wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein bL33m (39S ribosomal protein L33, mitochondrial) (L33mt) (MRP-L33) (Q9W4L1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O75394}.
Interaction partners:
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle 54 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle 19 kDa protein
- Signal recognition particle 14 kDa protein
- Signal recognition particle 9 kDa protein
- Serine/threonine-protein kinase ATR
- Ubiquitin-like protein 5
- Splicing factor 3B subunit 5
Sequence:
MRLTNVLFKKVKSKRIMVVLESVVSGHQFNAFRDRLADKLEIIRFDPYIQQESLYRERKKIRSA
Protein: Tegument protein VP22 (Tegument protein 9) (Q4JQW6)
Organism: Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3)
Function: Tegument protein that plays different roles during the time course of infection (By similarity). Participates in both the accumulation of viral mRNAs and viral protein translation at late time of infection (By similarity). Modulates the RNase activity of the virion host shutoff protein ORF17 probably to ensure necessary levels of key cellular mRNAs and proteins (By similarity). Plays a role in microtubule reorganization that occurs after viral infection by stabilizing microtubule network (By similarity). Plays a role in the inhibition of host innate immune system by targeting the CGAS enzymatic activity which is the principal cytosolic DNA sensor that detects invading viral DNA. Acts by mediating disruption of liquid-like droplets in which CGAS is activated, thereby preventing CGAS activity.
Subcellular location: Virion tegument {ECO:0000269|PubMed:18400847}. Host cytoplasm {ECO:0000250|UniProtKB:P10233}. Host nucleus {ECO:0000250|UniProtKB:P10233}. Host Golgi apparatus {ECO:0000250|UniProtKB:P10233}. Note=One of the most abundant tegument protein (about 2000 copies per virion). Localizes in the cytoplasm at 8 hours postinfection and in the nucleus at 16 hours postinfection. During virion morphogenesis, this protein probably accumulates at the trans-Golgi where secondary envelopment occurs. {ECO:0000250|UniProtKB:P10233}.
Interaction partners:
Sequence:
MASSDGDRLCRSNAVRRKTTPSYSGQYRTARRSVVVGPPDDSDDSLGYITTVGADSPSPVYADLYFEHKNTTPRVHQPNDSSGSEDDFEDIDEVVAAFREARLRHELVEDAVYENPLSVEKPSRSFTKNAAVKPKLEDSPKRAPPGAGAIASGRPISFSTAPKTATSSWCGPTPSYNKRVFCEAVRRVAAMQAQKAAEAAWNSNPPRNNAELDRLLTGAVIRITVHEGLNLIQAANEADLGEGASVSKRGHNRKTGDLQGGMGNEPMYAQVRKPKSRTDTQTTGRITNRSRARSASRTDARK
Protein: Phenylalanine aminomutase (L-beta-phenylalanine forming) (EC 5.4.3.10) (Phenylalanine ammonia-lyase) (EC 4.3.1.24) (Q6GZ04)
Organism: Taxus canadensis (Canadian yew)
Function: Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Also has low phenylalanine ammonia-lyase activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MGFAVESRSHVKDILGLINTFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQRKAEDGADIYGVTTGFGACSSRRTNQLSELQESLIRCLLAGVFTKGCASSVDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVVARIGDDVEVPAPEALSRVGLRPFKLQAKEGLALVNGTSFATALASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQDLSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLEQSCFGSILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSRFLPFYRFVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGVESFQSVWNKSA
Protein: High-affinity hexose transporter HXT7 (P39004)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity glucose transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- High-affinity hexose transporter HXT6
- Low-affinity glucose transporter HXT4
- High-affinity glucose transporter HXT2
- Low-affinity glucose transporter HXT1
- Probable glucose transporter HXT5
- Low-affinity glucose transporter HXT3
- Carbon catabolite-derepressing protein kinase
- Hexokinase-1
- Xylulose kinase
- D-xylulose reductase
Sequence:
MSQDAAIAEQTPVEHLSAVDSASHSVLSTPSNKAERDEIKAYGEGEEHEPVVEIPKRPASAYVTVSIMCIMIAFGGFVFGWDTGTISGFINQTDFIRRFGMKHKDGTNYLSKVRTGLIVSIFNIGCAIGGIILSKLGDMYGRKVGLIVVVVIYIIGIIIQIASINKWYQYFIGRIISGLGVGGIAVLSPMLISEVSPKHLRGTLVSCYQLMITAGIFLGYCTNFGTKNYSNSVQWRVPLGLCFAWALFMIGGMTFVPESPRYLAEVGKIEEAKRSIAVSNKVAVDDPSVLAEVEAVLAGVEAEKLAGNASWGELFSSKTKVLQRLIMGAMIQSLQQLTGDNYFFYYGTTIFKAVGLSDSFETSIVLGIVNFASTFVGIYVVERYGRRTCLLWGAASMTACMVVYASVGVTRLWPNGQDQPSSKGAGNCMIVFACFYIFCFATTWAPIPYVVVSETFPLRVKSKAMSIATAANWLWGFLIGFFTPFITGAINFYYGYVFMGCLVFMFFYVLLVVPETKGLTLEEVNTMWEEGVLPWKSASWVPPSRRGANYDAEEMTHDDKPLYKRMFSTK
Protein: Ethylene-responsive transcription factor ERF008 (O22174)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 67
- Protein LIKE EARLY STARVATION
Sequence:
METEAAVTATVTAATMGIGTRKRDLKPYKGIRMRKWGKWVAEIREPNKRSRIWLGSYATPEAAARAYDTAVFYLRGPSARLNFPELLAGLTVSNGGGRGGDLSAAYIRRKAAEVGAQVDALGATVVVNTGGENRGDYEKIENCRKSGNGSLERVDLNKLPDPENSDGDDDECVKRR
Protein: Y+L amino acid transporter 1 (Solute carrier family 7 member 7) (y(+)L-type amino acid transporter 1) (Y+LAT1) (y+LAT-1) (Q9Z1K8)
Organism: Mus musculus (Mouse)
Function: Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Plays a role in nitric oxide synthesis via transport of L-arginine, and is involved in the transport of L-arginine in monocytes.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9UM01}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- Amino acid transporter heavy chain SLC3A1
Sequence:
MVNSTKYEVAAQHEADDGSALGDGASPVAEQVKLKKEISLLNGVCLIVGNMIGSGIFVSPKGVLMYSASFGLSLVIWAVGGIFSVFGALCYAELGTTIKKSGASYAYILEAFGGFLAFIRLWTSLLIIEPTSQAVIAITFANYMVQPLFPSCGAPYAAGRLLAAACICLLTFINCAYVKWGTLVQDIFTYAKVLALIAVIIAGIVRLGQGATANFENSFEGSSFAMGDIALALYSALFSYSGWDTLNYVTEEIRNPERNLPLSIGISMPIVTIIYLLTNVAYYSVLDIKEILASDAVAVTFADQIFGVFNWIIPVAVAFSCFGGLNASIVAASRLLFVGSREGHLPDAICMVHVERFTPVPSLLFNGVLSLVYLCVEDIFQLINYYSFSYWFFVGLSIVGQLYLRWKDPDRPRPLKLSLFFPIIFCLCTIFLVAVPLYSDTINSLIGIGIALSGLPFYFFIIRVPEHKRPLFLRRIVASITRYLQILCMSVAAEMDLEDGELSKQDPKSK
Protein: Histone acetyltransferase KAT2B (EC 2.3.1.48) (Histone acetyltransferase PCAF) (Histone acetylase PCAF) (Lysine acetyltransferase 2B) (P300/CBP-associated factor) (P/CAF) (Spermidine acetyltransferase KAT2B) (EC 2.3.1.57) (Q1LUC3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation (By similarity). Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles (By similarity). Also acetylates non-histone proteins. Involved in heart and limb development by mediating acetylation of tbx5. Also acetylates spermidine (By similarity). Together with kat2a, required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92831}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92831}. Note=Mainly localizes to the nucleus. Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation. Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q92831}.
Interaction partners:
- Transcriptional adapter 3
- Transformation/transcription domain-associated protein
- Transcription initiation factor TFIID subunit 9
- SAGA-associated factor 29
- Transcription initiation factor TFIID subunit 10
- Transcriptional adapter.
- Transcription and mRNA export factor ENY2
- Histone H2A deubiquitinase MYSM1
- Transcription initiation factor TFIID subunit 12
- Ubiquitin carboxyl-terminal hydrolase 22
Sequence:
MSESTGIPQGSPAVGAAGSAPAAPGVGGTECSGAAVGSARIAVKKAQLRSSPRPKKLEKLGVYSSCKAEGACKCNGWKSQNPPPTPPPPTPPRAEQPTAVSLMEPCRSCSHALGDHVTHLENVSEEEMNRLLGIVLDVEYLYTCVHKEEDPDTKQVYFSLFKLLRKCILQMGRPVVEALESPPFEKPSIEQGVNNFVQYKFSHLPSKERQTIVELAKMFLNQINYWQLETPSQKRQRAPDDDVAGYKVNYTRWLCYCNVPQFCDSLPRYEATQIFGRIFLRSVFTIMRKQLLEQARQEKDKLPPEKRTLILTHFPKFLSMLEEEVYSHNSPIWSENFMIGLSGGQIPTVVSAPPVNRSLYYSSSPAPVELAGGGSVSPARKTASVLEPNPGGEKRKPAEPLSHEDSKRPRVVGDIPMELINEVMSTITDPTAMLGPETSLLSAHSARDEAARLEERRGVIEFHVIGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLSLIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHEILNFLTYADEYAIGYFKKQGFSKDIKVPKSKYVGYIKDYEGATLMGCELNPCIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIAIESIPGIRETGWKPLGKSKELKDPDQLYSTLKNILTQVKSHPNAWPFMEPVKKNEAPGYYQVIRFPMDLKTMSERLKSRYYTTRKLFMADMQRIFTNCREYNPPESEYYKCANLLEKFFYTKIKEAGLIDK
Protein: Putative corticotropin-releasing hormone receptor type 2 (Q7ZZZ2)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDVTISQFILEEFDANRSLLDLQETVLESFSISFLGFHGLYCNATTDQIGTCWPRASAGKLVERPCPEFFNGIKYNTTKNAYRECLGNGTWASKINYSQCEPILDDKRKYAHHYKIALIINYLGHCISVGALIVAFMLFLCLRSIRCLRNVIHWNLITTFILRNVMWFLLQMIDHNIHESNEPWCRCITTVYNYFVVTNFFWMFVEGCYLHTAIVMTYSTDKLRKWVFLFIGWCIPCPIIVAWAIGKLYYENEQCWFGKEPGKYIDYIYQGPVILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDISQIVFIYFNSFLQSFQGFFVSVFYCFLNGEVRSAARKRWHRWQDHHSLRVRVARAMSIPTSPTRISFHSIKQTAAV
Protein: LMO7a (Q6JBI7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEGMEDAEADCSIAFAEAQRWVEAVTEKNFETRDFRASLENGVLLCDLINKLKPGVVRKINRLSTPIAGLDNINVFLKACEQIGLKEAQLFHPGDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQNNPYYHGPYLNLKAFETLLGQALTKALEDSSCLKRSGRDSGYGDIWCPDRGDFPAPPGSHRREDSFESLDSLGSRSLTSCSSDLTLRGGREGCESDNDWEFTFKMQDYNKDDMSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKNEDNRRSWASPVYTETEGTFSSTQRRAWGPKMENWHTVQETSTSSWCLEEEEEKVTRLPNVVKDDLYVRKLSPVMPSPGSSFDQFLPKGWTPEDMNWKKIKRETYKPWYKEFQGLSQFLLLQALQTYSDDILSSETNVKLDPTSGPRLITRRKNFSPTPGYRAHDLEPQSLDPDLENDDFFVRKTRAFHANPCVLRAFEDFRRFSEPDDAVERDIILQCREGELVLPDLEKDDMIVRRIPAQKKEVPLSGAPDRYQPVPFPEPWTLPPEIQAKFLSVLERTCPPKDKPSSCRVLVPSHRLKKDDMLTRKIQSWKLGTAVPPISFRPGPCSEADLRKWEAIREASRLRHRKRLMVERLFQKIYGENGSKSLSDVSAEDVQSLRQLRYEEMQKIKSQLKEQDQKWQDDLAKWKDRRKSYTSDLQKKKEEREEIEKQALEKSDRSSKTFREMLQDRESQSSTTTSRRRIYSSDDILDDGVLPPTVTLSETSYQSERLEDKARAHPAEMPKEDSTTFASREDGIAAEIPLASHIPEERRQAPWPSAETRQASSSSAESHQASLPSTESDQARLPSAEPHQASFSSAEPRQVPLVSAEPHQASSFSSTEPHQASLSSALQRPSSLSSSQQSWSTRGESTRISASLPRSYQRSDTARLTSVVTARPFGTSSRGISSLPRSYTMDDGWIYNGDVEVVKREQHDSGRAAGMKPDSSHFILGSSSEKEVATGEDGASLSSFVLPSSSSLSHDQAASSKATFSSTSGLDSVSDSGEGRSSSLREVSRSPDQFSDMRISINQTPGTKHDFGFTIKWDVSGISVASVEKGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEAMANAQETGNLVMDVRRYGKSGSPETKWIDTTSGIYSTEKSSSLSVTTDFSESLQSPYSESKEINGIHEGSNAFDSKASESISLKNLKRRSQFFEQGSSDSVAPDLPVPTLSAPSRWAWDQEEERRRQERWQKEQDRLLQEKYQREQEKLREEWQRAQQEAERENSKYLDEELMVLNSNSISLTSRESVTASWEPSWSEGSKSLDREGTRAGDEDRGQLEDDAVYEDQSQKLQERLMLEHEKKRKEQEAQEEELRKQREAEAQARAEAEAQARAEAQARAEAQAQAEAEARKRAEAQKLQAERERETSVKIYQYRRPIDSYDLPKREEESSGLLPIDRSKSRSTTELNDPLIEKSGSSKYSDRIGTTSFSQRSSKKDQGPSEAELERQQILQEMRKKTSLHNDNSWIRQRSASVNKEPICLTGIMRRGESLDNLDSQRPGSWRQSSWHSQPAGVYASSSVQDFSRLPPQLLSTSNRAYMRNPSSAVPPLAGSVKTSPGSPSPRSHSPSMSQSGSQLRNRSVSGKRVCSYCNSILGKGAAMIIETLGLCYHLHCFKCVSCERDLGGSSSGAEVRIRNHQLYCNDCYLRFKSGRPTAM
Protein: Transcription factor EC (TFE-C) (mTFEC) (Q9WTW4)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter. Collaborates with MITF in target gene activation. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence) (By similarity). Binds to element F in an E-box sequence-specific manner (By similarity). Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in a homo- or heterodimeric form.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MTFDCRVCDQTLKRAQPPAASCMPLAEHEPMSPDSDAGCAGNPFTNLLALGKKDGAEKWHLSGSILDVYSDEQGISSANAGLTDAPCPSILPMRKEIAETDGRALAKERQKKDNHNLIERRRRYNINYRIKELGTLIPKSNDPDMRWNKGTILKASVDYIKWLQKEQQRARELEHRQKKLEHANRQLRLRIQELEIQARAHGLPILASLGTADVGTHITKQQTHPERNLGGCCLQLTPTQGTSPEFYEQAVAFSDPLSHFTDLSFSAALKEEQRLDGMLLSDTICPFGTDPLLSAISPAVSKASSRSSLSSEDGDEL
Protein: Serine/threonine-protein kinase ICK (EC 2.7.11.1) (Intestinal cell kinase) (MAK-related kinase) (MRK) (Q62726)
Organism: Rattus norvegicus (Rat)
Function: Required for ciliogenesis, particularly in neuronal and retinal progenitor cells (By similarity). Phosphorylates KIF3A (By similarity). Involved in the control of ciliary length (By similarity). Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (By similarity). May play a role in cardiac development. Regulates intraflagellar transport (IFT) speed and negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner and this regulation requires its kinase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8570168}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9JKV2}. Nucleus {ECO:0000250|UniProtKB:Q9UPZ9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9JKV2}. Note=Also found at the ciliary tip. {ECO:0000250|UniProtKB:Q9JKV2}.
Interaction partners:
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM2
- Cell division control protein
- Origin recognition complex subunit 5
- Origin recognition complex subunit 2
- DNA replication factor Cdt1
- Origin recognition complex subunit 4
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
Sequence:
MNRYTTIKQLGDGTYGSVLLGRSIESGELIAIKKMKRKFYSWEECMNLREVKSLKKLNHANIVKLKEVIRENDHLYFIFEYMKENLYQLIKERNKLFPESAIRNIMYQILQGLAFIHKHGFFHRDLKPENLLCMGPELVKIADFGLAREIRSRPPYTDYVSTRWYRAPEVLLRSTNYSSPIDVWAVGCIMAEVYTLRPLFPGASEIDTIFKICQVLGTPKKTDWPEGYQLSSAMNFIWPQCIPNNLKTLIPNASSEAIQLLRDLLQWDPKKRPTASQALRYPYFQIGHPLGISTQDSGKPQKDVQDKTGPPPYVKPAPPAQAPTKAHTLISSRPNQASQPHQHFVYPYKGEASRTEQLSHVQEGQPNPPFFPSLHNKNLPPKILAGLEQKSGDMKPKSRRRWGLISRSTKGSDDWADLADLDFSSSLTRIDVKNKKRQSDDPLCRFESVLDLKPSEPVGTGTSVSTQASSQRRDTPTLQSTAKQHYLKHSRYLPGINIRNGVLPNPGKDFLPSSSWSSSGLSGKSSGTVSVVSKITSVGSGSTSSTGLTGSYIPSFLKKEVGSVMQRVQLAPLAAPSPGYSSLKAVRPHPGRPFFHTQPRSTPGLIPRPPAVQPVHGRIDWSSKYPSRR
Protein: Spinophilin, isoform J (M9NFI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
- LD12639p
- Liprin-alpha, isoform E
Sequence:
MEKPMHHAPAPVGKVSQIANIFQRKPIEIQPVEQLSAVAAAHAAAAAAAAAAHHAHVQGAPAVRTESHSARFNNARALFEKLGVESNSNVSSRLLRSGSREDNLCDGSDRSSSRSSDRSQSPPKRRTPFPSGVSLVHNNNNAAIVAQNGVPPEQRLSNSKFIVEPAAQVVPTSVVKYPQHNISRLKSEEPSPVPPPASGSVSALFASSGGDKPEKPERKFNSRELIEKQKKWTSHFTKTKTTRTHSDLNRCDIIRTVPGTGLIMDSEKVAKPAMEPPQPPPNASPNPPMRAQAPPEIKPRSGKIGSPVKSPPLPPIPAVKPKNVSPVKFNPDRLRQSPTKTADNSPPPPPAKSAAVLQRSLMQEQQELLRNSCDQGVAPIPPEKPRKKSVDLIEDTLPLTNCSTPSSCASPTSSYLMQPAKRGSLDGGSGNGQYPGNGLSGSTNSATSGSPVASASSGPSSPVHTEDEKQENESTEKSEMEYYHGGNYNSVPRRRRSENEGRKSVDESSPSANNSQQQQQHSIPGSAAGSPQRVANKRSSITVNMPAAGLGQRPPSIISTTSQDEGGFNESAPELKAKLQPAYDQTEEQPHSLNYVDVGYRLNPDGSESREVYGSEAELYDTAKVTDMQRKFHGANGFGQESSTVYAIIKPDVQESQPVAPSRSVLIQSPNSSSVEGSPLHRGSYSSPPVGVVSPIRRRNSSNQDQSVGGGGSAKTTPQCSPARSALVKGIAPIASIDAHEEEELDLVEEDEHLAVEYVEVLELQQDEEEEEAPVLPERRAPAQGSLELQDLEYADTSAGEDEEDIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSSILENKIRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVYSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLASRGGLANRQLPSANGNSSTSNGAAVDLGQLSNGNLLKRSRSNSRSSDCTLDDTDEEEEREGSALNLAGAPVAHETISLSNGNSHLLANVNNLLQHHPPAMATVIATPSNGHLGTTTPILLNSTSSASSSSSNQSTAREAQINQLYAQVHKDPSKQQHQQQQQQQQQAQAVTTSIPSIFKNALGSPADNGLNDFHRGSMTTFGTGPATSSNRDLNSSYDSILGSNDKLAENDPAESWMYPSRRRVAPNGSKVPLPGSSFTDQLNQALSDRERRLGDGSSRHSSDDYTEINKSQSAAAINCKTLINEIRQAVNEAQPKVKQVVPQSLSPPGTVPWQQQHHQQIQQQPSAHTTGPPSPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK
Protein: Protein BMH2 (P34730)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein BMH1
- Retrograde regulation protein 2
- Serine/threonine-protein kinase STE20
- Cell division control protein 42
- Retrograde regulation protein 3
- Phosphatidylinositol 4-kinase PIK1
- Filament protein FIN1
- Cytosolic neutral trehalase
- M-phase inducer phosphatase
- Negative regulator of RAS-cAMP pathway
Sequence:
MSQTREDSVYLAKLAEQAERYEEMVENMKAVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKEKSEHQVELIRSYRSKIETELTKISDDILSVLDSHLIPSATTGESKVFYYKMKGDYHRYLAEFSSGDAREKATNSSLEAYKTASEIATTELPPTHPIRLGLALNFSVFYYEIQNSPDKACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDISESGQEDQQQQQQQQQQQQQQQQQAPAEQTQGEPTK
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (H0YKC5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGAKTPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSG
Protein: Meiosis-specific with OB domain-containing protein (EC 3.1.-.-) (Protein expressed in male leptotene and zygotene spermatocytes 675) (MLZ-675) (Q9D513)
Organism: Mus musculus (Mouse)
Function: Single-stranded DNA-binding protein required for homologous recombination in meiosis I. Required for double strand breaks (DSBs) repair and crossover formation and promotion of faithful and complete synapsis. Not required for the initial loading of recombinases but required to maintain a proper number of RAD51 and DMC1 foci after the zygotene stage. May act by ensuring the stabilization of recombinases, which is required for successful homology search and meiotic recombination. Displays Single-stranded DNA 3'-5' exonuclease activity in vitro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20339383}. Nucleus {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}. Chromosome {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}. Note=Co-localizes with the RPA complex on meiotic chromosome axes. Accumulates on resected DNA. Localization is dependent on SPATA22. {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}.
Interaction partners:
- Fanconi anemia group M protein homolog
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Spermatogenesis-associated protein 22
- Replication protein A 14 kDa subunit
- DNA repair protein RAD52 homolog
- DNA replication ATP-dependent helicase/nuclease DNA2
- Serine/threonine-protein kinase ATR
- Meiotic recombination protein DMC1/LIM15 homolog
- DNA helicase MCM9
- DNA replication complex GINS protein SLD5
Sequence:
MAKFFALKNFTALSDLHPNMANLKIIGIVIGKTDVKGFPDRKNIGSERYTFSFTIRDSPCHFVNVSSWGSEDYIRSLSESFRVAECVIIENPLIQRKDTEREEKFSPATPSNYKLLLSENHSMVKVCSPYEVDTKLLSLIHLPVKESRDYYSLADIVANGHSLDGRIINVLAAVRSVGEPKYFTTSDRRKGQRCEVKLFDETEPSFTMTCWDNESILLAQSWMARETVIFASDVRINFNKFQNCMAATVISKTIITVNPDTPEANILLNYIRENKETNVADEIDSYLKESVNLNTIVDVYTVEQLKVKALKSEGKADPFYGILYAYISTLNIDDETTKVVRNRCSSCGYIVNEASNTCTICNQDSSRLKSFFLSFDVLVDLTDHTGTLHSCSLSGSIAEETLGCTINEFLTMTSEQKTKLKWQLLLERSKIYLKLILSHRARGGLKVTILSCKLADPTEASRNLARQGHT
Protein: DNA repair protein RecN (Recombination protein N) (Q8NQM0)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- NAD kinase
- Protein RecA
- DNA repair protein RecO
- DNA repair protein RadA
- Holliday junction branch migration complex subunit RuvB
- Holliday junction branch migration complex subunit RuvA
- UvrABC system protein B
- Single-stranded DNA-specific exonuclease
- Predicted sugar phosphatases of the HAD superfamily
- Regulatory protein RecX
Sequence:
MLVDIAIENLGVIPAASAEFSSGLTVLTGETGAGKTMVVTGLRLLSGGRADASRVRTGSPQAVVEGRFVTQGVPCDIVERATGIVSNAGGAADENGEFLAVRSVGANGRSKAHLGGRSVPAATLSEFSDELLTIHGQNDQLRLLSPERQLEALDRFDPELAQLRKNYNAKYLTWKSLDKDLQKRLSSRRELAQEVDRLQFAINEIEEVSPQPGEDAELVEQIRRLQDVDTLREQAATALAAIDGAGSLSDAMGGSGGFDESQESASDQLGQAESALAGSDDSKLKDIAVQLAEITSQLSQVSMELGGFLSDLPADPQALDDMLTRQQQLKLLTRKYAADIDGVIEWQRKAQIRLDSIDISSEALDKLKEDAKKAQASMMRAAKKLSAVRAKAATKLGTTVTEELQGLAMQKARFEVALTSIEACASGIDQVEFQLAANAFAQPRPLASSASGGELSRVMLALEVILAAGTTGTTLVFDEVDAGVGGRAAVEIGRRLARLATKNQVIVVTHLPQVAAYADTHLHVAKNVGEASVTSGVESLTFDRRVEELSRMLAGLDDTATGRAHATELLERAQREKEDINEERVEPLLAASA
Protein: Membrane-bound transcription factor site-2 protease homolog (EC 3.4.24.-) (Endopeptidase S2P) (F4JUU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Metalloprotease that catalyzes the second step (site-2 cleavage) in the proteolytic activation of various factors, after site-1 cleavage. Part of a regulated intramembrane proteolysis (RIP) cascade. After ER stress, cleaves BZIP17 and BZIP28 proteins which functions as stress sensors and transducers in ER stress signaling pathway. The N-terminal bZIP component is translocated to the nucleus, where it activates the expression and production of ER chaperones, as well as proteins involved in brassinosteroid (BR) signaling, which is required for stress acclimation and growth.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:20876872}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Subtilisin-like protease SBT6.1
- bZIP transcription factor 28
- bZIP transcription factor 17
- bZIP transcription factor 60
- Serine/threonine-protein kinase/endoribonuclease IRE1b
- Probable zinc metallopeptidase EGY3, chloroplastic
- Probable zinc metalloprotease EGY1, chloroplastic
- Serine/threonine-protein kinase/endoribonuclease IRE1a
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein BIP1
Sequence:
MEISGRRMRRFRMRFRRDHLTGGENIENEASCCYCDLKISNFNEPIFRLGRRFSGVLKVWFSIGLGFGVASLILVTVFLLLQFHSNPLFSNRLTSAVFGFSPSTRVSLSGIAYVLVSTVITVSVHELGHALAAASEGIQMEYIAVFIAAIFPGGLVAFDNDVLQSLPSFNALRIYCAGIWHNAVFCALCVFALFLLPVMLSPFYKHGESLTVVDVPSVSPLFGYLSPGDVIVSLDGIQVHKPSEWLELAAILDKENSKTSNGSLYLGGSRRFHHGKGYCVPISLIEEGYKGKMVENQFVCPGDLTAFRTMPCSNAAIREVSVCLDAKDIVKLQKCGDGWVTTSDTDNQSDCVCPQGDLCLQAMQSPGVLWTEITYKRTSSQDCSRLGLDFNTSNCLGTFVFVGDLIAMSHSVHLTAYQPRWLFNFFGKSFPNILERSLTCTFHVSLALVLLNSLPVYYLDGESILESSLQSFTWLSPRKKKKALQVCLVGGSLLSFLAFFRIFLLGLPLSRRW