wanglab/gogpt-training-data huggingface dataset:
Protein: DNA/RNA-binding protein Alba 2 (Q97ZF4)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P60849, ECO:0000255|HAMAP-Rule:MF_01122}. Chromosome {ECO:0000250|UniProtKB:P60849, ECO:0000255|HAMAP-Rule:MF_01122}.
Interaction partners:
- DNA/RNA-binding protein Alba 1
- Chromatin protein Cren7
Sequence:
MTEKLNEIVVRKTKNVEDHVLDVIVLFNQGIDEVILKGTGREISKAVDVYNSLKDRLGDGVQLVNVQTGSEVRDRRRISYILLRLKRVY
Protein: Autophagy and beclin 1 regulator 1 (A0A8I6AGV8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTTVECCQHPGILCLCSRCAGTRVPSLLPHQDSVPPASARATTPSFSFVQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHRELAPGLTGSEWTRTVLTLNSRSEVESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPSSGLATESDGGNGSSQNNSGNIRHELQCDLRRFFLEYDRLQELDQSLSGETPQTQQAQEMLNNNIESERPGPSHQPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWHVSTTFEGMPPSGNQLPPLERTEGQMPNSSRLELSSSASSQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGIEYYWDQLNETVFTVHSSSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPTTSVTSQGTQTLALQLQNAETQTEREEEEPGTASSGPGEGEGSEYGGSGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTESGAARTSSPQPSTSRGLLSEPGQLAERGLSPRTASWDQPSTSGRELPQPALSSSSPVPIPVPLASNEGPTMHCNVTNNSHLPEGDSSNVGEAAGPSGEPRNR
Protein: mRNA-decapping enzyme 1A (EC 3.6.1.62) (MAD homolog 4-interacting transcription coactivator 1) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF) (Q91YD3)
Organism: Mus musculus (Mouse)
Function: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). Essential for embryonic development.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:19861488, ECO:0000269|PubMed:33813271}. Nucleus {ECO:0000250|UniProtKB:Q9NPI6}. Note=Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). Colocalizes with NANOS3 in the processing bodies (PubMed:19861488). {ECO:0000250|UniProtKB:Q9NPI6, ECO:0000269|PubMed:19861488}.
Interaction partners:
- m7GpppN-mRNA hydrolase
- 5'-3' exoribonuclease 1
- Enhancer of mRNA-decapping protein 3
- Enhancer of mRNA-decapping protein 4
- Probable ATP-dependent RNA helicase DDX6
- Protein PAT1 homolog 1
- mRNA-decapping enzyme 1B
- Proline-rich nuclear receptor coactivator 2
- Regulator of nonsense transcripts 1
- Nonsense-mediated mRNA decay factor SMG5
Sequence:
MALSCSTVRPRRRGSALRSKMELLSRAEQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVVEEETRRSQQAARDKQSPSQANGCSDQRPIDILEMLSRAKDEYERNQMGGSNISSPGLQPSTQLSNLGSTETLEETPSGSQDKSAPSGHKHLTVEELFGTSLPKEQPTAMGLESEDTDKLLGDASQKEPSSFLPFPFEQSGGAPQSENLGIHSAAHHTVQPEVSTPVLITPASIAQSGDKHPPSYTLPLSPVLSPTLPAEAPTTQVPHLPRNSTMIQAVKTTPRQKSPLLNQPVPELSHSSLVASQSPFRAPVSLANPAGTALPSVDLLQKLRLTPQHDQIQAQPLGKGTMAPSFSSAAGQLATPESFIEPSSKTAAARAAVSASLSNMVLAPTLQSMQQNQDPEVFSQPKVLPSAIPIAGSPLVPATTTAVSSVLLSPSVFQQTVPRAADLERKASSPSPLTVGTAESQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHAVYLQVLTKNKDNHNL
Protein: Type II restriction-modication system restriction endonuclease (Q8E8A6)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
Sequence:
MNSLMTGLIKVDNITRSGLTIYDRIRTGDQQFWLTSEELSAVLNLRLKGTSFYGLAIRTRSKVAKELVCNALGYKVPSSFVKCQPRFSGQMFDTYVQKSNNLQVWNEELDVERRYVIIRTDENDIITQVKVIAGSDLAVLDTTGTLTQKFQARLTLSDQKMELISHFDTLNIQKILAPISLNLEIDSPVSQPQNGKLLPIGECFRRLSKIVGCSFTDAGRTQERNRGAALHALVCKALGYTDYRDNGQFPDIKHQLLEVKLQTSPTIDLGLVCPNSQANLDIEQLGLQQIRHCDVRYAIFYGYIVNGLVHITNLYLTTGEDFFNRFEQFGGKVLNKKIQIPLPRDFFS
Protein: Junction plakoglobin (Catenin gamma) (Desmoplakin III) (Desmoplakin-3) (P14923)
Organism: Homo sapiens (Human)
Function: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:22781308}. Cell junction, desmosome {ECO:0000269|PubMed:21495994, ECO:0000269|PubMed:22781308, ECO:0000269|PubMed:25208567}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22781308}. Cell membrane {ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:22781308}; Peripheral membrane protein {ECO:0000269|PubMed:22781308}. Cytoplasm {ECO:0000250|UniProtKB:Q9PVF7}. Cell junction {ECO:0000250|UniProtKB:Q9PVF7}. Nucleus {ECO:0000250|UniProtKB:Q9PVF7}. Note=Cytoplasmic in a soluble and membrane-associated form. Colocalizes with DSG4 at desmosomes (PubMed:21495994). {ECO:0000269|PubMed:21495994}.
Interaction partners:
- Desmoplakin
- Cadherin-1
- Desmoglein-2
- Probable splicing factor YJU2B
- Catenin alpha-1
- Plakophilin-2
- Desmoglein-1
- Desmocollin-2
- Adenomatous polyposis coli protein
- Catenin beta-1
Sequence:
MEVMNLMEQPIKVTEWQQTYTYDSGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYGDDMDATYRPMYSSDVPLDPLEMHMDMDGDYPIDTYSDGLRPPYPTADHMLA
Protein: Acidic leucine-rich nuclear phosphoprotein 32 family member A (Acidic nuclear phosphoprotein pp32) (Leucine-rich acidic nuclear protein) (LANP) (Potent heat-stable protein phosphatase 2A inhibitor I1PP2A) (O35381)
Organism: Mus musculus (Mouse)
Function: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription. Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation. In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltranferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking. Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition. Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12807913}. Cytoplasm {ECO:0000269|PubMed:12807913}. Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Translocates to the cytoplasm during the process of neuritogenesis.
Interaction partners:
- Protein SET
- Exportin-1
- ELAV-like protein 1
- Nuclear pore complex protein Nup214
- Tumor necrosis factor ligand superfamily member 13
- Acidic leucine-rich nuclear phosphoprotein 32 family member B
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
Sequence:
MEMDKRIYLELRNRTPSDVKELVLDNCKSIEGKIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMYLDGYDRDNKEAPDSDVEGYVEDDDEEDEDEEEYDEYAQLVEDEEEEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEEAGEEEGSQKRKREPDDEGEEDD
Protein: Uncharacterized protein (Q38EV8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMQRDTEGSSTSFGSCRTASDVSSQVLEAFNQAEERTSAVWSRIGVAEVDRRNKWNSFVESRLLVYVNDFVRLQEAEEMSLAAENDRLFREMFFASVRLKEPPQCKMLSQLVESILEQSASLSAEKSEDDQPPLRKRAITPDMSNNGELCYNVSSRSGSPLRNKMYADATIDEMSESVTLPSFVTATTMLAAKWGDTPDDRNTSRLPSFHNEFQRQKRERSSPNPSALPQEGIHQRDSAWTALWHLAQNMTHQELNRTLESEVERMNFLADVRLGQLCFLYKQHALLQLPPQEQIELRRQYAEKFLSTDVHGKVLHQSRHASLVPGLGNQNLMNAVRPTSSDAKTPGISSSQCTIGTSDCRSSVVRDEFDLLSDSIPDQLRTSQGFPPLNYVGGKGSGNDTEESCRSGGSSAGAQRGEASARGTIFAVDVDDVLRFGRRQDLSLERINTEAHVIHGKIIAQNTRMADECEGEVKCIDELWAMLEDTKSTEKGERRSGRGQEEGGEGISQFAKDNESAVPSQQEFMSRLNQLLYDYEHPEECVSPAVLLPVEGGKHFDFSEGTPGQRTVSPVLSCGYNAGASNSITGAGGPVNHLPAPLLKLFTVPSYAPILAYAVNMRERLQRFVLQKRMCLVRRVTDQLTDAYQHYYNRTHDPAYRVTPDYSQWMKGISGTALAGGLNLSTSISINNSDSGSVWQQLLYKFKPRVNNEDLKELLKEVQHVERRAGAELDSLNARLRILDELGPLLQRRDEILQQQRAIQEGSRERLLSRKVNMAKQLLYEENVRRQCVHELPKIYGQIAESLRRWNEEVTDKSSKGETNSARRLLINGVDVAELINEYYASVASTTNTRRPVRSRSATASATTSRNNSPSPLPSRGDAHALTPPRHPMRKMSPAPRTPMALREEYIPSGKPSIVNLGASPSLRVRSQPNISQRPAMKSGEPSPVKTMTPLTRKLHPHNPHLRSESPVAATRETLFKDSRKANR
Protein: RNA polymerase II subunit M (Q9VDY6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MGDNVIPAPLSRIPGTSQAKEKHSKDLKTLTYPQLLEIKDRQSHFLSFKKRLHQLPDKGKRLQESYDKLLAEIRRRDEVEEATRMLSGLNIVEKGKIALNNLEWNGRNTDEGAHVDDILDSDDEVEMDPLRIIAQGTMHEKKVKVLPPPTSFITADDLADIEEFKKPTDSPDSALAGHSDTSSLPAEIVEIDASQVAAKLSRELPPDQHALYLIDKTETNVNTPREKFMPFRTTKSNVHNPDKERVRKKGKHWEITAATPPLIQHKEAQLVPLAESAALQIDYMQRVKEVRIQQAEQRLARLKDSRLRLGLPEESIVKTKESFRNYRDPQDTFLIEGRQKASEANEVQDPTVQDRGSSASGIHYTVFE
Protein: RNA helicase (EC 3.6.4.13) (F1MAM8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Gem
- Gem-associated protein 5
- Survival motor neuron protein
- GEM
- Gem-associated protein 7
- Gem-associated protein 7
- Serine-threonine kinase receptor-associated protein
- Gem-associated protein 6
- Gem-associated protein 2
- Protein argonaute-2
Sequence:
MAAAFEALPASTTSESAMAAELEAAPVPAAEPTPASPWNLRTAHDIGGPRTRTGDVVLAEPADFESLLLSRPVLEGLRAAGFERPSPVQLKAIPLGRCGLDLIVQAKSGTGKTCVFSTIALDSLILENYSTQILILAPTREIAVQIHSVITAIGIKMEGLECHVFIGGTPLSQDKTRLKKCHIAVGSPGRIKQLIELDYLNPGSIRLFILDEADKLLEEGSFQEQINWIYSSLPASKQMLAVSATYPEILANALTRYMRDPTFVRLNPSDPSLIGLKQYYQVVNSYPLAHKIFEEKTQHLQELFSKIPFNQALVFSNLHSRAQHLADILSSKGFPTECISGNMNQNQRLDAMAKLKQFHCRVLISTDLTSRGIDAEKVNLVVNLDVPLDWETYMHRIGRAGRFGTLGLTVTYCCRGEEENMMMKIAQKCNINLLPLPDPIPAGLMEECLDCDVEVKAAMHTYSSPSISTQSPKKQVQKPERAFQSQRTPGSHMPSPRNTSVSTLSAKSKHGKQKLPVKSHSECGILEKAAPPQELGCTTHPEEQVKNSVQTSTEESSSNSLHQAKETSPGSLPKIPCLSSFKVHQLSALTFAELVEDYEHYIKEGLEKPVEIIRHYTGPGAQTVNPQNGFVRNRVSADRVQMLVSSSQSGDSESESDSCSSRTSSQSKGNKSYLEGSSDTQLKDSECTSVGGPLSLEQIQNGNDTSTQVEYQESPETQVKARHKEGANQRSKPSRRNPPRRSSYRVQTEAQEEGWHDCHRETNASSSDPYQDYEEYWRAYYRAWQEYYAAASHSYYWNAQRHPSWMAAYHMNTVYLQEMMRGNQ
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTP4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Nuclear pore protein
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein
- Nuclear pore protein
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MSKRGADNQLTREELDRDDISDEETPHQATMASSDVISRRKIAMPKRKMAFPSTLRGNTDESKTANAFSFLKKPQTEKTAANADDKPAKLKALNLQFKDKLEEFLNSDPACDLRPVFMKYGKYIDEINSSTSKTSVPEPKAFSFTPQSITETVAPGFGKVSAPRATTTPDVHTPKQTTFPFAPQAPKPEAASSQEPPKSSFTFTKPTTTVSDSKANADSSESDSEDEKEIKITGPTFSISTKPITSDSVFAFGAAKKEQKKDDSDSESDVEIKGPEFKFAGEVKSDVFKLHKKADENKNETKTDNSKVTENKAPTFSFGSTPNPFNTSGSKDENNSGSNEPAKQANTVPKPAFSFTNNLISKESESSQEKKPLSFNFTAPKTDNNEVQEASESEKTKSSESSTFSFGNNTTTKTNPFSGNTSGFSFGKPASTSNTTESKPSISFSKPQNNDTVPKSAFSFGTSANTVTETNEEKDSNTNGGNEDSKPALNFNFSSNTSSQKPSFSFGSTSEKKEETTEHSTTSGGFSFGQSKAPAFSFGTPATNTTTNNPPSSGFKFSLPFNQENKSNEADSSKISEKKEDGNSATVETTEEQSTSSSIQLQNGEEDETPLFTCRSKLMTINTKTNGYDSRGVGELKLLQKKDDKSKIRLLCRSDGMGNILLNTAVVKSFKYSPLTPENENLVKIPTIDKDGALVTYVARFKQKADGRLFVKSIEDAKNDMN
Protein: DNA-binding protein inhibitor ID-1 (Class B basic helix-loop-helix protein 24) (bHLHb24) (Inhibitor of DNA binding 1) (Inhibitor of differentiation 1) (P41134)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus.
Interaction partners:
- Forkhead box protein O3
- Transcription factor E2-alpha
- Transcription factor 4
- Protein C-ets-2
- Thrombospondin-1
- Myoblast determination protein 1
- Transcription factor 12
- Ras-related protein Rap-1A
- Ras-related protein Rap-1b
- DNA-binding protein inhibitor ID-3
Sequence:
MKVASGSTATAAAGPSCALKAGKTASGAGEVVRCLSEQSVAISRCAGGAGARLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTPGGRGLPVRAPLSTLNGEISALTAEAACVPADDRILCR
Protein: Isocitrate dehydrogenase [NAD] subunit, mitochondrial (A0A668KL51)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU361266}.
Interaction partners:
Sequence:
MAALSNVRWLTRAVLAARNSGAWRGLGTSTAHAASQSQAQDVRVEGAFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFKEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIYTPMEYKGELASYDMQLRRKLDLFANVVHVKSLPGYKTRHNNLDLVIIREQTEGEYSSLEHESAKGVIECLKIVTRTKSQRIAKFAFDYATKKGRSKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSATNMLRHLNLEYHSSMIADAVKKVIKAGKVRTSDMGGYATCHDFTEAVITALS
Protein: DNA-binding transcriptional activator DevR/DosR (P9WMF9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system DevR/DevS (also called DosR/DosS) involved in onset of the dormancy response. Regulates an approximately 48-member regulon. When phosphorylated binds and activates the promoter of DevR regulon genes in response to hypoxia. The presence of target DNA increases stability of phospho-DevR in vitro. Activates its own transcription under hypoxic but not aerobic conditions, probably binds as a dimer to tandem binding sites within the devR and hspX promoters. Accepts a phosphate group from DevS (DosS) and from DosT. Does not regulate transcription of dosT.
Subcellular location: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: Host cytoplasmic vesicle, host phagosome {ECO:0000269|PubMed:10970762}. Note=(Microbial infection) In human monocytes after in vitro infection (PubMed:10970762). {ECO:0000269|PubMed:10970762}.
Interaction partners:
- Oxygen sensor histidine kinase response regulator DevS/DosS
- Oxygen sensor histidine kinase response regulator DosT
- Universal stress protein Rv3134c
- Universal stress protein Rv2623
- Universal stress protein Rv2028c
- Nitrate reductase-like protein NarX
- ATP-dependent 6-phosphofructokinase isozyme 2
- Uncharacterized protein Rv0569
- Alpha-crystallin
- Sensor histidine kinase NarS
Sequence:
MVKVFLVDDHEVVRRGLVDLLGADPELDVVGEAGSVAEAMARVPAARPDVAVLDVRLPDGNGIELCRDLLSRMPDLRCLILTSYTSDEAMLDAILAGASGYVVKDIKGMELARAVKDVGAGRSLLDNRAAAALMAKLRGAAEKQDPLSGLTDQERTLLGLLSEGLTNKQIADRMFLAEKTVKNYVSRLLAKLGMERRTQAAVFATELKRSRPPGDGP
Protein: Transmembrane protein 237A (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog A) (F1Q930)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250}. Note=Localizes to the transition zone. {ECO:0000250}.
Interaction partners:
- Arrestin 3b, retinal
Sequence:
MCVTSRADKMPSVKPKKKKIKKEINEVEEPEAGPEPAIEMEGLESRRQSESREPLTPEPHDNPPLKKKKKKKTHTFENEGEQQDHPNGDVQESPTDGEEVTKKSKKKRKNKMMENQSHNELGVEEDDIITDVHAPISQRSLFSAPLSHSHPIGKVFVEKNRRFQATDLSHDHLEEYMEVRPMWNTRDVAMRVHSGFRIIGLFSHGFLAGYAVWNIIVVYVLAGEQMTTLPNLLQQYHSLAYPAQSLLYLLLAISTVSAFDRVNLAKASMALRGFLTLDPAALASFLYFAALILSLSQQMTSDRIHLYPTANETLWPPGLEHQILQPWIVVNLVVALLVGLAWVFVATRPDMDYTEEFLMAMEVEEYPRHDDKHELAA
Protein: Uncharacterized protein YDR239C (Q03780)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Activator of C kinase protein 1
- Probable serine/threonine-protein kinase RTK1
Sequence:
MFDGFSNNKGKRRSFFRFGSESKNNDSEKSVRKPSVPSTIKKSTNIARTSTAETSAPDIPPRSPNRNAHSRSHSIQAPLQKETLKNTNPFLNAEDTLGDSLELTQSKEASGNDHKGIEYLQENNIIGQRTNPFTTSANSNAHFSKIKRSRPPPPPMDMKSITTSISNNTTKEEIESNNDSERDSIAISSTHNQHRRQRSEAEKLVDDIENYINEHKVSSGSSLSLDTSENSDTKASQDKLPVDVMEAPILRNVSAESSLSYVKPLIVDNEEVNKASNGNLVQSDHLKEFSSNLDDGDDKFSFSTSASGKSTKSLQQVSKDESSGFKAAHFDFAYKSNEHLGSDGSIASARKPLRITNEIDSGSSNEDDDDGLQEKGFVDSESKAFINYASDQGSSIKNDVSTQEPELPSHRRIFRVVNEDRPSFYLNSVNDTGSLTDKHSFDTASSGEYDAKSNFSSQSGLSISKGSKSTVLAALDSNGNTKSSNKTSELNSLNSISESLVPAAHSFNEHTVTIPATVDLPNPVHDAPSERSVKCSPLTSVVSNKSEKSVPLVSSYVEELRLKYYKTSNFLQAPPNLPVALKQKNNLIQPKNIKVKLRTSSKQIGIKHGKVKQKLLALETRNEESDGTATGLKNKINVDHTKEFHKLLGKENETGSISKKEGTDAEQAEDYLKDIPGDEAYNSDDIMAPLREKRGQNGSVDSVSRSNTVVSYYTRSQNRMRSGTLDNDYVNRQKLPTHISLQDYRDANARSNISRQDSVSTTNSDVVDLSYSLGHGLRVANPDSDPE
Protein: Myelin protein P0 isoform X2 (Myelin protein zero) (A0A0R4IS04)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLSVLALTSVVLLGIASQSTALVVNTDSEKHALVGSDVRLSCSFFSWQWTSPEVSFTWHYRPDGAKDAISIFHYGGGEAYPANKGPFQNRLEFVGNPSRRDGSILIKNLDFGDNGTFTCDAKNPPDIGGHPSTIRLLVFEKVPVQAGVITGSIIGVVLGLLILVVAIYYLMRFLVARRVFSLSMSKHGKKGKGKEGSQQKQKPKVPLVFISF
Protein: Nuclease SbcCD subunit D (O83634)
Organism: Treponema pallidum (strain Nichols)
Interaction partners:
- Nuclease SbcCD subunit C
- DNA polymerase I
- ATP-dependent DNA helicase RecQ
- DNA topoisomerase 1
- Protein RecA
- Putative ankyrin repeat-containing protein TP_0502
- Ankyrin, putative
- Asparagine--tRNA ligase
- Membrane-bound lytic murein transglycosylase D
- OmpA-like domain-containing protein
Sequence:
MKILHTADLHLGKTLHEVSLFASQKKMLGDLCTLLAQDNYAALIIAGDIYDRCVPSAESVSLFSSFLQNIKRSMPRLPIYLIPGNHDSAQRLSFAQELLKQQGVFIAQDPEESTRPHLLCHEGETVQLFLLPFLHAGAFSYLDEENTTCLIHTQSELLQEASRRLQRAVSLDTPSILVAHLFTQKGISCESERPFVGNAVYADPHWFDFFTYVALGHLHKCQKITERMYYSGSPLPYSFDEANTQKVALSVEIHCNTKGFPIHVTPLPLEPLIPLRTIRDSFHALYTGDRYLLYQRDFLEITLTDPALVHNPIGLLKPRYPGLLSIKQENAFAFDIPPPYSSNEGIAPCTHHSLRTHFDVFMHEVSPTPDDREKGALFQELFDEMQQEFSS
Protein: Myb transcription factor 42 (ZmMYB42) (Myb-related protein Zm38) (K7UPS5)
Organism: Zea mays (Maize)
Function: Transcription factor that regulates negatively the expression of caffeic acid O-methyl-transferase genes (COMTs) and of other genes involved in the biosynthesis of lignin, thus preventing lignification.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MGRSPCCEKAHTNRGAWTKEEDERLVAYVRAHGEGCWRSLPRAAGLLRCGKSCRLRWINYLRPDLKRGNFTADEDDLIVKLHSLLGNKWSLIAARLPGRTDNEIKNYWNTHIRRKLLGSGIDPVTHRRVAGGAATTISFQPSPNTAVAAAAETAAQAPIKAEETAAVKAPRCPDLNLDLCISPPCQHEDDGEEEEEELDLIKPAVVKREALQAGHGHGHGLCLGCGLGGQKGAAGCSCSNGHHFLGLRTSVLDFRGLEMK
Protein: Glutamine-dependent asparagine synthetase (C9J057)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHA
Protein: DDB1- and CUL4-associated factor 11 homolog (C6KRL4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGNWITSTFLRFDLFQRHQPNRFLEYTRVQHSNQSPAYSVRTAAEIVAHQRMKPNHSNDSDTDFSSDDEGCPKMTPHEEQQMFEREQHIAFSGRCHIGDPESCTQLRNEINSRCGPRPSTSNNMEFILNRDLQKRGTSISNPRTVARVLNSHLPNQKRRVDRVATKSFCTQYIQNGTKIVVASQDEKIRFYQRNPDKSKYRSKYMKSDELRVDQCGWSILDTAISLNGDLIAYGTWKDAVFVGKLDFTERQNITWFPIDLNGEPGRDHCAVFCVKFSDSSEQIVCGTSQYSIHVFDVEQRRRIRTIVNAHEDDVNSVCFADLGSNLIYSAGDDGLVKVWDKRAWSDGDVEPVGVFAGHRDGVTHVDSRQDERYLLSNSKDQTIKVWDLRKFSNMSGVSQHWDYRWQPAPPGLCQPVAGDTSVMTLRGHSVLHTLVRANFSPESTGRRYIYTGCARGEVVVYDIMSGTVSRRLKGHTAVVRECDWHPTENEIVSSAWDGVTTVWTWDERQEGVIAPYDHPNISQFGDEDSCDELFQPVKKQCRRQRKTMSSRGHPCSSSSISQN