wanglab/gogpt-training-data huggingface dataset:
Protein: Diacylglycerol kinase delta (DAG kinase delta) (EC 2.7.1.107) (130 kDa diacylglycerol kinase) (Diglyceride kinase delta) (DGK-delta) (Q16760)
Organism: Homo sapiens (Human)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). By controlling the levels of diacylglycerol, regulates for instance the PKC and EGF receptor signaling pathways and plays a crucial role during development (By similarity). May also regulate clathrin-dependent endocytosis.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000269|PubMed:17880279}. Cytoplasm {ECO:0000269|PubMed:12200442}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:12200442}; Peripheral membrane protein {ECO:0000269|PubMed:12200442}. Cytoplasm {ECO:0000269|PubMed:12200442}. Note=Isoform 1 translocation from cytoplasm to the plasma membrane is induced by phorbol esters (PubMed:12200442). Phorbol esters induce the conversion into the monomeric form which can translocate to the plasma membrane (PubMed:12084710). {ECO:0000269|PubMed:12084710, ECO:0000269|PubMed:12200442}.
Interaction partners:
- Lipoprotein lipase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Diacylglycerol O-acyltransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Diacylglycerol O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGMLTKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITPCRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVCREALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLEGNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTALNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGSACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFYEDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCSVLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARPQIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVCPPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKILYPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDFNNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAVLNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCRTVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCELPRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSMDRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMDRQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGAPVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILCGIKELSRSAPAVEA
Protein: Ribosomal protein S6 kinase-related protein (EC 2.7.11.1) (Sugen kinase 494) (Q96LW2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGAVSCRQGQHTQQGEHTRVAVPHKQGGNIRGPWARGWKSLWTGLGTIRSDLEELWELRGHHYLHQESLKPAPVLVEKPLPEWPVPQFINLFLPEFPIRPIRGQQQLKILGLVAKGSFGTVLKVLDCTQKAVFAVKVVPKVKVLQRDTVRQCKEEVSIQRQINHPFVHSLGDSWQGKRHLFIMCSYCSTDLYSLWSAVGCFPEASIRLFAAELVLVLCYLHDLGIMHRDVKVENILLDERGHLKLTDFGLSRHVPQGAQAYTICGTLQYMAPEVLSGGPYNHAADWWSLGVLLFSLATGKFPVAAERDHVAMLASVTHSDSEIPASLNQGLSLLLHELLCQNPLHRLRYLHHFQVHPFFRGVAFDPELLQKQPVNFVTETQATQPSSAETMPFDDFDCDLESFLLYPIPA
Protein: Serine/arginine-rich splicing factor 10 (40 kDa SR-repressor protein) (SRrp40) (FUS-interacting serine-arginine-rich protein 1) (Splicing factor SRp38) (Splicing factor, arginine/serine-rich 13A) (TLS-associated protein with Ser-Arg repeats) (TASR) (TLS-associated protein with SR repeats) (TLS-associated serine-arginine protein) (TLS-associated SR protein) (O75494)
Organism: Homo sapiens (Human)
Function: Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing. May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:26876937}. Cytoplasm {ECO:0000269|PubMed:11684676}.
Interaction partners:
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 4
- RNA-binding protein FUS
- YTH domain-containing protein 1
- Transformer-2 protein homolog beta
- Transformer-2 protein homolog alpha
- Serine/arginine-rich splicing factor 9
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Serine/arginine-rich splicing factor 11
Sequence:
MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRFKHRNRSFSRSKSNSRSRSKSQPKKEMKAKSRSRSASHTKTRGTSKTDSKTHYKSGSRYEKESRKKEPPRSKSQSRSQSRSRSKSRSRSWTSPKSSGH
Protein: Cilia- and flagella-associated protein 20 (Bug22p) (A0CDD4)
Organism: Paramecium tetraurelia
Function: Cilium- and flagellum-specific protein required for axonemal structure organization and motility. May also play a role in cortical organization of basal body.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:20118210}. Cell projection, cilium {ECO:0000269|PubMed:20118210}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9Y6A4}. Note=Localizes preferentially in the terminal plate of the basal body and the transition zone of the cilium as well as in the vicinity of the outer doublets of axoneme and between the axoneme and the cell membrane.
Interaction partners:
- Chromosome undetermined scaffold_106, whole genome shotgun sequence
- Chromosome undetermined scaffold_2, whole genome shotgun sequence
- Chromosome undetermined scaffold_22, whole genome shotgun sequence
- Chromosome undetermined scaffold_1, whole genome shotgun sequence
- Chromosome undetermined scaffold_30, whole genome shotgun sequence
- Chromosome undetermined scaffold_80, whole genome shotgun sequence
- Chromosome undetermined scaffold_31, whole genome shotgun sequence
- Chromosome undetermined scaffold_30, whole genome shotgun sequence
- Chromosome undetermined scaffold_31, whole genome shotgun sequence
- Chromosome undetermined scaffold_121, whole genome shotgun sequence
Sequence:
MFKNSFQSGFLSILYSIGSKPLQIWDKQIKNGHIKRITDQDIQSSVLEIMGTNVSTNFITAPADPKETLGIKLPFLVMIIKNLKKYFTFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDEGWNQIQFNLSDFTRRAYGTNYIETLRVQIHANCRIRRIYFSDRLYSEEELPPEFKLFLPIQKQG
Protein: Luminescence regulator LitR (Transcriptional regulator) (Q8KX64)
Organism: Aliivibrio fischeri (Vibrio fischeri)
Interaction partners:
Sequence:
MDTIQKRPRTRLSPEKRKEQLLDIAIEVFSQRGIGRGGHADIAEIAQVSVATVFNYFPTREDLVDDVLNKVENEFHQFINNSISLDLDVRSNLNTLLLNIIDSVQTGNKWIKVWFEWSTSTRDEVWPLFLSTHSNTNQVIKTMFEEGIERNEVCNDHTPENLTKMLHGICYSVFIQANRNSSSEEMEETANCFLNMLCIYK
Protein: assimilatory sulfite reductase (ferredoxin) (EC 1.8.7.1) (Q9ADG1)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Interaction partners:
- Adenosine 5'-phosphosulfate reductase
- sulfate adenylyltransferase
- Sulfate adenylyltransferase subunit 2
- uroporphyrinogen-III C-methyltransferase
- Adenylyl-sulfate kinase
- IS1 family transposase
- Sulfurtransferase
- Secreted protein
- Cysteine synthase
- L-cysteine desulfhydrase Cds1
Sequence:
MAATPPKPAAATPRRKVSRHRGEGQWAAGHFTPLNGNEQTKKDDDGLNVRTRIETIYSKRGFDSIDPGDLRGRMRWWGLYTQRRQGIDGGKTAILEPEELDDRYFMLRVRIDGGALTTAQLRVVGEISQEFARGTADITDRQNVQYHWIRIEDVPEIWNRLEGVGLSTVTACGDTPRVMIASPVAGIAEDEIIDGTPALEEMKRRVLNNPAYSNLPRKFKTAISGSPVQDVVHEINDVAFVGVEHPEHGPGFDLWVGGGLSTNPKLGVRLNAWVPIDDVPDVYEGVISIFRDYGYRRLRNRARLKFLVADWGAEKFRQVLEDEYLKRKLTDGPAPAEPSSRWRDHIGVHRQKDGRYYVGFAPRVGRVDGTILTKVADLAEAHGSGRVRTTVEQKMIVLDVEEGRVDSLVESLEALDLSARPSTFRRGTMACTGIEFCKLAIVETKARGASLIDELERRLPDFDEPLTINLNGCPNACARIQTADIGLKGQLMLDEHGEQVEGYQVHLGGALGLEAGFGRKVRGLKVTAQELPDYVERVLKRFQAEREDGERFAAWAARASEEALS
Protein: Periostin (A0A8I5Y6L2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MVPLLPLSALLLLFLCDVDPANANSYYDKVLAHSRIRGRDQGPNVCALQQILGTKKKYFSSCKNWYQGAICGKKTTVLYECCPGYMRMEGMKGCPAVMPIDHVYGTLGIVGATTTQHYSDVSKLREEIEGKGSYTYFAPSNEAWDNLDSDIRRGLENNVNVELLNALHSHMVNKRMLTKDLKHGMVIPSMYNNLGLFINHYPNGVVTVNCARVIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDELSSFRAAAITSDLLESLGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSEAITGGAVFETMEGNTIEIGCEGDSISINGIKMVNKKDIVTKNGVIHLIDEVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASSLKPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLSDLYNGQILETIGGKQLRVFVYRTAICIENSCMVRGSKQGRNGAIHIFREIIQPAEKSLHEKLRQDKRFSIFLSLLEAADLKDLLTQPGDWTLFAPTNDAFKGMTNEEREILIGDKNALQNIILYHLTPGVYIGKGFEPGVTNILKTTQGSKIYVKGVNETLLVNELKSKESDIMTTNGVIHVVDKLLYPADIPVGNDQLLELLNKLIKYIQIKFVRGSTFKEIPMTVYRPAMTKIHIEGEPDFRLIKEGETVTEVIHGEPVIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLQKFLQKEVSKVTKFIEGGDGHLFEDEAIKRLLQGG
Protein: Lipid A acyltransferase PagP (EC 2.3.1.251) (Antimicrobial peptide resistance) (Lipid A acylation protein) (Q8ZR06)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Transfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with an acyl chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000269|PubMed:11013210}.
Interaction partners:
- Dioxygenase for synthesis of lipid
- Lipid A biosynthesis acyltransferase
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Phosphoethanolamine transferase EptA
- Lipid A 1-diphosphate synthase
- Outer membrane protein
- Kdo
- Tetraacyldisaccharide 4'-kinase
- Virulence transcriptional regulatory protein PhoP
- 3-deoxy-D-manno-octulosonic acid transferase
Sequence:
MYVAMIIRKYFLIIALLLMPWLAIPSVSAADKGGFNTFTDNVAETWRQPEHYDLYVPAITWHARFAYDKEKTDRYNERPWGVGFGQSRWDDKGNWHGLYMMAFKDSFNKWEPIGGYGWEKTWRPLEDDNFRLGLGFTAGVTARDNWNYIPIPVLLPLASIGYGPATFQMTYIPGSYNNGNVYFAWMRFQF
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (D3ZCF5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSNPGTRRNGSSIKIRLTGLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGGGGSVVDCRGLLENEGTVYEDSGPGRPLSCLMEEPAPYTDGTGAAAGGGNCRFVESPSQDQRLLVQRLRNPEVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLQLPSEGSVEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE
Protein: Phosphatase IMPL1, chloroplastic (EC 3.1.3.25) (Protein MYO-INOSITOL MONOPHOSPHATASE-LIKE 1) (Q94F00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphatase acting preferentially on D-myoinositol 1-phosphate (D-Ins 1-P).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}.
Interaction partners:
- 3'
- Probable inositol 3-phosphate synthase isozyme 3
- Inositol-3-phosphate synthase isozyme 1
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Inositol-3-phosphate synthase isozyme 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- 3',5'-bisphosphate nucleotidase 2
- Probable 3'
- Probable 3'
- Bifunctional phosphatase IMPL2, chloroplastic
Sequence:
MGRSLIFSGNMSLRISHLPRSSLPLQNPISGRTVNRTFRYRCTRILSNSFKSTTRLQTKAVLSEVSDQTRYPRIGAKTTGTISPAHLLEVVELAAKTGAEVVMEAVNKPRNITYKGLSDLVTDTDKASEAAILEVVKKNFSDHLILGEEGGIIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLYRGNPAAASVVEFVGGPMCWNTRTFSATAGGGALCNGQKIHVSKTDAVERALLITGFGYEHDDAWSTNMELFKEFTDVSRGVRRLGAAAVDMCHVALGIAESYWEYRLKPWDMAAGVLIVEEAGGAVTRMDGGKFSVFDRSVLVSNGVLHPKLLERIAPATENLKSKGIDFSLWFKPEDYHTEL
Protein: Amino acid transporter (Q9VPS6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
Sequence:
MGPPTSTELPPKTTECSDAPVELTGYRRWLSENLMLLVTLSGVLLGVILGLSLRPLNLHGDSIMLISYPGELFMRVLKLMILPLVISSLIAGSASLNAKMNGKIALRTLVYFASTSFFNAALGIALVLLIHPGNPDLHNADDRSTDRRAVNLLDSLLDLGRNVFPDNLFQASIQQAHTVYLPKPSILHVFNETMNDTLASGSEAQRLSEDLTEDVVLVRDIQYRSGTNTLGIVFFCLVFGTFLGTIGQKGQVVVDFFAAIFEVIMKMVTCVMWLTPVGISSVIAGKILSVGDLGLVMSQLMWFIVTVAIGVFIYQFVVMQAIYFVVVRRNPFKFYAGLIQAMLTAFATASTAAALPITFRCMNEKLKVDPRITRFVLPIGCNINMDGTALYIAVASIFIAQMSGMVLGFGELLTVLLTSTAASMSSASVPSAALVLLLVVLTAIDAPVQDVTLLFAVDWFVDRIRTTNNMLGDCYTAAVVEELSRKELMALDAASVNYQDMPAGTPNGHGHGHGHHDGGLLEGQTELETSSKCVMTMTDSVVVDISAVMNNVNLQQEHCNRRV
Protein: Eukaryotic initiation factor 4A-3 (eIF-4A-3) (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A-3) (DEAD-box ATP-dependent RNA helicase 23) (eIF4A-2) (Q6Z2Z4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:23732981}. Note=Localizes to the nucleus when interacting with DRM2. {ECO:0000269|PubMed:23732981}.
Interaction partners:
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor isoform 4G-2
- Zinc finger CCCH domain-containing protein 43
- Eukaryotic translation initiation factor isoform 4G-1
- Eukaryotic initiation factor 4A-1
- Protein mago nashi homolog 1
- Protein mago nashi homolog 2
- Expressed protein
- RNA-binding protein Y14B
- 40S ribosomal protein S6
Sequence:
MAGMAPEGSQFDAKHYDSKMQELLHQGDNEEFFTSYDEVFESFDDMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGILQQLDYGLVECQSLVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILASGVHVVVGTPGRVFDMLRRQSLRPDHIKMFVLDEADEMLSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMNKPVRILVKRDELTLEGIKQFYVNVEKEDWKLDTLCDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQRFYNVTIEELPANVADLL
Protein: Crossover junction endodeoxyribonuclease Hjc (Hjc) (EC 3.1.21.10) (Holliday junction resolvase Hjc) (E7FHX4)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Cleaves both mobile and immobile junctions. Binds 4-way junction DNA, a synthetic Hj, binding is not competed by dsDNA.
Interaction partners:
- ATP-dependent DNA helicase Hel308
- Endonuclease NucS
- DNA repair and recombination protein RadA
- CARDB domain-containing protein
- DNA double-strand break repair nuclease NurA
- DNA primase DnaG
- DOD-type homing endonuclease domain-containing protein
Sequence:
MYRKGAQAERELIKLLEKHGFAVVRSAGSKKVDLVAGNGKKYLCIEVKVTKKDHLYVGKRDMGRLIEFSRRFGGIPVLAVKFLNVGWRFIEVSPKIEKFVFTPSSGVSLEVLLGIQKTLEGKS
Protein: Transcription factor cwo (Protein clockwork orange) (Q9VGZ5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in the regulation of circadian rhythms. Transcriptional repressor which inhibits Clock-mediated transcriptional activation by binding to E boxes in the promoters of Clock target genes and repressing their transcription. E box binding activity is time-dependent with higher binding activity seen in the early morning (zeitgeber time 2) than early evening (zeitgeber time 14) and is dependent on the presence of the circadian protein per. It is likely that per binds to Clock-cycle heterodimers, reducing their affinity for E box binding and allowing cwo to bind instead. Negatively regulates its own expression.
Subcellular location: Nucleus {ECO:0000255, ECO:0000269|PubMed:17578908, ECO:0000269|PubMed:18375860}.
Interaction partners:
- Circadian locomoter output cycles protein kaput
- Protein cycle
- GH27708p
- GH23983p
- Adaptor protein complex AP-3 small chain sigma3
- Period circadian protein
- Protein timeless
- Cryptochrome-1
Sequence:
MEPYWNETNGHAAHPVKYESEAAVSSFPYCTESSLNFSTSATAYSEDDAEYATGRRNKTSRQDPLSHRIIEKRRRDRMNSCLADLSRLIPPQYQRKGRGRIEKTEIIEMAIRHLKHLQSECQQKESDYRSGYMDCMKEAAKFLYDVHMQDFCHRLLGRLQEHIDEMFKTDCYKSTRSCHMPDNVSASSGSPHQAYHPPLCHLRDMLATSASDVEHSQDHNDVKDLSFRNHLNQLQRSQQAAAAAAVAAAAVAVANGSSPASNAGVDSKVPLTNGGGTGGAPPAADNVPSNSTGSGSAAACAGGNSNSSGSNSSNAASSTICPPAGGSCPAKVTPLAAHQQPHQAPVITSTAPHHHHHHTDSSHHDFESSREPILHTDTSNMHSPPPRDLLLQQHPHLAHSHHTQDSLMSVRMRNYSESSHEIEHNNNYKYKNHIKERFVHELHDEETSSEHCPVAAHLQSDHSHLQALSEHSKDGTEPEIAPIMAKKRKLAEAAANGEIPLEVHTESSNAGASSANRLDKPSPSFNFSDIKDIKAELHNGNSNSSPLLAKLSAVAAAGGQLSTPSSTTAPLPPRHTFTVPIFALHGQGNYYVPLNVDYNALVPFLNGMDLLEKSYTSMPVVHPININVNFMPSSPSASLLAAAAAAAVAVGKQQQQQAVVAAGAGLPLSTNSAAAQAAAVAAAAVAKAKLEQAMNQSW
Protein: Malic enzyme (A0A1W2PQY8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLSRLRVVSTTCTLACRHLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKMESQLCRPGWSEVVQSQFNTTSASQVQVILLPQPPE
Protein: Transforming growth factor beta-1-induced transcript 1 protein (Androgen receptor-associated protein of 55 kDa) (Hydrogen peroxide-inducible clone 5 protein) (Hic-5) (TGF beta-stimulated clone 5) (TSC-5) (Q62219)
Organism: Mus musculus (Mouse)
Function: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity.
Subcellular location: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton, colocalizes with stress fibers.
Interaction partners:
- Vinculin
- Protein-tyrosine kinase 2-beta
- ARF GTPase-activating protein GIT1
- Scaffold protein ILK
- Alpha-parvin
- Neutrophil cytosol factor 1
- Talin-1
- TNF receptor-associated factor 4
- Talin-2
- Tyrosine-protein phosphatase non-receptor type 12
Sequence:
MEDLDALLSDLETTTSHMSRLGAPKERPPETLTPPPPYGHQPQTGSGESSGTTGDKDHLYSTVCKPRSPKPVAPVAPPFSSSSGVLGNGLCELDRLLQELNATQFNITDEIMSQFPSSKMAEGEEKEDQSEDKSSPTVPPSPFPAPSKPSATSATQELDRLMASLSDFRVQNHLPASGPPQPPAASPTREGCPSPPGQTSKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFLCSGCSTTLGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGEEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECLAPFSGGSFFEHEGRPLCENHFHAQRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERASKPYCQPCFLKLFG
Protein: Golgin B1 (Q9CTU9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLSRLSGLANNVLHELSGDYTDWNLMASSDADSSQETAMESNNRIMESTQEDALHRLAEAEKLVVELKDIISQKDVQLQQKDEALQEEKKAAENKIKKIKLHAKAKIMSLNKHMEEIKTQGGAALPPEAQAEELSKHNKSSTEEEM
Protein: Uncharacterized protein (Q383E0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRRGATLLTSAAAGGSSVGNPPAVAPGVVRSLYRMLLREVRKIDESPLSKTLFPLTVDLQHLTKSHGPLYFPNGQKYMDILREVFHDAATPQKVNLAFETLTRLRSHNERVTSRLSVFEKDRMHLINTMEASQPDKGLYRVERAPYNVNATSYRLPVGGGPSSLHSKLKIRQGYAVELEEGVALVAHPLSSTHMDRRVILIYEKGPHFTTGVVLDMLFTYPLSHGNPMFPEVFWGHKVYDGGVSQINFTMPPTAHISILHTLEPPTEPESPQYLAWLKWKDVKSKSRNTETTAEHPRLLCKPLIRGGVLDDGTVEPTLYLSKVEALPYLAQLVPGKPRSSARVYWGNMRWPTRQLEAEVANGHWIPVKLSPTFFGPFPLMAESGRADMFPTVAELKGMKETRERRYGVDVSLPQVFPPDRILRRRECLWDQIMYCLGGEYRSLVGCFNPFLESTQGVLPYDLPSPPSVVGCGLSDTEESVMMMEDLIDDAVERGAGEEAESGNYEEDLPFSAQMLGVTEVQGEEQLAKGERPPGSEKESDNEDDDKKKS
Protein: Thioredoxin-like protein 4B (Dim1-like protein) (Q9NX01)
Organism: Homo sapiens (Human)
Function: Essential role in pre-mRNA splicing. Required in cell cycle progression for S/G(2) transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:15161931}.
Interaction partners:
- Pre-mRNA-processing factor 6
- U4/U6.U5 tri-snRNP-associated protein 1
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- U4/U6 small nuclear ribonucleoprotein Prp31
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein-associated protein N
- U6 snRNA-associated Sm-like protein LSm7
- Small nuclear ribonucleoprotein G
- U4/U6 small nuclear ribonucleoprotein Prp3
- Small nuclear ribonucleoprotein F
Sequence:
MSFLLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTAVYTQYFDISYIPSTVFFFNGQHMKVDYGSPDHTKFVGSFKTKQDFIDLIEVIYRGAMRGKLIVQSPIDPKNIPKYDLLYQDI
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) (A0A1D8PE63)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glutathione synthetase
- Glutathione hydrolase
- Ecm38p
- Cys-Gly metallodipeptidase DUG1
- 5-oxoprolinase
- Branched-chain-amino-acid aminotransferase
- Branched-chain-amino-acid aminotransferase
- Glutathione reductase
- Cysteine synthase
- cystathionine gamma-lyase
Sequence:
MGLLSIGTPLSWDESKKYNNHVRTNGITQLINIFKQHGHRENDVFLWGDEVEYMLVDFDKTNKTARLSIDKDYIINDLNDPEKLLPIAEKQDVSYHPEYGRFMVEATPAKPYNGNLLXXXXXXXXXXXXXXQLCEDNLPSHIKLLTLTTFPRMGCNIFTSPPSKSNGIASQSLFLPDDIINRHARFPTLTANIRKRKGHKVAINLPIYPDKSTKLLDDTIPQNRELFDSDKEPWIGASKPGFIYMDSMGFGMGSSCLQITMQTKNISQARYLYDSLAPIAPIMLSLSAAAPIFKGFLVDQDVRWNVVSGAVDDRTFIEKGQEPYSGYHLFGGLDIDAQDKLRINNHQINQQGDLLDLYTKDGKPIQRVPKSRYDSIDNYLNDNYYDTKYFQDEYNDLNAPINEQVYQRLIDEGKLDKYMANHFAHLFIRDPLVIFSERINQDNNLENDHFENIQSTNWQTLRFKPPALYTKDTDLTTKPGWRVEFRPMEIQLTDFENAAYSSFITLLSKAILKFQPNFYIPLSKVEINMKLAHKVDSTLKDKFWFRSFELWNIDPQEFDDYGFEWFDRFINGNQQQNGHVNNNNNNDKKTKNDPIIVNGSTTTTNGTNSGSGITETNGTMLPKGCEGKTVEEINDVDDNGIDQRYTICQLINGSGKFPGFIKLVIKLIATDLVPQALNNSTTSKEQLIEELIRLRSYLYLLATRANGEIPTTAHWVRNKVLQHQDYKQDSKVSEKITFDLIDDSIKITELKDRQLIEGFLGADITEYLMGSK