wanglab/gogpt-training-data huggingface dataset:
Protein: SnoN protein (Q60979)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MENLQSKFSLVQGSNKKLNGMEDDGSPPVKKMMTDIHANGKTLTKVKKEHLDDYGDASVEPDRARKRNRVSLPETLNLNPSLKHTLAQFHLSSQSSLGGPAAFSARYSQESMSPTVFLPLPSPQVLPGTLLIPSDSSTELTQTLLEGETISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVSGILPFNAPSCGLITLTDAQRLCNTLLRPRTFPQNGSILPAKSSLAQLKETGSAFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYLGTPEEKKLKIILEEMKEKFSMRNGKRIQSKTDTPSGMELPSWYPVIKQEGDHVPQTHSFLHPSYYLYMCDKVVAPNVSLTSAASQSKEATKAETSKSTSKQSEKPHESSQHQKTVSYPDVSLEEQEKMDLKTSRELYSCLDSSISNNSTSRKKSESAVCSLVRGTSKRDSEDSSPLLVRDGEDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDSTLEKDREAEYAGQLAELRQRLDHAEADQRELQDELRQEREARQKLEMMIKELKLQIGKSSKPSKD
Protein: Hematopoietic lineage cell-specific protein (Hematopoietic cell-specific LYN substrate 1) (LckBP1) (P49710)
Organism: Mus musculus (Mouse)
Function: Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Dynamin-2
- Actin nucleation-promoting factor WASL
- Tight junction protein 1
- Proto-oncogene tyrosine-protein kinase Src
- Cofilin-1
- Cofilin-2
- Protein deacetylase HDAC6
- Paxillin
- Actin-related protein 2
Sequence:
MWKSVVGHDVSVSVETQGDDWDTDPDFVNDISEKEQRWGAKTIEGSGRTEHINIHQLRNKVSEEHDILKKKELESGPKASHGYGGRFGVERDRMDKSAVGHEYVADVEKHSSQTDAARGFGGKYGVERDRADKSAVGFDYKGEVEKHASQKDYSHGFGGRYGVEKDKRDKAALGYDYKGETEKHESQRDYAKGFGGQYGIQKDRVDKSAVGFNEMEAPTTAYKKTTPIEAASSGARGLKAKFESLAEEKRKREEEEKAQQMARQQQERKAVVKMSREVQQPSMPVEEPAAPAQLPKKISSEVWPPAESHLPPESQPVRSRREYPVPSLPTRQSPLQNHLEDNEEPPALPPRTPEGLQVVEEPVYEAAPELEPEPEPDYEPEPETEPDYEDVGELDRQDEDAEGDYEDVLEPEDTPSLSYQAGPSAGAGGAGISAIALYDYQGEGSDELSFDPDDIITDIEMVDEGWWRGQCRGHFGLFPANYVKLL
Protein: Platelet endothelial aggregation receptor 1 (mPEAR1) (Jagged and Delta protein) (Protein Jedi) (Multiple epidermal growth factor-like domains protein 12) (Multiple EGF-like domains protein 12) (Q8VIK5)
Organism: Mus musculus (Mouse)
Function: When overexpressed, reduces the number of both early and late non-adherent myeloid progenitor cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5VY43}; Single-pass membrane protein {ECO:0000255}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q5VY43}. Note=Detected on the cell surface in resting platelets. {ECO:0000250|UniProtKB:Q5VY43}.
Interaction partners:
- PTB domain-containing engulfment adapter protein 1
Sequence:
MPLCPLLLLALGLRLTGTLNSNDPNVCTFWESFTTTTKESHLRPFSLLPAESCHRPWEDPHTCAQPTVVYRTVYRQVVKMDSRPRLQCCRGYYESRGACVPLCAQECVHGRCVAPNQCQCAPGWRGGDCSSECAPGMWGPQCDKFCHCGNNSSCDPKSGTCFCPSGLQPPNCLQPCPAGHYGPACQFDCQCYGASCDPQDGACFCPPGRAGPSCNVPCSQGTDGFFCPRTYPCQNGGVPQGSQGSCSCPPGWMGVICSLPCPEGFHGPNCTQECRCHNGGLCDRFTGQCHCAPGYIGDRCQEECPVGRFGQDCAETCDCAPGARCFPANGACLCEHGFTGDRCTERLCPDGRYGLSCQEPCTCDPEHSLSCHPMHGECSCQPGWAGLHCNESCPQDTHGPGCQEHCLCLHGGLCLADSGLCRCAPGYTGPHCANLCPPDTYGINCSSRCSCENAIACSPIDGTCICKEGWQRGNCSVPCPLGTWGFNCNASCQCAHDGVCSPQTGACTCTPGWHGAHCQLPCPKGQFGEGCASVCDCDHSDGCDPVHGQCRCQAGWMGTRCHLPCPEGFWGANCSNTCTCKNGGTCVSENGNCVCAPGFRGPSCQRPCPPGRYGKRCVQCKCNNNHSSCHPSDGTCSCLAGWTGPDCSEACPPGHWGLKCSQLCQCHHGGTCHPQDGSCICTPGWTGPNCLEGCPPRMFGVNCSQLCQCDLGEMCHPETGACVCPPGHSGADCKMGSQESFTIMPTSPVTHNSLGAVIGIAVLGTLVVALIALFIGYRQWQKGKEHEHLAVAYSTGRLDGSDYVMPDVSPSYSHYYSNPSYHTLSQCSPNPPPPNKVPGSQLFVSSQAPERPSRAHGRENHVTLPADWKHRREPHERGASHLDRSYSCSYSHRNGPGPFCHKGPISEEGLGASVMSLSSENPYATIRDLPSLPGEPRESGYVEMKGPPSVSPPRQSLHLRDRQQRQLQPQRDSGTYEQPSPLSHNEESLGSTPPLPPGLPPGHYDSPKNSHIPGHYDLPPVRHPPSPPSRRQDR
Protein: CUGBP Elav-like family member 2 (CELF-2) (Bruno-like protein 3) (CUG triplet repeat RNA-binding protein 2) (CUG-BP2) (CUG-BP- and ETR-3-like factor 2) (ELAV-type RNA-binding protein 3) (ETR-3) (RNA-binding protein BRUNOL-3) (Q7T2T1)
Organism: Gallus gallus (Chicken)
Function: RNA-binding protein implicated in the regulation of several post-transcriptional events. May be involved in mRNA translation repression and stability. Mediates exon inclusion in TNNT2 pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:15830352}. Cytoplasm {ECO:0000269|PubMed:15830352}. Note=Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. {ECO:0000269|PubMed:15830352}.
Interaction partners:
- Uncharacterized protein.
- Muscleblind like splicing regulator 3
- Muscleblind like splicing regulator 2
- Muscleblind-like protein 1
- Chloride channel protein.
- Pleckstrin homology, MyTH4 and FERM domain containing H2.
Sequence:
MNGALDHSDQPDPDAIKTFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATTTNANPLSTTTGALGALTSPVAASTANSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY
Protein: Poly(A) RNA polymerase cid12 (PAP) (EC 2.7.7.19) (Caffeine-induced death protein 12) (Polynucleotide adenylyltransferase cid12) (O74518)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:16823372}.
Interaction partners:
- RNA-dependent RNA polymerase 1
- Helicase required for RNAi-mediated heterochromatin assembly 1
- RNA-induced transcriptional silencing complex protein tas3
- Protein air1
- Protein Dicer
- Protein argonaute
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Chromatin-associated protein swi6
- Poly
- Chromatin modification-related protein rik1
Sequence:
MGKVLLELHSVPWNEEGLSDNARLYSFLEFVSPKIEELKYRKLLLEKLQTHIREVVLDAELQVYGSMYIGTTLSISDVDVSLKSPRVGELEKRRVTMVLRKYLDADADFHSSARVPRINLVDVSGIGVDLTFGNDKACRTAELQKAYNEEHPIFGRLLMLLKHWLFERDLENVHHGGIASCALSYMLIGWLEMRFHKKGIDSEVQPIRALLQKFFYFWGVEWTYELFVLRPLTGQIVPKLQKGWLNEVQPNLLSIEDPIDRNNDIGKQSFQISMIKAAFVASANELLSDKTWFSTFAITEDEMFLCKQFENVINTKRSLVEGYDSDTESDELQAGG
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A2R8RXK7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDEDVTIKRKLLHRPIFRLRCLVKQLDKGEVNVVDLRKNIEYAASVLEAVYIDETRRLLDTEDELSDIQADSVPMEVRDWLASTFTRKMGVVRRRPEEKPRFRSIVHAVQAGIFVERMYRRTSNMAGLTYPPSVITALKDVDKWSFDVFKLQEASSDHALKFLVYELLTRYDLISRFRIPVSSLVSFVEALEIGYSKHRNPYHNLIHAADVTQTAHYLMLHTGVMHWLTELEILAMVFAAAIHDFEHTGTTNNFHIQTRSEVAILYNDRSVLENHHVSAAYRLMQEDEMNILVNLSKDDWRELRTLVIEMVMSTDMSCHFQQIKTMRNSLQQPEGIDKAKALSLMLHAADISHPAKGWKLHYRWTQALMEEFFRQGDKEAELGLPFSPLCDRKATMIAQSQIGFIDFIVEPTFSVLVDTTEKIISPLIEEAVKSGGVRRSSLTGRGSAAVVESVQRHSDRGSNDECGGSTDYSLCGIDQKHVRHLLSEIIQNNKERWKELSVQELANKQHERMSDLQEEPMRSTQLTLSQENHDSESKSLNELNNTDSTHSSQDSLDQSSQSPTEGAGDASPEEHSSETLPWNGKSA
Protein: NAC domain-containing protein 68 (ANAC068) (Protein NAC WITH TRANSMEMBRANE MOTIF 1) (Protein NTM1-like 12) (A8MQY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) mediated by calpain or its functional homolog. Regulates cytokinin signaling during cell division.
Subcellular location: Membrane {ECO:0000269|PubMed:17098812}; Single-pass membrane protein {ECO:0000269|PubMed:17098812}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:17098812}. Note=Localized primarily in plasma membrane or endoplasmic reticulum membrane as dormant form and, upon specific stress or signal, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:17098812}.
Interaction partners:
- Protein CROWDED NUCLEI 1
- Protein CROWDED NUCLEI 2
- Protein CROWDED NUCLEI 4
- NAC
- glucan endo-1,3-beta-D-glucosidase
Sequence:
MMKGLIGYRFSPTGEEVINHYLKNKLLGKYWLVDEAISEINILSHKPSKDLPKLARIQSEDLEWYFFSPIEYTNPNKMKMKRTTGSGFWKPTGVDREIRDKRGNGVVIGIKKTLVYHEGKSPHGVRTPWVMHEYHITCLPHHKRKYVVCQVKYKGEAAEISYEPSPSLVSDSHTVIAITGEPEPELQVEQPGKENLLGMSVDDLIEPMNQQEEPQGPHLAPNDDEFIRGLRHVDRGTVEYLFANEENMDGLSMNDLRIPMIVQQEDLSEWEGFNADTFFSDNNNNYNLNVHHQLTPYGDGYLNAFSGYNEGNPPDHELVMQENRNDHMPRKPVTGTIDYSSDSGSDAGSISTTSYQGTSSPNISVGSSSRHLSSCSSTDSCKDLQTCTDPSIISREIRELTQEVKQEIPRAVDAPMNNESSLVKTEKKGLFIVEDAMERNRKKPRFIYLMKMIIGNIISVLLPVKRLIPVKKL
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (A0A494C1N1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNRQGLILLPRLECSGTITACCSFDLLGSSDPPTST
Protein: Binder of sperm protein homolog 2 (Q0Q236)
Organism: Mus musculus (Mouse)
Function: Binds sperm in vitro but has no effect on sperm capacitation. Also binds gelatin and heparin, but not chondroitin sulfate B or phospholipid liposomes.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVMSHLVHWVFLAVYMYELNAELISHLHPPEQEISTDSCVFPFVYADGFHYSCISLHSDYDWCSLDFQFQGRWRYCTAQDPPKCIFPFQFKQKLIKKCTKEGYILNRSWCSLTENYNQDGKWKQCSPNNF
Protein: Beta-1 adrenergic receptor (Beta-1 adrenoreceptor) (Beta-1 adrenoceptor) (Beta-T) (P07700)
Organism: Meleagris gallopavo (Wild turkey)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. In dorsal pons neurons, involved in the regulation of sleep/wake behaviors (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P18090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18090}. Early endosome {ECO:0000250}. Note=Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MGDGWLPPDCGPHNRSGGGGATAAPTGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRKIDRCEGRFYGSQEQPQPPPLPQHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLVPDWLFVFFNWLGYANSAFNPIIYCRSPDFRKAFKRLLCFPRKADRRLHAGGQPAPLPGGFISTLGSPEHSPGGTWSDCNGGTRGGSESSLEERHSKTSRSESKMEREKNILATTRFYCTFLGNGDKAVFCTVLRIVKLFEDATCTCPHTHKLKMKWRFKQHQA
Protein: Small ribosomal subunit protein uS8m (37S ribosomal protein subunit S8, mitochondrial) (O74956)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS12m
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS15m
Sequence:
MQLHYVFSHLQNSFRARKSLASVPNCNSVLELCAVLYHQGFLSSIQRGDIHGPDALPTITTRQNVATRRLWLGLKYFEGKPVLHYIRAVSKPSRKVNLTPSELLQFAKGRKVSFVNGLEPAEVGIVETKHGIMSIDDAIKNNLGGNVICRVK
Protein: Tyrosine-protein kinase abl-1 (EC 2.7.10.2) (P03949)
Organism: Caenorhabditis elegans
Function: Functions downstream of migratory protein mig-13 and is involved in Q neuroblast migration during larval development. Recruited by mig-13 to the leading edge of Q neuroblasts and their descendents to signal downstream, likely to the wve-1 pathway, and direct migration along the anteroposterior body axis. Promotes germline cell apoptosis in response to oxidative, osmotic and heat shock stresses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27780040}. Cytoplasm {ECO:0000269|PubMed:27780040}. Note=Enriched at the leading edge compared to cytoplasm. Targeted to the leading edge of Q neuroblasts by mig-13. {ECO:0000269|PubMed:27780040}.
Interaction partners:
- SH3 domain-containing protein
- Cell death abnormality protein 2
- Ras-related protein ced-10
- Rho-GAP domain-containing protein
- UNC-34
- E3 ubiquitin-protein ligase CBL
- Yes-associated protein homolog 1
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- CED-5
- CRAL-TRIO domain-containing protein
Sequence:
MGHSHSTGKEINDNELFTCEDPVFDQPVASPKSEISSKLAEEIERSKSPLILEVSPRTPDSVQMFRPTFDTFRPPNSDSSTFRGSQSREDLVACSSMNSVNNVHDMNTVSSSSSSSAPLFVALYDFHGVGEEQLSLRKGDQVRILGYNKNNEWCEARLYSTRKNDASNQRRLGEIGWVPSNFIAPYNSLDKYTWYHGKISRSDSEAILGSGITGSFLVRESETSIGQYTISVRHDGRVFHYRINVDNTEKMFITQEVKFRTLGELVHHHSVHADGLICLLMYPASKKDKGRGLFSLSPNAPDEWELDRSEIIMHNKLGGGQYGDVYEGYWKRHDCTIAVKALKEDAMPLHEFLAEAAIMKDLHHKNLVRLLGVCTHEAPFYIITEFMCNGNLLEYLRRTDKSLLPPIILVQMASQIASGMSYLEARHFIHRDLAARNCLVSEHNIVKIADFGLARFMKEDTYTAHAGAKFPIKWTAPEGLAFNTFSSKSDVWAFGVLLWEIATYGMAPYPGVELSNVYGLLENGFRMDGPQGCPPSVYRLMLQCWNWSPSDRPRFRDIHFNLENLISSNSLNDEVQKQLKKNNDKKLESDKRRSNVRERSDSKSRHSSHHDRDRDRESLHSRNSNPEIPNRSFIRTDDSVSFFNPSTTSKVTSFRAQGPPFPPPPQQNTKPKLLKSVLNSNARHASEEFERNEQDDVVPLAEKNVRKAVTRLGGTMPKGQRIDAYLDSMRRVDSWKESTDADNEGAGSSSLSRTVSNDSLDTLPLPDSMNSSTYVKMHPASGENVFLRQIRSKLKKRSETPELDHIDSDTADETTKSEKSPFGSLNKSSIKYPIKNAPEFSENHSRVSPVPVPPSRNASVSVRPDSKAEDSSDETTKDVGMWGPKHAVTRKIEIVKNDSYPNVEGELKAKIRNLRHVPKEESNTSSQEDLPLDATDNTNDSIIVIPRDEKAKVRQLVTQKVSPLQHHRPFSLQCPNNSTSSAISHSEHADSSETSSLSGVYEERMKPELPRKRSNGDTKVVPVTWIINGEKEPNGMARTKSLRDITSKFEQLGTASTIESKIEEAVPYREHALEKKGTSKRFSMLEGSNELKHVVPPRKNRNQDESGSIDEEPVSKDMIVSLLKVIQKEFVNLFNLASSEITDEKLQQFVIMADNVQKLHSTCSVYAEQISPHSKFRFKELLSQLEIYNRQIKFSHNPRAKPVDDKLKMAFQDCFDQIMRLVDR
Protein: Break repair meiotic recombinase recruitment factor 1 (Pre-T/NK cell-associated protein 3B3) (Q0VDD7)
Organism: Homo sapiens (Human)
Function: Meiotic recombination factor component of recombination bridges involved in meiotic double-strand break repair. Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with and stabilization of the BRCA2:HSF2BP complex during meiotic recombination. Indispensable for the DSB repair, homologous synapsis, and crossover formation that are needed for progression past metaphase I, is essential for spermatogenesis and male fertility.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q6DIA7}. Note=During meiosis, recruited to chromosomes and localizes on recombination sites in a double-strand break-dependent manner. First appears on the chromosome axis at leptotene. Along with the progression of meiotic recombination, released from the axis to form bridge-like structures linking homolog axes before they are synapsed. Finally, located between synapsed homolog axes and on the synaptonemal complex (SC). {ECO:0000250|UniProtKB:Q6DIA7}.
Interaction partners:
- Heat shock factor 2-binding protein
Sequence:
MTKRKKLRTSGEGLCPPKPLKNPRLGDFYGDPQSSMLGCLHHPEEPEGKLGPVPSTQQHGEEPGKAVSSSPDEETGSPCRLLRQPEKEPAPLPPSQNSFGRFVPQFAKSRKTVTRKEEMKDEDRGSGAFSLETIAESSAQSPGCQLLVETLGVPLQEATELGDPTQADSARPEQSSQSPVQAVPGSGDSQPDDPPDRGTGLSASQRASQDHLSEQGADDSKPETDRVPGDGGQKEHLPSIDSEGEKPDRGAPQEGGAQRTAGAGLPGGPQEEGDGVPCTPASAPTSGPAPGLGPASWCLEPGSVAQGSPDPQQTPSRMGREGEGTHSSLGCSSLGMVVIADLSTDPTELEERALEVAGPDGQASAISPASPRRKAADGGHRRALPGCTSLTGETTGESGEAGQDGKPPGDVLVGPTASLALAPGSGESMMGAGDSGHASPDTGPCVNQKQEPGPAQEEAELGGQNLERDLEGFRVSPQASVVLEHREIADDPLQEPGAQQGIPDTTSELAGQRDHLPHSADQGTWADSLAVELDFLLDSQIQDALDASDFEAPPEQLFPSGNKPGPCWPGPSSHANGDPVAVAKAQPRTFVGIQASEASRMEDATNVVRGLIVELSNLNRLIMGTHRDLEAFKRLNYRKTKLGGKAPLPYPSKGPGNIPRGDPPWREL
Protein: Chloride intracellular channel Clic (Q9VY78)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26777142}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSEVESQQSQETNGSSKFDVPEIELIIKASTIDGRRKGACLFCQEYFMDLYLLAELKTISLKVTTVDMQKPPPDFRTNFEATHPPILIDNGLAILENEKIERHIMKNIPGGYNLFVQDKEVATLIENLYVKLKLMLVKKDEAKNNALLSHLRKINDHLSARNTRFLTGDTMCCFDCELMPRLQHIRVAGKYFVDFEIPTHLTALWRYMYHMYQLDAFTQSCPADQDIINHYKLQQSLKMKKHEELETPTFTTYIPIDISE
Protein: Protein bem46 (P54069)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Suppressor of bem1/bud5.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-galactose transporter homolog 1
- GDP-Man:Man
- Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit
- Seipin homolog
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Alpha-1,3/1,6-mannosyltransferase alg2
- Vacuolar protein sorting-associated protein 55
- Nucleus-vacuole junction protein 2
- UDP-N-acetylglucosamine transporter yea4
- Phosphatidyl-N-methylethanolamine N-methyltransferase
Sequence:
MAGSLSSAIFNVLKYSGMASLAVTLIALGFLYKYQKTLVYPSAFPQGSRENVPTPKEFNMEYERIELRTRDKVTLDSYLMLQSESPESRPTLLYFHANAGNMGHRLPIARVFYSALNMNVFIISYRGYGKSTGSPSEAGLKIDSQTALEYLMEHPICSKTKIVVYGQSIGGAVAIALTAKNQDRISALILENTFTSIKDMIPTVFPYGGSIISRFCTEIWSSQDEIRKIKKLPVLFLSGEKDEIVPPPQMVLLFGLCGSAKKKFHSFPKCTHNDTCLGDGYFQVIADFLAENDINTPAS
Protein: ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b) (P0ABA0)
Organism: Escherichia coli (strain K12)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit c
- ATP synthase epsilon chain
- ATP synthase subunit beta
- ATP synthase subunit alpha
- ATP synthase gamma chain
- ATP synthase subunit delta
- Inorganic pyrophosphatase
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL23
Sequence:
MNLNATILGQAIAFVLFVLFCMKYVWPPLMAAIEKRQKEIADGLASAERAHKDLDLAKASATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVAQAQAEIEAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL
Protein: Ferrochelatase (EC 4.98.1.1) (Q8ID58)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000607}.
Interaction partners:
- Protoporphyrinogen oxidase
- Protoheme IX farnesyltransferase, mitochondrial
- Uroporphyrinogen decarboxylase
- Holocytochrome c-type synthase
- Holocytochrome c-type synthase
- Delta-aminolevulinic acid dehydratase
- hydroxymethylbilane synthase
- Methyltransferase, putative
- ATP synthase-associated protein, putative
Sequence:
MDVQDFLNCNKLKISKEKISNLNKSKIGILITNLGSPEKLTYWSLYKYLSEFLTDPRVVKLNRFLWLPILYTFVLPFRSGKVLSKYKSIWIKDGSPLCVNTHNQCLALKKILNEKYNNKVVISYGMRYGERSIKKGLEYLQKENINKLLVLPLYPQSAECTVSSTLDCIGKNLKNWSNVPELRFISGYCLKDIFINTMKENIENYWELYGKSKKLIISYHSLPIRNVIQGDLYPFFCIESTKKLVKSLNLNKDDYILVFQSKIKGQQWVKPCIEDTIIRLAKQGYKQIDIVSPSFSSDCLETLEEIKIHYQQLFRKYSNGNLRYINCLNDTTIGIKLIMNLIEQNIIGWV
Protein: Protein STRUBBELIG-RECEPTOR FAMILY 1 (Leucine-rich repeat receptor kinase-like protein SRF1) (Q06BH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not essential for epidermal patterning and not redundant with STRUBBELIG.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein MEI2-like 3
Sequence:
MRSMRSGRDNNICFLGFLSFALISLPSLSLALTNPDDVAAINSLFLALESPLLPGWVASGGDPCGESWQGVLCNASQVETIILISANLGGELGVGLNMFTSLKAMDFSNNHIGGSIPSTLPVSLQNLFLSGNNFTGTIPESLSSLKSLSVMSLNNNLLSGKIPDVFQDLGLMINIDLSSNNLSGPLPPSMQNLSTLTSLLLQNNHLSGELDVLQDLPLKDLNVENNLFNGPIPEKLLSIPNFIKGGNLFNVTIAPSPSPETPPSPTSPKRPFFGPPSPNASAGHGQAHVRSPPSDHHPSRPTPQGKEDSFTSKRIIWISILGAFSFVVLALVCLLCGRKCLRKREDSEQLSKPHLTSEYGRAREGSRSNASMLPPSNTFNKDKEARPKERVGGASKLHGGAERSVGSESKQESHEIDMNGNAMDLMHPSSIPPIKRVIAKATEPAEASLKRTTSKSHGPLTAVKHFTVASLQQHTNSFSHENLIGTGMLGSVYRAELPGGKLFAVRKLDKKSPNHEEEGKFLELVNNIDRIRHANIVQLVGFCSEHSQRLLIHEYCRNGTLHDLLHIDDRLKIELSWNVRVRIALEAAKALEYLHEICDPPSIHRNFKSANILLDDDIRVHVSDCGLAPLISSGAVSQLSGQLLAAYGYGAPEFEYGIYTMKCDVYSFGVVMLELLTGRKSYDKKRDRGEQFLVRWAIPQLHDIDALAKMVDPSLKGDYPAKSLSHFADVISRCVQSEPEYRPLMSEVVQDLSDMIQREHRRNDSNGDNQYTGRR
Protein: D-Ala-D/L-Ala epimerase (EC 5.1.1.-) (Q11T61)
Organism: Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465)
Function: Catalyzes the epimerization of D-Ala-D-Ala to D-Ala-L-Ala. Has broad substrate specificity and catalyzes the epimerization of a variety of dipeptides containing an N-terminal Ala followed by a hydrophobic or polar residue, such as Val, Ser and Met (in vitro).
Interaction partners:
Sequence:
MIITQVELYKSPVKLKEPFKISLGILTHANNVIVRIHTASGHIGYGECSPFMTIHGESMDTAFIVGQYLAKGLIGTSCLDIVSNSLLMDAIIYGNSCIKSAFNIALYDLAAQHAGLPLYAFLGGKKDKIIQTDYTVSIDEPHKMAADAVQIKKNGFEIIKVKVGGSKELDVERIRMIREAAGDSITLRIDANQGWSVETAIETLTLLEPYNIQHCEEPVSRNLYTALPKIRQACRIPIMADESCCNSFDAERLIQIQACDSFNLKLSKSAGITNALNIIRLAEQAHMPVQVGGFLESRLGFTAAAHVALVSKTICYYDFDTPLMFEADPVRGGIVYQQRGIIEVPETAGLGAGYQKDYLSGLEKICIN
Protein: DNA primase (EC 2.7.7.-) (P17149)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011}. Note=Requires the presence of the primase associated factor to properly localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011}.
Interaction partners:
Sequence:
MTLVLFATEYDSAHIVANVLSQTPTDHCVFPLLVKHQVSRRVYFCLQTQKCSDSRRVAPVFAVNNETLQLSRYLAARQPIPLSALIASLDEAETQPLYRHLFRTPVLSPEHGGEVREFKHLVYFHHAAVLRHLNQVFLCPTSPSWFISVFGHTEGQVLLTMAYYLFEGQYSTISTVEEYVRSFCTRDLGTIIPTHASMGEFARLLLGSPFRQRVSAFVAYAVARNRRDYTELEQVDTQINAFRERARLPDTVCVHYVYLAYRTALARARLLEYRRVVAYDADAAPEAQCTREPGFLGRRLSTELLDVMQKYFSLDNFLHDYVETHLLRLDESPHSATSPHGLGLAGYGGRIDGTHLAGFFGTSTQLARQLERINTLSESVFSPLERSLSGLLRLCASLRTAQTYTTGTLTRYSQRRYLLPEPALAPLLERPLPVYRVHLPNDQHVFCAVASETWHRSLFPRDLLRHVPDSRFSDEALTETVWLHDDDVASTSPETQFYYTRHEVFNERLPVFNFVADFDLRLRDGVSGLARHTVFELCRGLRRVWMTVWASLFGYTHPDRHPVYFFKSACPPNSVPVDAAGAPFDDDDYLDYRDERDTEEDEDGKEDKNNVPDNGVFQKTTSSVDTSPPYCRCKGKLGLRIITPFPACTVAVHPSVLRAVAQVLNHAVCLDAELHTLLDPISHPESSLDTGIYHHGRSVRLPYMYKMDQDDGYFMHRRLLPLFIVPDAYREHPLGFVRAQLDLRNLLHHHPPHDLPALPLSPPPRVILSVRDKICPSTEANFIETRSLNVTRYRRRGLTEVLAYHLYGGDGATAAAISDTDLQRLVVTRVWPPLLEHLTQHYEPHVSEQFTAPHVLLFQPHGACCVAVKRRDGARTRDFRCLNYTHRNPQETVQVFIDLRTEHSYALWASLWSRCFTKKCHSNAKNVHISIKIRPPDAPVPPATAV
Protein: Uncharacterized protein YdcY (P64455)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YjbT
- Putative dehydratase subunit YjiM
- Orphan toxin OrtT
- UPF0509 protein YciZ
Sequence:
MSHLDEVIARVDAAIEESVIAHMNELLIALSDDAELSREDRYTQQQRLRTAIAHHGRKHKEDMEARHEQLTKGGTIL