wanglab/gogpt-training-data huggingface dataset:
Protein: Condensin complex subunit 1 (XCAP-D2 homolog) (Q06156)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.
Subcellular location: Nucleus {ECO:0000269|PubMed:11854418}. Chromosome {ECO:0000269|PubMed:11854418}. Note=Nuclear throughout the cell cycle. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. At anaphase, it is enriched at rDNA. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 3
- Structural maintenance of chromosomes protein 2
- Condensin complex subunit 2
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- DNA polymerase alpha catalytic subunit A
- Sister chromatid cohesion protein PDS5
Sequence:
MSGFSLSEYLTKFQTTDRESYPRLQDPSRELNVIIDQLAVSPEQIDASPDSLEALIDLCHDFPHLTPKLQTQLSYLISSSLSNLSKDIKANLSSNVNFTEIGGLIPQWKRHLEEYGYLIQVLLTFLQDELHKVSSQSTNLNRSAKNSKNDSANVELFKRDCNQMENLLESITKLLEINLSKIFQTTPEKDLFIGLFTRPLFVLLEIEPVTKVSSLKMFIQRILAMCVKNHGQSSSIQSSLMTNLTYFLHLSVFNAELLKLLNDEYNYPQLTEDILKEISTRVFNAKDTTGPKAISNFLIKLSELSPGIMLRQMNLVITLLNNSSITLRCSVVEACGNIVAELAQDPQTMEHYKQQIAVLIELLEERFQDSNPYVRTKAIQGCSKICDLSSKFNKSKAKFTSLAVRSLQDRSSLVRRNSVKLLSKLLLKHPFKAIHGSQLRLSEWEEYLKGSESQLNSTLKKVESQETLNDTIERSLIEEEVEQDEGQCRTELEGSFNKSAELSRIENEVENINATNTSVLMKLKLMIVYYKDAISFIKEIHKSIELISNLLFSKNRNEVLESMDFLVLADAFDIELSEFGIKKMLHLVWMKGTNDEGTSISVHLIECYKQLFLTAPDSCNMQEKAAHIAKNLINLSIGASIADLASLEQLLGMMYEQKLIDQHVINILWAIYNSASKASMQKEQNVNNRDSEKGFSKEQIHGSIIILGMLSLADNEIALKGLESLLNIGLGAVGLKDLTLCRYSCLALERMVPKRSTIITKAINQELEDVAVKKLYAIIINYTKDNEYYPMCEQALSALFTISSKPDILATDLIREKTMMTFGKPEEEDSILSLEQSSRVVSLSQLLFIVGQVAIKTLVYLEKCEAEFKKRKIEAETRNGKVKNQGADVTNTTQDNGGDKELEMIGGTNEDDFTDAIQFVKENELLFGEKSILGKFCPIVEEIVSNSSRFSDPMLQRTATLCLEKLMCLSSKYCEKSLPLLITVMEKSPDPTIRSNAVLGLGDMAVCFNNLVDENTDYLYRRLHDENLMVQRTCLMTVTFLILAGQVKVKGQLGEMAKCLDNPDQGISDMCRLFFTELASKDNAIYNGFIDIFSNLSSDDLLGKESFKKIIKFLLTFIDKERHQKQLNEKLVGRLRKCETQKQWDDIAFVLNNLPYKNEDVTALLEQGFKVVSAKE
Protein: ER lumen protein-retaining receptor 1 (KDEL endoplasmic reticulum protein retention receptor 1) (KDEL receptor 1) (Q99JH8)
Organism: Mus musculus (Mouse)
Function: Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. {ECO:0000250|UniProtKB:P33946}.
Interaction partners:
- Coatomer subunit beta
- Transmembrane emp24 domain-containing protein 10
- Coatomer subunit delta
Sequence:
MNLFRFLGDLSHLLAIILLLLKIWKSRSCAGISGKSQVLFAVVFTARYLDLFTNYISLYNTCMKVVYIACSFTTVWMIYSKFKATYDGNHDTFRVEFLVVPTAILAFLVNHDFTPLEILWTFSIYLESVAILPQLFMVSKTGEAETITSHYLFALGVYRTLYLFNWIWRYHFEGFFDLIAIVAGLVQTVLYCDFFYLYITKVLKGKKLSLPA
Protein: DEAD-box ATP-dependent RNA helicase CshB (EC 3.6.4.13) (P54475)
Organism: Bacillus subtilis (strain 168)
Function: DEAD-box RNA helicase that plays a role in 70S ribosome assembly. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:16352840, ECO:0000269|PubMed:20572937}. Note=Shows transcription-dependent localization at subcellular sites surrounding the nucleoid.
Interaction partners:
- Probable endonuclease 4
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease Y
- Elongation factor G
- Peptidyl-prolyl cis-trans isomerase B
- Large ribosomal subunit protein uL3
- Uncharacterized protein YqeH
- Large ribosomal subunit protein uL13
- Polyketide synthase PksJ
- Large ribosomal subunit protein uL24
Sequence:
MKETKFELYELKPFIIDAVHRLGFYEPTDIQKRLIPAVLKKESVIGQSQTGTGKTHAYLLPLLNKIDPAKDVVQVVITAPTRELANQIYQEALKITQGEEGSQIRSKCFIGGTDKQKSIDKLKIQPHLVVGTPGRIADLIKEQALSVHKAESLVIDEADLMLDMGFLADVDYIGSRMPEDLQMLVFSATIPEKLKPFLKKYMENPKYAHVEPKQVTAAKIEHILIPSKHRDKDKLLFDIMSHLNPYLGIVFANTKNTADHIAQYLTGKGMKIGLLHGGLTPRERKKVMKQINDLEFTYIIATDLAARGIDIKGVSHVINYELPDDLDFYVHRVGRTARAGSSGQAMTIYELTDEDALVRLEKMGIEFEYLELEKGEWKKGDDRQRRKKRKKTPNEADEIAHRLVKKPKKVKPGYKKKMSYEMEKIKKKQRRNQSKKRK
Protein: Putative adenosylhomocysteinase 3 (AdoHcyase 3) (EC 3.13.2.1) (Long-IRBIT) (S-adenosyl-L-homocysteine hydrolase 3) (S-adenosylhomocysteine hydrolase-like protein 2) (Q68FL4)
Organism: Mus musculus (Mouse)
Function: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A6QLP2, ECO:0000269|PubMed:19220705}. Microsome {ECO:0000269|PubMed:19220705}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000269|PubMed:19220705}.
Interaction partners:
- Cystathionine beta-synthase
- Betaine--homocysteine S-methyltransferase 1
- Methionine synthase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- S-adenosylhomocysteine hydrolase-like protein 1
- DNA
- Adenosylhomocysteinase
- DNA
- DNA
- Kynurenine--oxoglutarate transaminase 3
Sequence:
MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSAAAVGAMVPPAGGGDPEAPAPAPAAERPPAPGPGSGPTAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY
Protein: Granny smith, isoform F (EC 3.4.-.-) (A0A0C4FEI8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPYPNGFLSYAVAIHLKSPHLQMEESLRQGAGYWNALSSREKNQYRSKYQKRCLSKSSTSRHRRQSEKLKHMGCGRKKIVPKCSRKPTTPACKPRSVNRCPRKSSSNRSSRECMLMKSPKGMATDVKFNESLGCSDPQTHPVLIIGQLRHLNLLKFSHLESKLSPRVTEETFLNAVACLHPAPTDKVSLYLDVATVAALPLKASRHNTASRAHAITRLVKNHVLNVSEESVVLVCERENLFASACAVVRAFPLYSRKTGNLLASSQPKLNLGCGDGNANSGRNVVNVEFVLINKDGCIESEPLTDDELNCLNETTRAIRMTARIVDMPCNEMNVDHFIQEVEDVGRELCITPKVIRGEELLEQGFGGIYGVGKAAAVPPALVVLSHEPKGAQETIALVGKGIVYDTGGLSIKAKTGMPGMKRDCGGAAAILGTFYAAVQCGFRDNLHAVFCLAENSVGPNATRPDDIHTLYSGRTVEINNTDAEGRLVLADGVCYANKDLKANIILDMATLTGAQGVATGKYHGAILTNSETWEAKSLQAGRKSGDLLAPIIYCPELHFSEFASAIADMKNSVADRQNAQSSCAGLFIAAHLGFDYPGIWMHVDMATPVHCGERATGYGVSLLLTLFGGHTDSKLLQSIASTDEEPPSKRWCRD
Protein: Pentatricopeptide repeat-containing protein At5g64320, mitochondrial (Q9FMF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Presenilin-like protein At2g29900
Sequence:
MVMLARSKLALDVSRRSQSLQRICYYASLSSRFSGGGGDDGGGSSPEIGGTDSANEWEKLLKPFDLDSLRNSFHKITPFQLYKLLELPLNVSTSMELFSWTGSQNGYRHSFDVYQVLIGKLGANGEFKTIDRLLIQMKDEGIVFKESLFISIMRDYDKAGFPGQTTRLMLEMRNVYSCEPTFKSYNVVLEILVSGNCHKVAANVFYDMLSRKIPPTLFTFGVVMKAFCAVNEIDSALSLLRDMTKHGCVPNSVIYQTLIHSLSKCNRVNEALQLLEEMFLMGCVPDAETFNDVILGLCKFDRINEAAKMVNRMLIRGFAPDDITYGYLMNGLCKIGRVDAAKDLFYRIPKPEIVIFNTLIHGFVTHGRLDDAKAVLSDMVTSYGIVPDVCTYNSLIYGYWKEGLVGLALEVLHDMRNKGCKPNVYSYTILVDGFCKLGKIDEAYNVLNEMSADGLKPNTVGFNCLISAFCKEHRIPEAVEIFREMPRKGCKPDVYTFNSLISGLCEVDEIKHALWLLRDMISEGVVANTVTYNTLINAFLRRGEIKEARKLVNEMVFQGSPLDEITYNSLIKGLCRAGEVDKARSLFEKMLRDGHAPSNISCNILINGLCRSGMVEEAVEFQKEMVLRGSTPDIVTFNSLINGLCRAGRIEDGLTMFRKLQAEGIPPDTVTFNTLMSWLCKGGFVYDACLLLDEGIEDGFVPNHRTWSILLQSIIPQETLDRRRFYNAAF
Protein: Inner kinetochore subunit mis15 (CENP-N homolog) (Constitutive centromere-associated network protein mis15) (Sim4 complex subunit mis15) (Q9C0W0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. Has a role in the formation and/or maintenance of specialized chromatin at the centromere.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Inner kinetochore subunit mis17
- Inner kinetochore subunit mal2
- Inner kinetochore subunit mis6
- Kinetochore protein mis14
- Kinetochore protein mis13
- Inner kinetochore subunit fta1
- Inner kinetochore subunit fta4
- Inner kinetochore subunit fta3
- Inner kinetochore subunit fta2
- Inner kinetochore subunit fta6
Sequence:
MRTELSSNIRIKHDKKIQKLLNRFPRDFLVKLCVEWIQKQTYPPNAKDINLEDMLDDEEWNPEAFYKNVPKSMLKRSIIHRMLVYDWPNGFYLGQIAQLEILALAHGFVSMRWTASKVHHSAEKTVLPNPLVFLELLKSELESIFVYHTYISRHETLPITFIRLVLWDSKRPTALHTYPSSKQIFYLGLMDDSDVLLHNIFLRNDVCHSLFLQCLSRLLYRLKAGSALRPIDLVSKNLTTFCTNVGVNKEANALGAWQIYAKNLVDRSPLDTRPILSDDNSSLIADSTQNCEKHREMAIQRRFGDTHSQVLDKLLITLDHDYIEKSTEKDKVLEENVESYNPTEQRPLVVMQLRGQHILEGLKDICRQDALDPFTMPSYLTGETGLSILYVRDGLVLQRQESLGQQEIN
Protein: Mitochondrial RNA-binding protein RBP38 (Q86PT1)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MFRRLTQYTGVVGAVRTIVVFSQQHHILESNQKARSSPSNVWIEDWEAESYGLTPEPGAVSTQLLLDKPLELYNFDQLLSPPEVMEAPKHSSYSSRKVYGEKLQFELNDRAQKHGFHSKWWLTRTQAVKNALTFKNNARSSIILSKSSLRLYHSSQLVGGEALMTHPVSGGSRKLYSRKGDAYQVLCEHIRQNAFNSGLYFTRRQLEFFKLAVQPSQAPVMMDVSSGERFLIFNVEQLEDPEVALRTLDRSPVSIPTFLLSGEPMQHEGVKRLPRFKSNYWLSGRDAELYQWPIKESEKKRGVTLKNEGSASLQVELFNVEQLANPEEAFAKAGLFVQ
Protein: Sensor protein QseC (EC 2.7.13.3) (P40719)
Organism: Escherichia coli (strain K12)
Function: Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Transcriptional regulatory protein QseB
- KDP operon transcriptional regulatory protein KdpE
- Transcriptional regulatory protein GlrR
- Transcriptional regulatory protein BasR
- Protein YgiW
- HTH-type transcriptional activator AaeR
- Aerobic respiration control sensor protein ArcB
- Transcriptional regulatory protein PhoP
- HTH-type DNA-binding transcriptional activator EutR
- Phosphate regulon transcriptional regulatory protein PhoB
Sequence:
MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNRLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGEDDPWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSSVMDIYHTAQQAKIDVRLTLNAHSIKRTGQPLLLSLLVRNLLDNAVRYSPQGSVVDVTLNADNFIVRDNGPGVTPEALARIGERFYRPPGQTATGSGLGLSIVQRIAKLHGMNVEFGNAEQGGFEAKVSW
Protein: Uncharacterized protein (Q384P7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWHSFLRLNPLSPLLMRCHHRHHRTALAGFSGCGIASSALQNPLRACMCTLSQHSGETTDSCGDVHSSAVGATVSSKSVRMTCDLHGTSSTQTQVEEMSGESMDLKRMLFSLKDHNTGVVTCLDVEERLRNVELLDEWCVRKLFRDSGWVSKVQEEGETAPQYRNIIGEHRILRNMLERFVSNRAMWHDELIELLQLVLKRGAEVQESKDLLDVGFRNGEKHPVTHHNFTPNRVHSRCSRAVVECCHNGVVAFDAAMIWNSLRRISDSSCFYSYGLQGVLWEFLHYGSNSSGDPRELWHMFVAFYRNMRVAPSTKRPLFSSHDMIITLTETEFQEDTRESVMAGVMGENELTENVVDGVSLNWPEGWKAKDPTHLSEEGFPADCKRRTNCNARHQRYLTDTFYINMIEPSEVLTGCHNSCGSEISTEELEQEKGRAATGGWWRGEERNVINPMNGELEDIHLTQLWHLFQNMRIDEIVDVYRTVCGGFGALQAEVYVDIMTRRALLMLFFARDEVRAITPPPVTYQRLSSLHNELLCLSSWCLASPQRNSFLVAPPRPFEELPLQDQLSYSCFGQLHAPRMPRRFCLPKSAATPEELYRWYCEMYPLFSSSCDSRVAAEVLDSNQKDSCNSSAVGTSCTWPRFEWLNELQQSSLRFPFGDSVYFQSTSYSTPDTTEPLAMTGTRPSTSNEATGDASGARTESSREAHKRRTRHRKNRGSSTPHKEVRRITSDGESSHKSAEFAAGDTPSEEPAVLKNVSRQREHFKGAKKTSKTKEKHHHRRSSDKLRTEDVQRSADEGKPEEPRLTGGEPMRRARPRGSKKKQSAKGKHHRGSVDGISKRQSVTTNEVSKRKKGPKGTKSTPKTYEEVWYPTPDSKASGEGTQLIPDAETNEEVESTKKVAIRRTHPKREKKDSHNVLKGRRYATAESESSREKIRSDTNDEANGDVAPVDTEPKRRGRPKKSGGIVGAQVEV
Protein: Anoctamin-10 (Transmembrane protein 16K) (Q9NW15)
Organism: Homo sapiens (Human)
Function: Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane.
Interaction partners:
Sequence:
MKVTLSALDTSESSFTPLVVIELAQDVKEETKEWLKNRIIAKKKDGGAQLLFRPLLNKYEQETLENQNLYLVGASKIRMLLGAEAVGLVKECNDNTMRAFTYRTRQNFKGFDDNNDDFLTMAECQFIIKHELENLRAKDEKMIPGYPQAKLYPGKSLLRRLLTSGIVIQVFPLHDSEALKKLEDTWYTRFALKYQPIDSIRGYFGETIALYFGFLEYFTFALIPMAVIGLPYYLFVWEDYDKYVIFASFNLIWSTVILELWKRGCANMTYRWGTLLMKRKFEEPRPGFHGVLGINSITGKEEPLYPSYKRQLRIYLVSLPFVCLCLYFSLYVMMIYFDMEVWALGLHENSGSEWTSVLLYVPSIIYAIVIEIMNRLYRYAAEFLTSWENHRLESAYQNHLILKVLVFNFLNCFASLFYIAFVLKDMKLLRQSLATLLITSQILNQIMESFLPYWLQRKHGVRVKRKVQALKADIDATLYEQVILEKEMGTYLGTFDDYLELFLQFGYVSLFSCVYPLAAAFAVLNNFTEVNSDALKMCRVFKRPFSEPSANIGVWQLAFETMSVISVVTNCALIGMSPQVNAVFPESKADLILIVVAVEHALLALKFILAFAIPDKPRHIQMKLARLEFESLEALKQQQMKLVTENLKEEPMESGKEKAT
Protein: Protein arginine N-methyltransferase 7 (EC 2.1.1.321) (Histone-arginine N-methyltransferase PRMT7) ([Myelin basic protein]-arginine N-methyltransferase PRMT7) (Q9NVM4)
Organism: Homo sapiens (Human)
Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15494416}. Nucleus {ECO:0000269|PubMed:15494416}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Transcriptional repressor CTCFL
- Methylosome protein WDR77
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2 subunit 2
- Histone H4
- rRNA 2'-O-methyltransferase fibrillarin
- Histone H4-like protein type G
Sequence:
MKIFCSRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNVKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPEGDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVESGRMWSWNKLFPIHVQTSLGEQVIVPPVDVESCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSIDFSKQVSSSAACHSRRFEPLTSGRAQVVLSWWDIEMDPEGKIKCTMAPFWAHSDPEEMQWRDHWMQCVYFLPQEEPVVQGSALYLVAHHDDYCVWYSLQRTSPEKNERVRQMRPVCDCQAHLLWNRPRFGEINDQDRTDRYVQALRTVLKPDSVCLCVSDGSLLSVLAHHLGVEQVFTVESSAASHKLLRKIFKANHLEDKINIIEKRPELLTNEDLQGRKVSLLLGEPFFTTSLLPWHNLYFWYVRTAVDQHLGPGAMVMPQAASLHAVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPLWEYPCRSLSEPWQILTFDFQQPVPLQPLCAEGTVELRRPGQSHAAVLWMEYHLTPECTLSTGLLEPADPEGGCCWNPHCKQAVYFFSPAPDPRALLGGPRTVSYAVEFHPDTGDIIMEFRHADTPD
Protein: Uncharacterized protein (Q5BF02)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MKGLQHGLSLLVILCLAHWVSSRAVRFDLRLTWEDRNVAGVVRKVILSNGQFPGPTLRVKQGDEVEFRVRNLMPFSTSVHFHGISQLGTPWSDGTPGLSQEPIEPGHQFIYRWTADEYGSYIYHSHSRGQLIDGLYGAIYVEPRGSVEKPFRLITQDATDLAAMISAESKTEPVMLSDWRFLTSEDIWQVEIASGVESVCSNAILINGKGSAWCLPQQRINDLTSVGQRQLLGNETMTDIGCFPPIDSFFGNYPRDPSILPKGFNSGCIPGYGPEEIVMVDASTRYISRDLISMAGSASLIFSIDEHPMYIYAIDGRYIEPVLVEAVRIVPGSRYSVLIELKQNRTAKDYTIRVAQNGLNQIINGSATMLYTSHRPQQNASIPYITETGDATTPQTVYLNESLIVPFPVQLPAPTVDQTIILNINHYHAAYRWQLGNGSFPMELEEVRPALFNASAIPYPYSVSTLNDTWVDIVFNVSGANQPPHPMHKHSNKYFVIGEGSTPFIWSSVAEAMEEMPENFNLVNPQLRDTYPTPFVPEATGVWLAIRYKVVNPGPFLLHCHLQMHQSGGMTLAILDGIGDWPLVPAEYQLSAAAAL
Protein: Slr0708 protein (Q55972)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
Sequence:
MSQNFFANLPKTRLLARLNDGWLGKAVLALALVLLMAFPTWALLNNAIKSSLLLDSQMNVYYAKSLDRYTGEFRAKHPIILGLFSNEGGDFYLYMPGKTTPIQAPPVPVQYQVVKGVSHSSMAIYAILQPYFATADNAPAAGDGWKAELTAYRAEQANTLAQADQLGLEPDALTAVKEILTNNISFIDETLAAGVIDHQKINAWIKEVVPHFTTTIATAATYQVDHWMEVMAEWKKMIGDQWDQTFGVTNTLYVTRTNNILFTLMAQFFGKEAINDRLLLFETTEFTTKPDTMLSLLTRIVKDRELGLAFFDDYFLMDVELLSTGAREAIARQDGARVPMAASQGSYAVGPAHARIRAYDEANGITPMLPPLAPFHSQEWPWRTVASEGEGPETLQEALDQK
Protein: Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (TANK-binding kinase 1) (Q0GKD6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Interferon regulatory factor 3
- TRAF family member-associated NFKB activator.
- TNF receptor-associated factor
- Stimulator of interferon genes protein
- Protein ref
- Guanine nucleotide exchange protein smcr8b
- Mitochondrial antiviral-signaling protein
- TNF receptor-associated factor 6
- Optineurin
- RNA helicase
Sequence:
MQSTANYLWMMSDLLGQGATANVYRGRHKKTGDLYAVKVFNNLSFLRPLDVQMREFEVLKKLNHKNIVKLFAVEEESNTRHKVLVMEYCPCGSLYTVLEEPTNAYGLPEDEFLIVLQDVVAGMNHLREYGIVHRDIKPGNIMRVIGDDGFSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITEKPPGAISGHQKFENGKIEWSSEMPISCSLSKGLQSLLTPVLANILEADQEKCWGFDQFFAETSDILHRIVVYVFSLQQATLHHVYIHTYNTANLFQELLFRRTNITPSHQELLYEGRRLVLDPNRQAQTFPKTSRDNPIMLLCRDPVNTVGLLFEDPSPPKVQPRYDLDLDASYAKTFAGDVGYLWKTSDSLLLYQELVRKGVRGLNELIRDEYSETMHKKTEVFHLCSHCSQTLERSEQLCEALMQGNILSAEYDEIRDTRKKVLRLSGSLASMDQTLQDINSMFLPGGSLTDTWTQQVGTHPEDRNVEKIKVLLDAIGAIYQQFKKDKAERRLPYNEEQIHKFDKQKLVLHATKARALFTDECAMKYRLFISKSEEWMKKFHHVRKHLLSLTGQFSSLEQEVTLLMQRLYKLLEQFPQKVVPMASGVLKPQAYLSPSTLVEMTLGMKKLKEEMEGVVKELAENNLFLERFGSLTVDGGMRTVERM
Protein: Protein phosphatase 2C 32 (AtPP2C32) (EC 3.1.3.16) (Protein POLTERGEIST) (Protein phosphatase 2C POL) (PP2C POL) (Q8RWN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of pedicel length and of CLAVATA pathways controlling stem cell identity at shoot and flower meristems.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein kinase and PP2C-like domain-containing protein
- Inactive leucine-rich repeat receptor-like protein kinase CORYNE
- Receptor protein kinase CLAVATA1
- Homeobox protein SHOOT MERISTEMLESS
- Protein phosphatase 2C 70
- 60S ribosomal protein L36
- Probable protein phosphatase 2C 59
Sequence:
MGNGTSRVVGCFVPSNDKNGVDLEFLEPLDEGLGHSFCYVRPSIFESPDITPSNSERFTIDSSTIDSETLTGSFRNDIVDDPSFLNRHNSKGLAETTFKAISGASVSANVSTARTGNQMALCSSDVLEPAASFESTSSFASIPLQPLPRGGSGPLNGFMSGPLERGFASGPLDRNNGFMSGPIEKGVMSGPLDVSDRSNFSAPLSFRRKKPRFQRFMRSVSGPMKSTLARTFSRRSGGLSWMHRFFLHPETRVSWAVGKDGKLHGEDPESCLESNRNLQWAHGKAGEDRVHVVLSEEQGWLFIGIYDGFSGPDAPDFVMSHLYKAIDKELEGLLWDYEEPSEDNQLQPDQEPPTEENMCDPESISEQHSKSVVAESEEVMIDDISSLGNTDTQIADGPPGDSAGPGKKSMRLYELLQLEQWEGEEIGLKRYGGNVALNNMTNQVENPSTSGGGAGNDPCTTDRSALDGIPNSGQRHGTKKSQISSKIRRMYQKQKSLRKKLFPWSYDWHREEGICVEEKIVESSGPIRRRWSGTVDHDAVLRAMARALESTEEAYMDMVEKSLDINPELALMGSCVLVMLMKDQDVYVMNVGDSRAILAQERLHDRHSNPGFGNDEGIGHKSRSRESLVRIELDRISEESPIHNQATPISVSNKNRDVTSYRLKMRAVQLSSDHSTSVEEEIWRIRSEHPEDDQSILKDRVKGQLKVTRAFGAGFLKKPNFNEALLEMFQVEYIGTDPYITCEPCTVHHRLTSSDRFMVLSSDGLYEYFSNEEVVAHVTWFIENVPEGDPAQYLIAELLSRAATKNGMEFHDLLDIPQGDRRKYHDDVSVMVVSLEGRIWRSSGQYYPERKQKFNR
Protein: Heme ligase (EC 4.99.1.8) (Heme detoxification protein) (PfHDP) (Hemozoin synthase) (Q8IL04)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Heme detoxifying enzyme that converts heme to crystalline hemozoin (beta-hematin) to protect the organism from the toxic effects of heme. During its development, P.falciparum proteolyzes vast amounts of host hemoglobin, leading to heme release.
Subcellular location: Vacuole {ECO:0000269|PubMed:18437218, ECO:0000269|PubMed:23471987}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:18437218}. Note=Delivered to the food vacuole, the site of hemozoin formation, via a unique trafficking route (PubMed:18437218, PubMed:23471987). Initially secreted into the cytosol of infected red blood cells (PubMed:18437218). A subsequent endocytosis of host cytosol delivers HDP to the food vacuole (PubMed:18437218). {ECO:0000269|PubMed:18437218, ECO:0000269|PubMed:23471987}.
Interaction partners:
Sequence:
MKNRFYYNLIIKRLYTRSGGLRKPQKVTNDPESINRKVYWCFEHKPVKRTIINLIYSHNELKIFSNLLNHPTVGSSLIHELSLDGPYTAFFPSNEAMQLINIESFNKLYNDENKLSEFVLNHVTKEYWLYRDLYGSSYQPWLMYNEKREAPEKLRNLLNNDLIVKIEGEFKHCNHSIYLNGSKIIRPNMKCHNGVVHIVDKPIIF