wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin, type II cytoskeletal 1b (Cytokeratin-1B) (CK-1B) (Embryonic type II keratin-1) (Keratin-77) (K77) (Type-II keratin Kb39) (Q6IFZ6)
Organism: Mus musculus (Mouse)
Interaction partners:
- Keratin, type II cytoskeletal 1
Sequence:
MSRQFSSQSAFSSRSRRAYSSRSSSGFGGGRQALVSVSQSRRYGGDYGGGFSSRSLYSLGGSKSIFGNLVGRSASGFCQSRGPGGGFGGGIGGGIGGGRGFGGGGFGGGYGGGGRFGGGFGGAGFGFGGFGPSYPPGGIHEVTINQSLLEPLHLEVDPEIQRVKTQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGALQSQVSISVQSSQVTIGGGGGGSGSYSGSSRGGGGGGGGTGSRGGGGGGGGSSYVSSSRSATKYGSGGGSSRTQILQTSTHSSRRHVVE
Protein: 4-hydroxyproline 2-epimerase (4Hyp 2-epimerase) (4HypE) (EC 5.1.1.8) (B9R4E3)
Organism: Roseibium alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11) (Labrenzia alexandrii)
Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Displays no proline racemase activity.
Interaction partners:
Sequence:
MRVIDSHTAGEPTRLVVEGGPDLGPGSLIEKAACLEAEHMDFCASVVLEPRGHDAIIGALLLPPSQPDCAAAVIYFNNLQNLGMCGHATIGLAVTLAHMGRIDPGRHKFETPVGIVEVDLQDANTVSVVNVESYRLHKDVTVEVPGHGKVTGDVAWGGNWFFLVKESPFDLTLENVPALTAYTKTIRQALENAGVTGTDCAWIDHIELFGPPKDPFAQSRNFVLCPGGAYDRSPCGTGCSAKLACLAEDGVLAPGEDWIQESVIGSTYRISYQPGTTKGVIPTITGQAFVTSDAHLIFNPADPYRFGIRPQNWTTSWITRTLSVEHG
Protein: 13 kDa ribonucleoprotein-associated protein (O74690)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Common component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA. In association with box C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and site-specific 2'-O-methylation of substrate RNAs. Essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U4/U6.U5 tri-snRNP-associated protein snu66
- U3 small nucleolar RNA-associated protein 15
- rRNA 2'-O-methyltransferase fibrillarin
- Pre-mRNA-processing factor 31
- Uncharacterized WD repeat-containing protein C2E1P5.05
- Pre-mRNA-splicing factor brr2
- Nucleolar protein 56
- Nucleolar protein 58
- U3 small nucleolar RNA-associated protein 4
- U4/U5/U6 small nuclear ribonucleoprotein prp3
Sequence:
MSVNPKAFPLADSGLTQQILDLVQQASHYKQLRKGANEATKTLNRGISEFIVMAADTEPIEILLHLPLLCEDKNVPYVFVPSKAALGRACGVSRPVISASITTNEASDLLPQIQAIKLAIEKLLI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (J3KNK0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGGGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSGGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGAPPRSLQPPPGRPDPELSSSPRRGPPKDKKLLATNGTPLP
Protein: MAM domain-containing glycosylphosphatidylinositol anchor protein 2 (MAM domain-containing protein 1) (P60756)
Organism: Rattus norvegicus (Rat)
Function: May be involved in cell-cell interactions.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Neuroligin-2
Sequence:
MDLVYGLVWLLTVLLEGISGQGVYAPPTVRIVHSGLACNIEEERYSERVYTIREGETLELTCLVTGHPRPQIRWTKTAGSASDRFQDSSVFNETLRITSIQRHQGGRYYCKAENGLGSPAIKSIRVDVYYLDDPVVTVHQSIGEAKEQFYYERTVFLRCVANSNPPVRYSWRRGQEVLLQGSDKGVEIYEPFFTQGETKILKLKNLRPQDYANYSCIASVRNVCNIPDKMVSFRLSNKTASPSIKLLVDDPIVVNPGEAITLVCVTTGGEPMPSLTWVRSFGTLPEKIVLNGGTLTIPAITSDDAGTYSCIANNNVGNPAKKSTNIIVRALKKGRFWITPDPYHKDDNIQIGREVKISCQVEAVPSEELTFSWFKNGRPLRSSERMVITQTDPDVSPGTTNLDIIDLKFTDFGTYTCVASLKGGGISDISIDVNISSSTVPPNLTVPQEKSPLVTREGDTIELQCQVTGKPKPIILWSRADKEVAMPDGTMQMESYDGTLRIVNVSREMSGMYRCQTSQYNGFNVKPREALVQLIVQYPPAVEPAFLEIRQGQDRSVTMSCRVLRAYPIRVLTYEWRLGNKLLRTGQFDSQEYTEYPLKSLSNENYGVYNCSIINEAGAGRCSFLVTGKAYAPEFYYDTYNPVWQNRHRVYSYSLQWTQMNPDAVDRIVAYRLGIRQAGQQRWWEQEIKINGNIQKGELITYNLTELIKPEAYEVRLTPLTKFGEGDSTIRVIKYTGEFHCGFEDGNICLFTQDDTDNFDWTKQSTATRNTKYTPNTGPNADRSGSKEGFYMYIETSRPRLEGEKARLLSPVFSIAPKNPYGPTNSAYCFSFFYHMYGQHIGVLNVYLRLKGQTTIENPLWSSSGNKGQRWNEAHVNIYPITSFQLIFEGIRGPGIEGDIAIDDVSIAEGECAKQDLPTKNSVDGAVGILVHIWLFPVIILISILSPRR
Protein: Interferon-related developmental regulator 1 (Nerve growth factor-inducible protein PC4) (O00458)
Organism: Homo sapiens (Human)
Function: Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal (By similarity).
Interaction partners:
- Ubiquitin-like protein FUBI
- Histone deacetylase 1
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL36
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL20
- Paired amphipathic helix protein Sin3b
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL38
Sequence:
MPKNKKRNTPHRGSSAGGGGSGAAAATAATAGGQHRNVQPFSDEDASIETMSHCSGYSDPSSFAEDGPEVLDEEGTQEDLEYKLKGLIDLTLDKSAKTRQAALEGIKNALASKMLYEFILERRMTLTDSIERCLKKGKSDEQRAAAALASVLCIQLGPGIESEEILKTLGPILKKIICDGSASMQARQTCATCFGVCCFIATDDITELYSTLECLENIFTKSYLKEKDTTVICSTPNTVLHISSLLAWTLLLTICPINEVKKKLEMHFHKLPSLLSCDDVNMRIAAGESLALLFELARGIESDFFYEDMESLTQMLRALATDGNKHRAKVDKRKQRSVFRDVLRAVEERDFPTETIKFGPERMYIDCWVKKHTYDTFKEVLGSGMQYHLQSNEFLRNVFELGPPVMLDAATLKTMKISRFERHLYNSAAFKARTKARSKCRDKRADVGEFF
Protein: Methyltransferase domain-containing protein (Q38BY6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Methyltransferase
- Phosphotyrosine protein phosphatase I domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Potassium voltage-gated channel, putative
- Succinate dehydrogenase assembly factor 3
- 30S Ribosomal protein S17, putative
- Treble clef zinc finger domain-containing protein
- Uncharacterized protein
Sequence:
MRIATSPTGRGKNSSVLPLLRRFSWGNGMCSPYYTEHRRQSTLTSSALSSPANHNQQVVYRSIRDCRERAFHLIQELVSSPIPGCGLSYSTNGSFGGPSLTVNAVSGVASLLELYDKAYYFLHLLHRTILVPRNVVRDTDDFTEFLLRCFRRPSDSLLKGDEELQMSDTAIVDGFVEWMETSLMSAGQFVSFVEVLQLVGSYVRYHKGVRWGARPSEEEWYRCGYRLHPWHDTYCPSSRAEQMPYVHLLQWLMRAKPTKLEEKIDDKEGAHGASSLFSTAAKESAMRAWYATEEFSPPSWHTVVGNSNRLGFTALDCGCHSGYMTELLLKAGAQEVLGVDVSPHHLGNAEATLSEHLRERRSSSYSRKTVQFVRCDILPDLPDEARQTKTPPLGPEGSTNSAAAENRRRLARCHHMPSDSDGLKTETEVTGPFDLLLFHPPLPLLFPTWPLFHDLYESVDQLAYDAGRRHPHCRLSVLNEFLQRLLGSSNGEENNSERRRNAHQQLNHQRRLVAPLIKDNGYVAFILPRNFDTRAILQRMSTSSAGKNCTSCGSDGLAPLVPLSDVVTMTLEGSYTLVLKRSHSLSSLLNRMDYIQKSISAFIRAFVSPQHRSRVEQEVRDFYSNHQAIDLIVMRKIARQKTNEDNDNKDCSVRAVLQKVSEPIAYEDSFEYEEYIPAGGSPLAHHWTEMTPSFSYLEDEFFGCADSVGTNGPPNGASFLAVGHPLVPVTRQLVGVDRFGAGGRDATQGESGSFDKMFAKEMRRRGGRMRKMALTPLEKQEWYIDEKLVKSEAAKVDLMNELSRFELKDFD
Protein: Ipomoelin (Jacalin related lectin) (JRL) (P93193)
Organism: Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Function: Lectin involved in defense reactions of the leaves in response to wounding by herbivorous insects and pathogens (Probable). Retards the growth and development of silkworm thus reducing their survival rates. Has hemagglutinating activity against human erythrocytes (Ref.4).
Interaction partners:
Sequence:
MALQLAAHSDARSGPVGSNGGQFWSFRPVRPLNKIVLSFSGSPDQTLNLISITFSSNPTDIITVGGVGPEPLTYTETVNIDGDIIEISGMIANYKGYNVIRSIKFTTNKKEYGPYGANAGTPFNIKIPDGNKIVGFFGNSGWYVDAIGAYYTAK
Protein: Polychaetoid, isoform K (A8JQV8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQFDYACYTVPECSTDDDDDNDDELGSNVTLENKDHSDCTLESDATTTTSSLERHMYRNRYRSNRSFGPQRVSMPILRSSRSREMTPQLGMYHEGPNRDPQWGYFVPLSPNFFFSPPMQRRRYREKENDRNRRAVSYGGDATSSPHSATIPRAAPRRVALMKDPPPPPPPKPQLGSKADSVSHLASKYPQSEYNLIQKIDSNSTLTAPAQYQPQNFYANTGTISSTNGYGSLLCHASSTTSPLAVRKRDKLLHRFSDAATLGRKLKKKKNTNRTCRSMTEAIEMLADPVIEDEFFGDRTTWEYHTVAVTRVPGYGFGIAVSGGRDNPHFANGDPSIAVSDVLKGGPAEDRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNTVQLVVKRRVPLNPINAAGAVQHQHSHSLSSVGLMANGSGGVAPTPITSLSQPNSLNSSLVQNASSGQPIKVTLTKGGKKDDYGVVLGCRLFVKEISSKAREQLNANGYSLQEGDIITRIHNTNCGDTMSLKEAKKIIDGCKERLNLVVLRDITNQTAVSQLNLNNSASHQASGNIYATHQPQVSGCSSSNNNLEDPYLPGGASYSSQNLYVQPPTRTSNGPNINGNGLNDEKSNLTPRGRSRGPIMDGVSLQQLDRPVTPTRGRSAAIDEPPRPPPPRGSSGGAAQEDFYSSRRQLYEERQSAEPRFISFQKEGSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQYCKEEYDEVVTNQRGDSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAEELATAQFNATKKEMNANESRGNFFRRRRSTHRRSKSLSRENWDDVVFSDSISKFPAYERVVLRHPGFVRPVVLFGPVSDLARERLAKDFPDKFSTPLQDDDKSAATSGKCRIVRLSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKAAHKSSKKLLEQCQKLERVWSHIFSTQIALSDEESWYRKLRDSIDLQQSGAVWMSESKFPDSPTEMLFPPYIAQPCKLACCRPISSTSVPRYSQDMNLNLNQNPSKSYSLIQNQAHTPPPPRPPPVGYAHSQSLAEKPRDRRSYTMVPIIKPASSMPSGLAPTVEPAAPMMPLDDCVLAMDGSNSQYHSSQPNLMSQSYLNSNLNGGSTSAVDQTNHSNAMRGFQPGPSVVSRYGLRSNAQVERRTTPYYYHELLLQKNLFDSSLNLLPQQQQQHQPDLAKSKNSNVQLEQQQQQQQQHQKHLADASNASKRAPMAKPQQRLISNGQGRSNYSSSGSLSNLLGNGHGLSNGHESSDGTLVDEGSFTLAFNNLTNQIASLNNSSSLNNNNCSTSRSINNNSNSHNINANNNNSHVNNADSNNNVGQSNECIA
Protein: Cell adhesion molecule DSCAML1 (Down syndrome cell adhesion molecule 2) (Down syndrome cell adhesion molecule-like protein 1) (Q8TD84)
Organism: Homo sapiens (Human)
Function: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11453658}; Single-pass type I membrane protein {ECO:0000305}. Synapse {ECO:0000250|UniProtKB:E1C8P7}.
Interaction partners:
- Cell adhesion molecule DSCAM
- Apolipoprotein A-V
Sequence:
MWLVTFLLLLDSLHKARPEDVGTSLYFVNDSLQQVTFSSSVGVVVPCPAAGSPSAALRWYLATGDDIYDVPHIRHVHANGTLQLYPFSPSAFNSFIHDNDYFCTAENAAGKIRSPNIRVKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSIIPEHRFFITYHGGLYISDVQKEDALSTYRCITKHKYSGETRQSNGARLSVTDPAESIPTILDGFHSQEVWAGHTVELPCTASGYPIPAIRWLKDGRPLPADSRWTKRITGLTISDLRTEDSGTYICEVTNTFGSAEATGILMVIDPLHVTLTPKKLKTGIGSTVILSCALTGSPEFTIRWYRNTELVLPDEAISIRGLSNETLLITSAQKSHSGAYQCFATRKAQTAQDFAIIALEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPIVRDGSHRTNQYTMSDGTTISHMNVTGPQIRDGGVYRCTARNLVGSAEYQARINVRGPPSIRAMRNITAVAGRDTLINCRVIGYPYYSIKWYKDALLLPDNHRQVVFENGTLKLTDVQKGMDEGEYLCSVLIQPQLSISQSVHVAVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIRITWRKDGQVIISGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPVPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKSMFLTVKIPAMITSHPNTTIAIKGHAKELNCTARGERPIIIRWEKGDTVIDPDRVMRYAIATKDNGDEVVSTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPVTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRALSITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYVDGEWGEMQNITTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDVPGPPAGIKAVPSSASSVVVSWLPPTKPNGVIRKYTIFCSSPGSGQPAPSEYETSPEQLFYRIAHLNRGQQYLLWVAAVTSAGRGNSSEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGDPAPAVKWTKDSEDSAIPVSMDGHRLIHTNGTLLLRAVKAEDSGYYTCTATNTGGFDTIIVNLLVQVPPDQPRLTVSKTSASSITLTWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLDSLKCGTWYKVKLAAKNSVGSGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWNNGGCPITAIVLEYRPKGTWAWQGLRANSSGEVFLTELREATWYELRMRACNSAGCGNETAQFATLDYDGSTIPPIKSAQGEGDDVKKLFTIGCPVILATLGVALLFIVRKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDAEFSQAVNPQSFCTGVSLHHPTLIQSTGPLIDMSDIRPGTNPVSRKNVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGVTVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTNENADSMTSMSTPSEPGICRFTASPPKPQDADRGKNVAVPIPHRANKSDYCNLPLYAKSEAFFRKADGREPCPVVPPREASIRNLARTYHTQARHLTLDPASKSLGLPHPGAPAAASTATLPQRTLAMPAPPAGTAPPAPGPTPAEPPTAPSAAPPAPSTEPPRAGGPHTKMGGSRDSLLEMSTSGVGRSQKQGAGAYSKSYTLV
Protein: Palmdelphin (Q9JHU2)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm. Cell projection, dendrite. Cell projection, dendritic spine {ECO:0000250}.
Interaction partners:
Sequence:
MEEAELVKGRLQAITDKRKIQEEISQKRLKIEEEKLKHQHLKKKALREKWLLDGIGSGKEHEEMRKQNQQDQHQTQVLEQSILRLEKEIQDLEKAELQISANEEAILKKLKSIEKTTEDIIRSVKVEKEENPEESIEDIYANIPDLPSSYIPSRLRKERNEGPDDEQNRKALYAMEIKVEKDLKTGESVVLSSIPLPSDDFKSTGIKVYEDRQKSVYAVSSNQNTTYNGTDGLAPVEVEDLLRQASERNSKSPTEYHEPVYANPFCRPVTPQRERVISPGPNFQERIMMKTNGLGNHANESAHNMTDGLSERRSNGPTHTSPTRPTPQPRSMVQQVEEMVHTQQKRMASPWEESSNRQNEHEVSPRMELSPSRASPGKSGPQCSSPTCQEETEDVRYNIVHSLPSDVDDTEPVTMIFMGYQQADDNEEEKKLLTGYDGVIHAELVVIDDEAEDNEGQTERPSYHPVAPYNQVYQPPKPTPLPRKRAEVRPYENTNHKSPHKNSISLKEQEERLGSPARHSPLDVPVAGDGTEDPSLTALRIRMAKLGKKVI
Protein: 2'-5'-oligoadenylate synthase-like protein 2 (EC 2.7.7.84) (54 kDa 2'-5'-oligoadenylate synthase-like protein) (p54 OASL) (M1204) (Q9Z2F2)
Organism: Mus musculus (Mouse)
Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L.
Interaction partners:
- Ubl carboxyl-terminal hydrolase 18
- Antiviral innate immune response receptor RIG-I
- Antiviral innate immune response effector IFIT1
- 2'-5'-oligoadenylate synthase-like protein 1
- Interferon-induced protein 44
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Ubiquitin-like protein ISG15
- Interferon-induced protein with tetratricopeptide repeats 2
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon regulatory factor 7
Sequence:
MDPFPDLYATPGDSLDHFLEHSLQPQRDWKEEGQDAWERIERFFREQCFRDELLLDQEVRVIKVVKGGSSGKGTTLNHRSDQDMILFLSCFSSFEEQARNREVVISFIKKRLIHCSRSLAYNIIVLTHREGKRAPRSLTLKVQSRKTDDIIWMDILPAYDALGPISRDSKPAPAIYETLIRSKGYPGDFSPSFTELQRHFVKTRPVKLKNLLRLVKFWYLQCLRRKYGRGAVLPSKYALELLTIYAWEMGTESSDSFNLDEGFVAVMELLVNYRDICIYWTKYYNFQNEVVRNFLKKQLKGDRPIILDPADPTNNLGRRKGWEQVAAEAAFCLLQVCCTTVGPSERWNVQRARDVQVRVKQTGTVDWTLWTNPYSPIRKMKAEIRREKNFGGELRISFQEPGGERQLLSSRKTLADYGIFSKVNIQVLETFPPEILVFVKYPGGQSKPFTIDPDDTILDLKEKIEDAGGPCAEDQVLLLDDEELEDDESLKELEIKDCDTIILIRVID
Protein: Uncharacterized protein (Q586B9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLSCGPRTPYMPRMERFFLLLLTGQALLCHFHQPAAAVVGLQEANMTLEARDWSQDSAVLDTSVKVVTSTVCGLINSTEEISIPNGWCVAFLTPMAPGKLTLNIHAETSNVRDFVTVSDTFRYWVGDDSKDLMDRITEAVNRELGVQYSTLSKLSGVYSSPCRSSKVNEMLPLCNSTRNCKTVLSFEGLKSNVTEFLCARVPKPCEKHVQTEEVWGGNVEIIIEGVKNSMEIAIDLVAEVREGNFSAERIELLQDERAAQLFASNELKMYDYPLIDEKKCASGNDLWLLLIAVPLILLLFSFRYIFGIGRRSGKHIERNAIIDDEVHGQQMGTACLPGQFQEFMYVDPQQLNGCEGNEFIQEADQILENQYTPQFTPACAEGDGETASCPGEEHTEDNAIYEYGTEQQFGAGGDRADHV
Protein: Replication factor C subunit 2 (Replication factor C2) (Activator 1 41 kDa subunit) (P40348)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair. RFC2 binds ATP and single-stranded DNA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Replication factor C subunit 4
- Chromosome transmission fidelity protein 8
- Chromosome transmission fidelity protein 18
- Proliferating cell nuclear antigen
- Checkpoint protein RAD24
- Replication factor C subunit 5
- Replication factor C subunit 1
- Telomere length regulation protein ELG1
- Sister chromatid cohesion protein DCC1
- Replication factor C subunit 3
Sequence:
MFEGFGPNKKRKISKLAAEQSLAQQPWVEKYRPKNLDEVTAQDHAVTVLKKTLKSANLPHMLFYGPPGTGKTSTILALTKELYGPDLMKSRILELNASDERGISIVREKVKNFARLTVSKPSKHDLENYPCPPYKIIILDEADSMTADAQSALRRTMETYSGVTRFCLICNYVTRIIDPLASRCSKFRFKALDASNAIDRLRFISEQENVKCDDGVLERILDISAGDLRRGITLLQSASKGAQYLGDGKNITSTQVEELAGVVPHDILIEIVEKVKSGDFDEIKKYVNTFMKSGWSAASVVNQLHEYYITNDNFDTNFKNQISWLLFTTDSRLNNGTNEHIQLLNLLVKISQL
Protein: Protein Mo25 (dMo25) (P91891)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein kinase STK11
- Synaptosomal-associated protein
- non-specific serine/threonine protein kinase
- STE20-related kinase adapter protein stlk
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Protein trachealess
- EG:100G10.5 protein
- Serine/threonine-protein kinase tricornered
Sequence:
MPLFGKSQKSPVELVKSLKEAINALEAGDRKVEKAQEDVSKNLVSIKNMLYGSSDAEPPADYVVAQLSQELYNSNLLLLLIQNLHRIDFEGKKHVALIFNNVLRRQIGTRSPTVEYICTKPEILFTLMAGYEDAHPEIALNSGTMLRECARYEALAKIMLHSDEFFKFFRYVEVSTFDIASDAFSTFKELLTRHKLLCAEFLDANYDKFFSQHYQRLLNSENYVTRRQSLKLLGELLLDRHNFTVMTRYISEPENLKLMMNMLKEKSRNIQFEAFHVFKVFVANPNKPKPILDILLRNQTKLVDFLTNFHTDRSEDEQFNDEKAYLIKQIKELKPLPEA
Protein: PIH1 domain containing 3 (Protein PIH1D3) (Twister) (Q6IVV7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Dynein axonemal assembly factor 4.
- Sperm-associated antigen 1A
- PIH1 domain-containing protein 2
- Dynein axonemal assembly factor 11
- Dynein axonemal assembly factor 10
- RNA polymerase II-associated protein 3
- Axonemal dynein light intermediate polypeptide 1
- TOG domain-containing protein.
- Dynein axonemal assembly factor 3
- RuvB-like 2
Sequence:
MEGLASVHDLQALSALLSKPKDNDEEEEDLTLQPMARMGPGHIGPPAAPSGKNKGSTSAYVKKNSKDIWDEAEVTEGAHFDDLNDPRPQPEYEIVLKQSVGTEDLFLGLSRKDPSSMCCESMLVRVKLPDTKTSDLVLDVRETFLDLRTPKYKLGLHLPHPVHKQEGNARFITEREELEITLPMNRPMDCINLT
Protein: MAP/microtubule affinity-regulating kinase 4 (EC 2.7.11.1) (Q8CIP4)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase (By similarity). Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Also phosphorylates the microtubule-associated proteins MAP2 and MAP4 (By similarity). Involved in regulation of the microtubule network, causing reorganization of microtubules into bundles (By similarity). Required for the initiation of axoneme extension during cilium assembly (By similarity). Regulates the centrosomal location of ODF2 and phosphorylates ODF2 in vitro (By similarity). Plays a role in cell cycle progression, specifically in the G1/S checkpoint (By similarity). Reduces neuronal cell survival (By similarity). Plays a role in energy homeostasis by regulating satiety and metabolic rate. Promotes adipogenesis by activating JNK1 and inhibiting the p38MAPK pathway, and triggers apoptosis by activating the JNK1 pathway. Phosphorylates mTORC1 complex member RPTOR and acts as a negative regulator of the mTORC1 complex, probably due to disruption of the interaction between phosphorylated RPTOR and the RRAGA/RRAGC heterodimer which is required for mTORC1 activation (By similarity). Involved in NLRP3 positioning along microtubules by mediating NLRP3 recruitment to microtubule organizing center (MTOC) upon inflammasome activation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:28656979}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm {ECO:0000250|UniProtKB:Q96L34}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q96L34}. Note=Localized at the tips of neurite-like processes in differentiated neuroblast cells. Detected in the cytoplasm and neuropil of the hippocampus. {ECO:0000250|UniProtKB:Q96L34}.
Interaction partners:
- Gamma-tubulin complex component 6
- Tubulin gamma-1 chain
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- E3 ubiquitin-protein ligase Topors
- Phosphodiesterase
- CDK5 regulatory subunit-associated protein 2
- Protein NEDD1
- Mitotic-spindle organizing protein 2
- Gamma-tubulin complex component 5
- Mitotic-spindle organizing protein 1
Sequence:
MSSRTALAPGNDRNSDTHGTLGSGRSSDKGPSWSSRSLGARCRNSIASCPEEQPHVGNYRLLRTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPSSLQKLFREVRIMKGLNHPNIVKLFEVIETEKTLYLVMEYASAGEVFDYLVSHGRMKEKEARAKFRQIVSAVHYCHQKNIVHRDLKAENLLLDAEANIKIADFGFSNEFTLGSKLDTFCGSPPYAAPELFQGKKYDGPEVDIWSLGVILYTLVSGSLPFDGHNLKELRERVLRGKYRVPFYMSTDCESILRRFLVLNPAKRCTLEQIMKDKWINIGYEGEELKPYTEPEEDFGDTKRIEVMVGMGYTREEIKEALTNQKYNEVTATYLLLGRKTEEGGDRGAPGLALARVRAPSDTTNGTSSSKGSSHNKGQRASSSTYHRQRRHSDFCGPSPAPLHPKRSPTSTGDTELKEERMPGRKASCSAVGSGSRGLPPSSPMVSSAHNPNKAEIPERRKDSTSTPNNLPPSMMTRRNTYVCTERPGSERPSLLPNGKENSSGTSRVPPASPSSHSLAPPSGERSRLARGSTIRSTFHGGQVRDRRAGSGSGGGVQNGPPASPTLAHEAAPLPSGRPRPTTNLFTKLTSKLTRRVTDEPERIGGPEVTSCHLPWDKTETAPRLLRFPWSVKLTSSRPPEALMAALRQATAAARCRCRQPQPFLLACLHGGAGGPEPLSHFEVEVCQLPRPGLRGVLFRRVAGTALAFRTLVTRISNDLEL
Protein: THO complex subunit 1 (AtTHO1) (HPR1 homolog) (AtHPR1) (Q93VM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export. Contributes to the integrity of the endogenous trans-acting small interfering RNA (ta-siRNA) pathway. May process or transport a long RNA molecule so that it can be a template for secondary siRNA production. May participate in the trafficking of siRNA precursors to the ARGONAUTE catalytic center. Required for the generation of functional messenger ribonucleoproteins (mRNPs). Plays an important roles in plant innate immunity.
Subcellular location: Nucleus {ECO:0000269|PubMed:22035198}.
Interaction partners:
- THO complex subunit 7B
- THO complex subunit 7A
- THO complex subunit 2
- THO complex subunit 3
- THO complex subunit 6
- THO complex subunit 5A
- THO complex subunit 5B
- THO complex subunit 4B
- THO complex subunit 4C
- THO complex subunit 4A
Sequence:
MDAFRDAILQRAPIETFALKTVQHFIQPQKQTKLAQDENQMLENMLRTLLQELVAAAAQSGEQIMQYGQLIDDDDDDDDIHGQIPHLLDVVLYLCEKEHVEGGMIFQLLEDLTEMSTMKNCKDVFGYIESKQDILGKQELFARGKLVMLRTCNQLLRRLSKANDVVFCGRILMFLAHFFPLSERSAVNIKGVFNTSNETKYEKDPPKGISVDFNFYKTFWSLQEYFCNPASLTSASTKWQKFSSSLAVVLNTFDAQPLSEEEGEANSLEEEAATFNIKYLTSSKLMGLELKDSSFRRHILLQCLIMFDYLRAPGKNDKDLPSETMKEELKSCEDRVKKLLEITPPKGKEFLRAVEHILEREKNWVWWKRDGCPPFEKQPIDKKSPNAGQKKRRQRWRLGNKELSQLWRWADQNPNALTDSQRVRTPDIADYWKPLAEDMDPSAGIEDEYHHKNNRVYCWKGLRFTARQDLEGFSRFTEMGIEGVVPVELLPPEVRSKYQAKPNEKAKRAKKEETKGGSHETEGNQIGVSNSEAEAEGGRGDAETMESDAIADTPTPEEQQRLGGSDTENGQEAGQIEDGETEEAGLMDTDLDHPPMPVS