed:19888548}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type.
Interaction partners:
Sequence:
MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE
Protein: ADP-ribosylation factor GTPase-activating protein GCS1 (ARF GAP GCS1) (P35197)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11839779}. Mitochondrion {ECO:0000269|PubMed:11839779}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839779}. Golgi apparatus {ECO:0000305|PubMed:11839779}. Note=Found also in the mitochondria and in the perinuclear region.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor-like protein 1
- ADP-ribosylation factor 2
- ARF guanine-nucleotide exchange factor 2
- ADP-ribosylation factor GTPase-activating protein GLO3
- ADP-ribosylation factor 3
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- ARF guanine-nucleotide exchange factor 1
- ADP-ribosylation factor GTPase-activating protein effector protein 2
- Protein transport protein SEC22
Sequence:
MSDWKVDPDTRRRLLQLQKIGANKKCMDCGAPNPQWATPKFGAFICLECAGIHRGLGVHISFVRSITMDQFKPEELLRMEKGGNEPLTEWFKSHNIDLSLPQKVKYDNPVAEDYKEKLTCLCEDRVFEEREHLDFDASKLSATSQTAASATPGVAQSREGTPLENRRSATPANSSNGANFQKEKNEAYFAELGKKNQSRPDHLPPSQGGKYQGFGSTPAKPPQERSAGSSNTLSLENFQADPLGTLSRGWGLFSSAVTKSFEDVNETVIKPHVQQWQSGELSEETKRAAAQFGQKFQETSSYGFQAFSNFTKNFNGNAEDSSTAGNTTHTEYQKIDNNDKKNEQDEDKWDDF
Protein: Sodium-dependent phosphate transport protein 1, chloroplastic (Anion transporter 1) (Na(+)/PI cotransporter 1) (Phosphate transporter PHT4;1) (Sodium/phosphate cotransporter 1) (O82390)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specific for inorganic phosphate transport across the thylakoid membrane in a sodium dependent manner. Binds glutamate but cannot transport it. May act as an ascorbate transporter at the thylakoid membrane (Probable).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780}; Multi-pass membrane protein {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780}.
Interaction partners:
- Inorganic phosphate transporter 2-1, chloroplastic
- Inorganic phosphate transporter 1-4
- Nucleotide-sugar transporter family protein
- Thylakoid ADP,ATP carrier protein, chloroplastic
- Probable sodium/metabolite cotransporter BASS4, chloroplastic
- K
Sequence:
MNARALLCSSNIHSLYTSNRPPEKTSSSRSLRNLKPSPKSLRVWIYPRNRSSVFRVLVRSSDKSESSNSYYVEGDKVSGNNDVVSDSPSSIVLPWWEEFPKRWVIVLLCFSAFLLCNMDRVNMSIAILPMSAEYGWNPATVGLIQSSFFWGYLLTQIAGGIWADTVGGKRVLGFGVIWWSIATILTPVAAKLGLPYLLVVRAFMGVGEGVAMPAMNNILSKWVPVQERSRSLALVYSGMYLGSVTGLAFSPFLIHQFGWPSVFYSFGSLGTVWLTLWLTKAESSPLEDPTLLPEERKLIADNCASKEPVKSIPWRLILSKPPVWALISCHFCHNWGTFILLTWMPTYYHQVLKFNLMESGLLSVFPWMTMAISANAGGWIADTLVSRGFSVTNVRKIMQTIGFLGPAFFLTQLKHIDSPTMAVLCMACSQGTDAFSQSGLYSNHQDIAPRYSGVLLGLSNTAGVLAGVLGTAATGHILQHGSWDDVFTISVGLYLVGTVIWNLFSTGEKIID
Protein: Small ribosomal subunit protein eS32A (60S ribosomal protein L41-A) (Large ribosomal subunit protein eL41A) (P0CT81)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytochrome c oxidase subunit 4, mitochondrial
- Septin homolog spn3
Sequence:
MRDKWRKKRVRRLKRKRRKMRARSK
Protein: EH domain binding protein 1, isoform CRA_a (Testis tissue sperm-binding protein Li 50e) (A0A140VK17)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASVWKRLQRVGKHASKFQFVASYQELMVECTKKWQPDKLVVVWTRRSRRKSSKAHSWQPGIKNPYRGVVVWPVPENIEITVTLFKDPHAEEFEDKEWTFVIENESPSGRRKALATSSINMKQYASPMPTQTDVKLKFKPLSKKVVSAALQFSLSCIFLREGKATDEDMQSLASLMSMKQADIGNLDDFEEDNEDDDENRVNQEEKAAKITELINKLNFLDEAEKDLATVNSNPFDDPDAAELNPFGDPDSEEPITETASPRKTEDSFYNNSYNPFKEVQTPQYLNPFDEPEAFVTIKDSPPQSTKRKNIRPVDMSKYLYADSSKTEEEELDESNPFYEPKSTPPPNNLVNPVQELETERRVKRKAPAPPVLSPKTGVLNENTVSAGKDLSTSPKPSPIPSPVLGRKPNASQSLLVWCKEVTKNYRGVKITNFTTSWRNGLSFCAILHHFRPDLIDYKSLNPQDIKENNKKAYDGFASIGISRLLEPSDMVLLAIPDKLTVMTYLYQIRAHFSGQELNVVQIEENSSKSTYKVGNYETDTNSSVDQEKFYAELSDLKREPELQQPISGAVDFLSQDDSVFVNDSGVGESESEHQTPDDHLSPSTASPYCRRTKSDTEPQKSQQSSGRTSGSDDPGICSNTDSTQAQVLLGKKRLLKAETLELSDLYVSDKKKDMSPPFICEETDEQKLQTLDIGSNLEKEKLENSRSLECRSDPESPIKKTSLSPTSKLGYSYSRDLDLAKKKHASLRQTESDPDADRTTLNHADHSSKIVQHRLLSRQEELKERARVLLEQARRDAALKAGNKHNTNTATPFCNRQLSDQQDEERRRQLRERARQLIAEARSGVKMSELPSYGEMAAEKLKERSKASGDENDNIEIDTNEEIPEGFVVGGGDELTNLENDLDTPEQNSKLVDLKLKKLLEVQPQVANSPSSAAQKAVTESSEQDMKSGTEDLRTERLQKTTERFRNPVVFSKDSTVRKTQLQSFSQYIENRPEMKRQRSIQEDTKKGNEEKAAITETQRKPSEDEVLNKGFKDTSQYVVGELAALENEQKQIDTRAALVEKRLRYLMDTGRNTEEEEAMMQEWFMLVNKKNALIRRMNQLSLLEKEHDLERRYELLNRELRAMLAIEDWQKTEAQKRREQLLLDELVALVNKRDALVRDLDAQEKQAEEEDEHLERTLEQNKGKMAKKEEKCVLQ