wanglab/gogpt-training-data huggingface dataset:
Protein: G protein alpha s subunit (Adenylate cyclase-stimulating G alpha protein) (Guanine nucleotide-binding protein G(s) subunit alpha) (P20354)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase (By similarity).
Interaction partners:
- G protein beta subunit 5
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit gamma-e
- Guanine nucleotide-binding protein subunit gamma-1
- G protein alpha o subunit subunit alpha 47A)
- Adenylate cyclase type 9
- Dopamine receptor 1
- 5-hydroxytryptamine
- Uncharacterized protein, isoform B
Sequence:
MGCFGSPTSKQSDVNSEDSKSQKRRSDAISRQLQKDKQLYRATHRLLLLGAGESGKSTIVKQMRILHVDGFSDSEKKQKIDDIKKNIRDAILTITGAMSTLNPPVALEKKENEPRVEYIQDYASSPDFNYPPEFYEHTEELWKDKGVLQTYERSNEYQLIDCAKYFLDRVSTIKNPNYTPNEQDILRCRVLTSGIFETRFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVTACSSYNMVLREDPTQNRLRESLDLFKSIWNNRWLRTISIILFLNKQDLLAEKIKAGKSKLSEYFSEFNKYQTPIDTGDAIMESNDDPEVIRAKYFIRDEFLRISTASGDGKHYCYPHFTCAVDTENIKRVFNDCRDIIQRMHLRQYELL
Protein: Uncharacterized HTH-type transcriptional regulator YvaP (O32238)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Catechol-2,3-dioxygenase
- Putative NAD
- FMN-dependent NADH:quinone oxidoreductase 1
- General stress protein 14
Sequence:
MNQSEMCPRFEKAVDILSKRWVALIVFQLLNGSQRFSEIEAALPNLSGRVLSERLKELELEGVVKRDVIPETPVRIEYSLTDKGKALAPILGEISKWATEWIDPSFLD
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (A0A060Z4B6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- RRM domain-containing protein
- RRM domain-containing protein
- 6-phosphogluconolactonase
- 6-phosphogluconolactonase
- Transaldolase
- Transaldolase
- GDH/6PGL endoplasmic bifunctional protein
- Hexose-6-phosphate dehydrogenase
- Glucose-6-phosphate isomerase
Sequence:
TYDNIPISLWSQVADSEAERLSVFFSRNSYVSGKYTEESAFSNLHTHLLSLPGGGKANRLFYLALPPSVYHDVTKNIKHHCMSTKGWSRVIVEKPFGRDLQSSEELSTHLSSLFTEDQIYRIDHYLGKEMVQNLMVLRFGNRIFGPIWNRDSIACVVLTFKEPFGTQGRGGYFDDFGIIRDVMQNHLLQMLSLVAMEKPASTSSDDVRDEKVKVLKCIAPITMSDVVLGQYVGDPEGEGDAKLGYLDDPTVPKGSTQATFTTAVLYVHNERWDGVPFILRCGKALNERKAEVRLQFTDVPGDIFGAQCRRNELVVRVQPNEAVYAKMMSKKPGVYFHPEETELDLTYKSRYKDVNLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIESEKPPPIPYIYGSRGPTEADELSKRVGFHYEGTYKWVNPHKL
Protein: LP14345p (Lethal (3) neo38, isoform D) (E0R905)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMNFSAFGGPFSGIHQFAAKFDAQTPGAFGTPPAAAANAAAAAAAAGTDNHVQRYQTNGNHFNQNVPNVSAANNMQYGQNISIPYSQPQGDLNFLNAAAAADHKVLNQQILQNVNQSWQTLANTANTVDYSSHLLSATLPISIQHFLKYSETIKKESTGDVLKNGTNLASLALGGVALTPSNNGANGGHHNGLVGMDHGGHMTNMTDANGAALTNGASNGVNGNANGTVTNGGAGAVSSSGSVGTTNASGGTGTASGKKTKKKKPPKEKKPRPKPGEIRETKALDGSTLYCCPECQMAYPDRSLIEQHVISHAVERRFVCDICNAALKRKDHLTRHKLSHIPDRPHVCNICMKSFKRKEQLTLHIVIHSGEKKHVCIECGKGFYRKDHLRKHTRSHIARRVKSEVSAQNVNGSAGGGGGGGGGNSAQSNALHGS
Protein: N-alpha-acetyltransferase 40 (EC 2.3.1.257) (A0A1D8PLA7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone H4
- NAD-dependent protein deacetylase HST2
- 4-nitrophenylphosphatase
Sequence:
MEEIAEDLSLNYLTDRFRLPNFETYIEASHNMDENQIDKFIQLIDDNLGDLYVESEQYNWKNNKKEEMLEPGLVYIWFTETTPEEEEEEELVGFLSFKLCEDVDDVFVLYLFEIHLTQKYQGQKLGQSLIDQFHEFAKSLQNSSHELYSMLQGTALTVFSNNTRALNWYKKMNYELTEGSPMDRKLRNGTVIKPVLYLMRREL
Protein: Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) (Deubiquitinating enzyme 7) (Q9VYQ8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolase that deubiquitinates target proteins.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q93009}.
Interaction partners:
- GMP synthase
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin-ribosomal protein eL40 fusion protein
- Forkhead box protein O
- Ubiquitin-ribosomal protein eS31 fusion protein
- GH17761p
- Daxx-like protein
- Polyubiquitin
- BcDNA.LD22910
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MEIETDQSIEAMDTQDTQEVEILTSDLQQTQQQRNSPPQLPKFKNLIQPQLHAVGAVTQLPSENGNMPPQQLLADSSSTSFGDGEAMGIDDESKEDQFRSETTFSFTVENVVQLKSQRLSPPVYVRMLPWRIMVIPNDRALGFFLQCNGENDSPTWSCNAIAELRLKCHKPDAQPFTRARIKHLFYSKENDYGYSNFITWQELKDSEKSYVHNNSITLEVHVVADAPHGVLWDSKKHTGYVGLKNQGATCYMNSLLQTLYFTNSLRLSVYRIPTEADDSSKSVGLSLQRVFHELQFGDRPVGTKKLTKSFGWETLDSFMQHDVQEFLRVLLDKLESKMKGTILEGTIPGLFEGKMSSYIKCKNVDYNSTRYETFYDIQLNIKDKKNIYESFQDYVAPETLEGDNKYDAGVHGLQEASKGVIFTSFPPVLHLHLMRFQYDPVTDSSIKYNDRFEFYEHINLDRYLAESENTLADYVLHAVLVHSGDNHGGHYVVFINPKADGRWFKFDDDVVSSCRKQEAIEQNYGGMDDEISFHAKCSNAYMLVYIRQSELDRVLGDITESEISSDLVERLDLEKRIEMARRKERGEANTYVSVHVILEENFEEQHKRRLFDLEKVHPRVFRIKQNQTVDELVDLFVRGFGVSRQRMRMWNLCTAQTQKFSHFDFVAEGSRTIEQISTSQKPWVIWLQLAWTDVPGPLPPFNPKTESLLFLKYYDPRNKRLNYIGCTQQPHTRRLIDLVPDVNSKLGFEPDTELTIYDEYADKKLVNLNEPIESALFIPQDHLQGHILIFERENVDAKLDLPTVGDYFLDLVYRIEIIFSDKCNPNEPDFTLELSNRYNYDQLANAVAERLNTDPQKLQFFMCINNYKETAGNAVPYTFKGTIKDLVSYTKQSSTKRIFYQRLSLSIHELDNKKQFKCVWVSSDLKDEKELVLYPNKNDTVKGLLEEAAKKISFAENSRRKLRLLKISNHKIVAVCKDDIPLDTLLKSNESITTAQGAQKTFRIEEVPAEDMQLAENEFLIPVAHFSKELYNSFGIPFLTKARQGEPYGALKQRIQRRLNVQDKEWENYKFCVISMGHNADVNDNTPVDLEVYRSWTSGQLPFFGLDHINKSRKRSSLNFSEKAIKIYN
Protein: H/ACA ribonucleoprotein complex subunit 4 (EC 5.4.99.-) (Nucleolar protein at 60B) (Protein minifly) (O44081)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for maintenance of the germline stem cell lineage during spermatogenesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10087258, ECO:0000269|PubMed:37343092, ECO:0000269|PubMed:9829824}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 3
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit 1
- Nucleolar protein 56
- Protein SHQ1 homolog
- Nucleolar protein 58
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- rRNA 2'-O-methyltransferase fibrillarin
- Probable ATP-dependent RNA helicase pitchoune
Sequence:
MADVEVRKEKKKKKIKEEPLDGDDIGTLQKQGNFQIKPSSKIAELDTSQWPLLLKNFDKLNIRSNHYTPLAHGSSPLNRDIKEYMKTGFINLDKPSNPSSHEVVAWIKKILKVEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQSAGKEYVAIFKLHGAVESVAKVRQGLEKLRGALFQRPPLISAVKRQLRVRTVYDSKLLDYDETRNMGVFWVSCEAGSYIRTMCVHLGLVLGVGGQMLELRRVRSGIQSERDGMVTMHDVLDAMWLYENHKDESMLRRVIKPLEGLLVNHKRIIMKDSSVNAVCYGAKITLPGVLRYEDGIEIDQEIVICTTKGEAICLAIALMTTATMASCDHGVVAKIKRVIMERDTYPRKWGLGPKASAKKALIAAGKLDKFGRPNENTPKEWLTGYVDYNAKKPAAQEVSPTNGSSEPSKRKLSTSSVEETAAAAVSEETPSKDKKKKKKKHKGDEEAPEAAEEEAEPVEKEKKKKKKKDKDRDRDEAQE
Protein: Angiomotin (A6NP16)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MEHRGPPPEYPFKGMPPQSVVCKPQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARNSQPHSPTSSLTSGGSLPLLQSPPSTRLSPARHPLVPNQGDHSAHLPRPQQHFLPNQAHQGDHYRLSQPGLSQQQQQQQQQHHHHHHHQQQQQQQPQQQPGEAYSAMPRAQPSSASYQPVPADPFAIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSCMRPAKSLMSISNAGSGLLSHSSTLTGSPIMEEKRDDKSWKGSLGNDSK
Protein: 2-dehydro-3-deoxyphosphooctonate aldolase 2 (EC 2.5.1.55) (3-deoxy-D-manno-octulosonic acid 8-phosphate synthase) (KDO-8-phosphate synthase 2) (AtkdsA2) (KDO 8-P synthase) (KDOPS) (Phospho-2-dehydro-3-deoxyoctonate aldolase) (Q6NQL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the stereospecific condensation of D-arabinose 5-phosphate and phosphoenolpyruvate to form 3-deoxy-D-manno-octulosonate 8-phosphate (KDO-8-phosphate) and inorganic phosphate. Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO) which is an indispensable component of rhamnogalacturonan II (RG-II), a structurally complex pectic polysaccharide of the primary cell wall. RG-II is essential for the cell wall integrity of rapidly growing tissues and pollen tube growth and elongation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- 3-deoxy-manno-octulosonate cytidylyltransferase, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- 2-dehydro-3-deoxyphosphooctonate aldolase 1
- Probable arabinose 5-phosphate isomerase
- Sialyltransferase-like protein 2
- Sialyltransferase-like protein 1
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase MGP4
- Transcription elongation factor SPT4 homolog 2
- DNA-directed RNA polymerase V subunit 5C
- DNA-directed RNA polymerase subunit 10-like protein
Sequence:
MANSASLLYDQLKVAEPFFLLAGPNVIESEEHVLRMAKSIKDISTKLGLPLVFKSSFDKANRTSSKSFRGPGMAEGLKILEKVKVAFDLPIVTDVHESSQCEAVGKVADIIQIPAFLCRQTDLLVAAAQSGKIINIKKGQFCGHSVMRNSAEKVRLAGNPNVMVCERGTMFGYNDLIVDPRNLEWMREADCPVVADITHSLQQPAGKKLDGGGVASGGLRELIPCIARTAVAVGVDGIFMEVHDDPLNAPVDGPTQWPLRHLEELLEELIAIASVTKGKQQFQIDLTPYRD
Protein: K Homology domain-containing protein (Q7KN84)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKQLEEDCPNVNVNCLEDKIKLEGDPENVDRAVAYLSEIIKNYEENFTFEVMTVNPSYYKHIIGKAGANVNRLKDELKVNINIEEREGQNNIRIEGPKEGVRQAQLELQEKIDKLENEKSKDVIIDRRLHRSIIGAKGEKIREVKDRYRQVTITIPTPQENTDIVKLRGPKEDVDKCHKDLLKLVKEIQESSHIIEVPIFKQFHKFVIGKGGANIKKIRDETQTKIDLPAEGDTNEVIVITGKKENVLEAKERIQKIQNELSDIVTEEVQIPPKYYNSIIGTGGKLISSIMEECGGVSIKFPNSDSKSDKVTIRGPKDDVEKAKVQLLELANERQLASFTAEVRAKQQHHKFLIGKNGASIRKIRDATGARIIFPSNEDTDKEVITIIGKEESVKKAREQLEAIIKECDEVTEGEVSVDPKHHKHFVAKRGFILHRISEECGGVMISFPRVGINSDKVTIKGAKDCIEAARQRIEEIVADLEAQTTIEVVIPQRHHRTIMGARGFKVQQVTFEFDVQIKFPDRDATEPVEGLTNGGSGENGGENEGQEGEQEVEKEAEQEPVRQCDVIRITGRIEKCEAAKQALLDLIPIEEELSVPFDLHRTIIGPRGANVRQFMSKHDVHVELPPSELKSDVIKVCGTPARVAEAREALVKMIEDYEADRADRELRSFVLQVDVDTEFHSKLIGRHGAVINKLRADHDVIISLPKRDEPNDRIISITGYQANAEAARDAILEIVGDPETLHREVIEIDKRIHPHLIGQRRRTIRKIIEDNKVNIKFSADDDNPNSIFISGKIEDVENVKELLFGMAEDYERDYLDNVAIAPPTIGAFLTGQGSGSDAAGASENGFVIKDAPWEKQKQAKNLTAPNTQSQEDFPHFAAGGAPVASTPITSVWGPKN
Protein: Riboflavin biosynthesis protein RibBA [Includes: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)] (P9WHF1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- Riboflavin synthase
- Riboflavin biosynthesis protein RibD
- GTP cyclohydrolase 1
- 3,4-dihydroxy-2-butanone-4-phosphate synthase
- Bacterial bifunctional deaminase-reductase C-terminal domain-containing protein
- GTP 3',8-cyclase 1
- GTP 3',8-cyclase 2
- Nucleoside diphosphate kinase
- Uncharacterized protein Rv1417
Sequence:
MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMVRYTSGYLCVPLDGAICDRLGLLPMYAVNQDKHGTAYTVTVDARNGIGTGISASDRATTMRLLADPTSVADDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQPAGAICEIVSQKDEGSMAHTDELRVFADEHGLALITIADLIEWRRKHEKHIERVAEARIPTRHGEFRAIGYTSIYEDVEHVALVRGEIAGPNADGDDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAMVAREGRGVVLYMRGHEGRGIGLMHKLQAYQLQDAGADTVDANLKLGLPADARDYGIGAQILVDLGVRSMRLLTNNPAKRVGLDGYGLHIIERVPLPVRANAENIRYLMTKRDKLGHDLAGLDDFHESVHLPGEFGGAL
Protein: Leucine-rich repeat extensin-like protein 5 (AtLRX5) (LRR/EXTENSIN5) (Cell wall hydroxyproline-rich glycoprotein) (Q9SN46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Protein RALF-like 1
- Probable pectinesterase/pectinesterase inhibitor 33
- Ferritin-4, chloroplastic
Sequence:
MKTKMMMKNTSLIFVLLFITFFFTSISYSLSLTFNGDLSDNEVRLITQRQLLYFRDEFGDRGENVDVDPSLVFENPRLRNAYIALQAWKQAILSDPNNFTTNWIGSDVCSYTGVYCAPALDNRRIRTVAGIDLNHADIAGYLPQELGLLTDLALFHINSNRFCGTVPHRFNRLKLLFELDLSNNRFAGIFPTVVLQLPSLKFLDLRFNEFEGPVPRELFSKDLDAIFINHNRFRFELPDNLGDSPVSVIVVANNHFHGCIPTSLGDMRNLEEIIFMENGFNSCLPSQIGRLKNVTVFDFSFNELVGSLPASIGGMVSMEQLNVAHNRFSGKIPATICQLPRLENFTFSYNFFTGEPPVCLGLPGFDDRRNCLPARPAQRSPGQCAAFSSLPPVDCGSFGCGRSTRPPVVVPSPPTTPSPGGSPPSPSISPSPPITVPSPPTTPSPGGSPPSPSIVPSPPSTTPSPGSPPTSPTTPTPGGSPPSSPTTPTPGGSPPSSPTTPTPGGSPPSSPTTPSPGGSPPSPSISPSPPITVPSPPSTPTSPGSPPSPSSPTPSSPIPSPPTPSTPPTPISPGQNSPPIIPSPPFTGPSPPSSPSPPLPPVIPSPPIVGPTPSSPPPSTPTPVYSPPPPSTGYPPPPPFTGYSPPSPPPPPPPTFSPSPSIPPPPPQTYSPFPPPPPPPPQTYYPPQPSPSQPPQSPIYGTPPPSPIPYLPSPPQFASPPPPAPYYYSSPQPPPPPHYSLPPPTPTYHYISPPPPPTPIHSPPPQSHPPCIEYSPPPPPTVHYNPPPPPSPAHYSPPPSPPVYYYNSPPPPPAVHYSPPPPPVIHHSQPPPPPIYEGPLPPIPGISYASPPPPPFY
Protein: Androgen receptor (Q689Y8)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Interaction partners:
Sequence:
GSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKVKKLGSLKTQDEAEAASSSSPTEEQAPKMAMTHIGGFECQPIFLNVLEAIEPAVVCAGHDNSQPDSFSNLLSSLNELGERQLVYVVKWAKALPGFRNLHVDDQMSIIQYSWMGLMIFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCIRMRQLSQEFGWLQITPQEFLCMKALLFFSIIPVDGLKNQKLFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKVLDSVHPIAKDLHQFTFDLLIKAHMVSVDYPEMMAEIISVQVPKILSGKVKPIYFHAE
Protein: DNA helicase MCM9 (hMCM9) (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9) (Q9NXL9)
Organism: Homo sapiens (Human)
Function: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MRN complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. Acts as a helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand. In addition, recruits MLH1, a component of the MMR complex, to chromatin. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. Probably by regulating HR, plays a key role during gametogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26300262}. Chromosome {ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26300262}. Note=Colocalizes to nuclear foci with RPA1 following DNA damage (PubMed:23401855). Localizes to double-stranded DNA breaks (PubMed:23401855). Recruited to chromatin by MSH2 (PubMed:26300262). {ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26300262}.
Interaction partners:
- DNA helicase MCM8
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- DNA replication factor Cdt1
- DNA replication licensing factor MCM6
- Cell division control protein 6 homolog
- Cardiolipin synthase
- WD repeat and HMG-box DNA-binding protein 1
Sequence:
MNSDQVTLVGQVFESYVSEYHKNDILLILKERDEDAHYPVVVNAMTLFETNMEIGEYFNMFPSEVLTIFDSALRRSALTILQSLSQPEAVSMKQNLHARISGLPVCPELVREHIPKTKDVGHFLSVTGTVIRTSLVKVLEFERDYMCNKCKHVFVIKADFEQYYTFCRPSSCPSLESCDSSKFTCLSGLSSSPTRCRDYQEIKIQEQVQRLSVGSIPRSMKVILEDDLVDSCKSGDDLTIYGIVMQRWKPFQQDVRCEVEIVLKANYIQVNNEQSSGIIMDEEVQKEFEDFWEYYKSDPFAGRNVILASLCPQVFGMYLVKLAVAMVLAGGIQRTDATGTRVRGESHLLLVGDPGTGKSQFLKYAAKITPRSVLTTGIGSTSAGLTVTAVKDSGEWNLEAGALVLADAGLCCIDEFNSLKEHDRTSIHEAMEQQTISVAKAGLVCKLNTRTTILAATNPKGQYDPQESVSVNIALGSPLLSRFDLILVLLDTKNEDWDRIISSFILENKGYPSKSEKLWSMEKMKTYFCLIRNLQPTLSDVGNQVLLRYYQMQRQSDCRNAARTTIRLLESLIRLAEAHARLMFRDTVTLEDAITVVSVMESSMQGGALLGGVNALHTSFPENPGEQYQRQCELILEKLELQSLLSEELRRLERLQNQSVHQSQPRVLEVETTPGSLRNGPGEESNFRTSSQQEINYSTHIFSPGGSPEGSPVLDPPPHLEPNRSTSRKHSAQHKNNRDDSLDWFDFMATHQSEPKNTVVVSPHPKTSGENMASKISNSTSQGKEKSEPGQRSKVDIGLLPSPGETGVPWRADNVESNKKKRLALDSEAAVSADKPDSVLTHHVPRNLQKLCKERAQKLCRNSTRVPAQCTVPSHPQSTPVHSPDRMLDSPKRKRPKSLAQVEEPAIENVKPPGSPVAKLAKFTFKQKSKLIHSFEDHSHVSPGATKIAVHSPKISQRRTRRDAALPVKRPGKLTSTPGNQISSQPQGETKEVSQQPPEKHGPREKVMCAPEKRIIQPELELGNETGCAHLTCEGDKKEEVSGSNKSGKVHACTLARLANFCFTPPSESKSKSPPPERKNRGERGPSSPPTTTAPMRVSKRKSFQLRGSTEKLIVSKESLFTLPELGDEAFDCDWDEEMRKKS
Protein: RING finger protein nhl-1 (Q03601)
Organism: Caenorhabditis elegans
Interaction partners:
- PH domain-containing protein
- Ubiquitin-conjugating enzyme E2 13
Sequence:
MSSSPQNEAEAREKMRELMSRPPSSRPADFVNPLEKIEQLLTCPICLDRYKQPKLLPCQHTFCYPCLESCADTLHRNLKCPECRAEHNIPYDGVKAFQPNYTLTGFLEIHLQATPESAAEIEEYIHRYNLERCKICDEKADCEPCAHCDRKACKECRQTHMDMLKRDMSRLLNQVKRLANRITEASDNLSKGVDMMTMNCETTKAEIKEYFHRYQRDLKKKEDNFLMEVDTFQATETRNMSNLRDVLEIESSNMSEAVSRLDAAIKGECSIEDSELVRMKNTFTEGLEYLRNFQPDADELFNRKLRFSAGDDAAKLPAAITTSGELCVLVPQFSGRYLPLEQSYLPRPFRLPLESDSYRVKSDERASMRDREADRTSSRHSHRNPEPDESSIRYRRRQQLEDEAWNRLRNSSAAPSLLTTSVTADSSSRTSPWAADRVTRSVEPTKSRPTSLIVPNTETPRTVSPASKPPLPPQSVERVERTEDASPAPLPQLPIRKPPLPRQQSSNDDSLNEKVETIRRAHQQRQDASRAASRAVSSEESEGEDFPVSTNRGRIRIVCRAASVNRDDGLMSMIPGTGTIINVPPPQHQLPASAPITNGTSEQVAIPVTHFTGEEDESDIVVPAWLQRRRQRFQRSRTNPDIQAQFTSARVQQLLAERQSRLDSSTTTDEEKEKLAVLRQRGRSASREAGEWRARGRPRAVFGRKGAKDGELNWPRGICALSGGLVATCDSSNHRVCVFDKDGKFVRQFGGYGAGAGQLDSAAGLASSKLRVIVSDRYNHRISVFGLEGDHLFSFGGHGQGNAKFNNPWGVAVDDLGSIYVADKDNHRVQVFDKNGQFIAKFGSFGHLPGQLNSPLFIAVSRVTHHVYVSDSSNHRISVFDPHGVHLFSFGEEGFHGGQFKFPRGIAIDSQENLIIADSGNNRIQVFDAQGQFVSSFGTWGGGAGQLKGVEDVCVTADGSIVVTDRENHRIQIF
Protein: Cyclic GMP-AMP synthase-like receptor 1 (cGLR1) (EC 2.7.7.-) (A1ZA55)
Organism: Drosophila melanogaster (Fruit fly)
Function: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in antiviral innate immunity. Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',2'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish). 3',2'-cGAMP is protected from poxin cleavage.
Interaction partners:
Sequence:
MAMNLENIVNQATAQYVKIKEHREPYTAHYNALKDKVYSEWKSSAVLGKLLKGSTLCGGYGDKLKVSIPDEFDLLIHLVFPENDKIIVKADASKPGNVILDMTKVMEIIGSQEHNKPVFDRLQKIVNNKKQLLEDKLNSFLESIMTQTLNKMGNQIEVAGRISHLQYKKCGPAHTIFVKGSCKYSVDFVPAIRLSAAQVVLAPEQRIHFGETLYWDAIPKPMKPAKTDNTSFTSSFYEAERRLLYGKQFLKPAIRLMKQNRNVKNKANLKSYHIKTLFLWQVIQQDPSYWSNSPKDIFIEMLGKLADSLALTPKKGKLPFFWDPKLDMFAQLTDSQRTDLYNHFRKCEYTFRKDNGNVNDCTENNVHSSFSKNTTYKL
Protein: Contactin-2 precursor (Transiently expressed axonal glycoprotein) (Q9W675)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MRMRILLCLLSLSFLALSNALGGDVCESGHDSGPVFEEQPSSLIYPEGMPEGKVTLGCQARSSPAAVYRWRVNGTDISFAEESHYTQVAGNLVINNPQNGRDGGSYQCLAINRCGTIVSRVANLKFGYLRDFPPESRSPQTVHEGMGTFLACQPPAHYPALSYRWFINEFPNFIQPEAGRWFVSQVTGNLYLANARANDTGNYFCFTTINMDVSTKSIFSKAVQLTVHPDASPRKTAPNIRVRFPAETYALSGQTAQLECFAYRNPIPKIRWRKVDGILPPKVGTSVDGPILIIPELNFDDEGMYECEVYNSEGRETHQGRVSVQAQPDWLQVMSDSEVEISSELQWSCAAAGKPRPTIRWLRNGHALITQDRVEVNNGRLKIANLALEDSGMYQCVAENKHSTIYSNAELRVQVQAPDFRLNPVRKLVPAARGGQVKMECKPRAAPKPTLFWSRGTELLTNSTRITVTPDGILWIYNISRADEGKYTCFAENYLGKANSTGHLSVRDATKITLAPSNADINQGENATLQCHASHDPTMDLTFTWSLNGVPLDLEEPNGHYRRMEGKETIGDLVIVNGQLSHAGTYTCTAQTVVDSAMASAKLVVRGPPGPPGGLVVTSVNDTSVELRWSRGYDNHSPIGKYVILGRSSQTHDWKRMRTDPANIEGNAESARVIDLRPWMDYEFQVIASNILGSGEPSMPSPRAQTKEAAPTVAPSGLGGGGGNRNELIITWTPMAREYQNGDSFGYILAFRKQGIPTWTVVKVPNVESSRYVYSNDSLTAYCPFEVRIKAYNKKGEGPFSQIAVVHSAEEEPTVSPRWINATALTAFEIQVSWEPIQHLNINGVLRGYEIRYWRQHEREAAADRVRTAGLENTARVTGLRPNTLYHITVLAYNSAGTGPASPRTTVITKKPPPNRPPGNVSWKVDGSWVTVRWDHVKSMDNESAVLGYKVLYKHEGQSALKVLEKSKTSVKLPLPKDNGYVVLEIRSWGDGGDGAAHETIVSRDSGTGMMVQNSSGNWRTPCWSLLLFTALALIGSSGL
Protein: Protein FRIGIDA-ESSENTIAL 1 (Zinc finger CCCH domain-containing protein 27) (AtC3H27) (Q84VG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator involved in the FRIGIDA-mediated vernalization pathway, but not in the autonomous flowering pathway. Acts cooperatively with FRI (FRIGIDA) or FRL1 (FRIGIDA-LIKE 1) to promote FLC (FLOWERING LOCUS C) expression. Required for the stabilization of the FRI-C complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:16291783}.
Interaction partners:
- FRIGIDA-like protein 1
- Protein SUPPRESSOR OF FRI 4
- Inactive protein FRIGIDA
- Inactive FRIGIDA-like protein 2
- Protein FLX-like 4
- Protein FLC EXPRESSOR
- Transcription initiation factor TFIID subunit 14
- Zinc finger CCCH domain-containing protein 44
- Zinc finger CCCH domain-containing protein 6
- Zinc finger CCCH domain-containing protein 55
Sequence:
MSDSDMDIDDDEVEQKVQVHTIVRESELFDKPPIQASNSHNDVKRHSVTTPLDEQSKIIKEQAFAQDNGTLPRFPAPGIPPRSFFTGGGGNEPEQKRAALPCKFFAKGWCFNGVSCKFLHVKENSNCTSQQLAENSMAGNGGIRSDLERRILDSREGVRVSQLSENGVTSLPTREDISFMNPQRVFSSMSFVNPPGSQRVFPFNNEMRFMPSFENIRRESLKQTYGADFTDNRSLVINNANSFALRSSFVHEHRPSISSYLKTDMGSAGPAWTGSLSSSVPMNDRASTVGDFENGNSLSGSGSLPTLQGVAVSSDKGAEANTTSTKKKVSSDDWEPSEPFKASFTIPPYILPSSDALYDPFTDIENLGDRPLNDSLSSKGEHARKSSCQQKDGDSASGPQARDCKNDDKSSSCSQNQHQETVARSLEAHGVVEGVATSVVDQNDTATPSKEISSATAAENRVVLKRIKPAGHDSWHRSDGSSYKKTKKSDEIDGEVRSDAGMKVMRLFRTAVVETIKEMLKPLWREGRLTKDVHNMIVKKAAEKVVGAAVQFHQVPTDTESVDQYLGLSGTRIVKLVEGYVEKYGKP
Protein: Cyclin 9 (Q382D4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein kinase, putative
- Protein kinase, putative
- Telomerase-associated protein, putative
- Transcription initiation protein, putative
- Spt4/RpoE2 zinc finger domain-containing protein
- [RNA-polymerase]-subunit kinase
- Plastid-encoded RNA polymerase subunit alpha
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerase subunit beta
- Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein
Sequence:
MAGFTETPSWPSLSCEQSSAAAVSVSYSPFVVEMSYYTIAIQAYSMTRYVVENLRLDSAVVGTAMTYWHIFVSVHGLKKVDEIVLSAACTFLASKVEHHKVRLSDIVALVFEVDPVGGVMESWRDVVGQAELLLCYTLKFNFQVIHPVNRINELVFDGNKAVLECAQRLFLLSFVTPLCTRASAEEIVEALVYLAADGAERLEVYANGFNITSSERRDGIISVMLDALVAMRKTTKLPKIDNVISARRKRLREQESTRPSVACSSVGTASTDNTPCAPSVE