wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase F(0) complex subunit a (F-ATPase protein 6) (Proton-conducting channel, ATP synthase F(0) complex subunit a) (P00847)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- ATP synthase F
- Cytochrome c oxidase subunit 3
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSIHNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT
Protein: Amyloid beta precursor like protein 1 (cDNA FLJ56046, highly similar to Amyloid-like protein 1 (APLP)(APLP-1)) (B7Z4G8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MEAVCGAWGRGLVLGVSVLGSKEPGDPHANAPRALTVLSTSIQAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRSGSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPGTPDPSGTAVGDPSTRSWPPGSRVEGAEDEEEEESFPQPVDDYFVEPPQAEEEEETVPPPSSHTLAVVGKVTPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTHLQVIEERVNQSLGLLDQNPHLAQELRPQIQELLHSEHLGPSELEAPAPGGSSEDKGGLQPPDSKDDTPMTLPKGSTEQDAASPEKEKMNPLEQYERKVNASVPRGFPFHSSEIQRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP
Protein: Phospho-2-dehydro-3-deoxyheptonate aldolase (EC 2.5.1.54) (Q9SK84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000256|RuleBase:RU363071}.
Interaction partners:
- 3-dehydroquinate synthase, chloroplastic
- Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic
- Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
- Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic
- 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic
- 3-phosphoshikimate 1-carboxyvinyltransferase
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- Shikimate kinase 2, chloroplastic
- Shikimate kinase 1, chloroplastic
Sequence:
MALMNGSMNLSSVKSSMINHRQPNFSSAVSRPTSFRISAVQTDPKTPAASSASAATTTPATLTKPVGVNVGKGKWAPESWRTKKALQQPDYPDLAALEAVLETIEAFPPIVFAGEARLLEERLGQAAMGEAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQVPVVKVGRMAGQFAKPRSDSFEEKDGVKLPSYRGDNINGDAFDSKSRIPDPQRMIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTERSEQGDRYRELANRVDEALGFMHAAGLTLDHPIMQTTDFWTSHECLLLPYEQSLTRLDSTSGLYYDCSAHMIWVGERTRQLDGAHVEFLRGVANPLGIKVSDKMDPKELVKLIEILNADNKPGRITIITRMGAENMRVKLPHLIREVRRAGQIVTWVSDPMHGNTIKAPCGLKTRPFDAILAEVRAFFDVHEQEGSHPGGIHLEMTGQNVTECIGGSRTVTFDDLGSRYHTHCDPRLNASQSLELSFIIAERLRKRRIKSQKAFAL
Protein: Splicing factor 45 (45 kDa-splicing factor) (RNA-binding motif protein 17) (Q96I25)
Organism: Homo sapiens (Human)
Function: Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia.
Subcellular location: Nucleus {ECO:0000269|PubMed:9731529}.
Interaction partners:
- ATP-dependent RNA helicase DHX15
- Splicing factor 3B subunit 1
- SURP and G-patch domain-containing protein 1
- U2 snRNP-associated SURP motif-containing protein
- Calcium homeostasis endoplasmic reticulum protein
- Ataxin-1
- U2 small nuclear ribonucleoprotein A'
- Splicing factor 3A subunit 3
- Splicing factor 3A subunit 1
- Splicing factor 1
Sequence:
MSLYDDLGVETSDSKTEGWSKNFKLLQSQLQVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIVDTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDATEKDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDEDLEVETKEECEKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGRVVKACFYNLDKFRVLDLAEQV
Protein: Bacterial microcompartment shell vertex protein PduN (Bacterial microcompartment protein pentamer) (BMC-P) (Propanediol utilization protein PduN) (Q9XDN3)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Probably forms vertices in the shell of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:21239588}.
Interaction partners:
- Bacterial microcompartment shell protein PduK
- Bacterial microcompartment shell protein PduT
- Bacterial microcompartment shell protein PduJ
- Bacterial microcompartment shell protein PduA
- Bacterial microcompartment shell protein PduU
- Bacterial microcompartment shell protein PduB
- Propanal dehydrogenase
- Bacterial microcompartment assembly protein PduM
- Propanediol dehydratase large subunit
- Cobalamin reductase PduS
Sequence:
MHLARVTGAVVSTQKSPSLIGKKLLLVRRVSADGELPASPTSGDEVAVDSVGAGVGELVLLSGGSSARHVFSGPNEAIDLAVVGIVDTLSC
Protein: Kinesin-like protein KIF18A (Q91WD7)
Organism: Mus musculus (Mouse)
Function: Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression (By similarity).
Subcellular location: Cell projection, ruffle {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Interaction partners:
- Centromere-associated protein E
- Kinesin-like protein KIF11
- Kinesin-like protein KIF2C
- Kinetochore protein Nuf2
- Kinesin-like protein KIF14
- Protein regulator of cytokinesis 1
- Disks large-associated protein 5
- Mitotic spindle assembly checkpoint protein MAD2A
- Kinesin-like protein KIF23
- Cell division cycle protein 20 homolog
Sequence:
MSGTEEDLCHRMKVVVRVRPENTKEKAVQFCKVVHVVDKHILSFDPKQEEISFFHRKKTTNFDITKRQNKDLKFVFDAVFDETSTQMEVFEHTTKPILHSFLNGYNCTVFAYGATGSGKTHTMLGSAAEPGVMYLTMLDLFKCIDEIKEEKECSTAVSYLEVYNEQIRDLLTNSGPLAVREDSQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDVNAVSSRSHAVFQIYLRQQDKTASINQNVRIAKMSLIDLAGSERASVSGAKGSRFVEGTNINKSLLALGNVINALANTKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLKYANRAKEIKSSLKSNVLNLNSHISQYVKICNMQKAEILMLKEKLKAYEEQKALSDRNDCAKLVHSNPEDRETERFQEILNCLFQNREGIRQEYLKLEMLLKANALKSSYHQQCHKQIEMMCSEDKVEKATCKRDHRLEKLKTNSCFLEKKKEEVSKQFDENTNWLHRVENEMRLLGQNGDIPEALNKELHCHHLHLQNKELKTQMAHMTALACLQEQQHKQTEAVLNALLPVLRKQYWKLKETGLSNAAFDSDFKDIEHLVERKKVVAWADQTNEHSNRNDLPGISLLMTFPQLEPIQSISCCTSVSDPNVLKLTPQRRTRRKIIPSPLKVQHTQKSALSESTQLNDSFSKELQPIVYTPEDCKKAQDLFPSLTRTSSQSANVMNDNSQKALCRIESPLSRTECKQGLYSTSTLCDSIRGLKNKWPEQEPLASSKSSVHRIESSSFSTKDSMPESAGVPSYMAMTTAAKRKWKQMSSTSNASIKSDESCGFAKRIRRDNSSVKPMQENRLKVGYKRNTNKTNSNMLRKFRRNTSKENVQ
Protein: Protein chibby homolog 2 (Spermatid-associated protein) (Q8NA61)
Organism: Homo sapiens (Human)
Interaction partners:
- DNA mismatch repair protein Mlh1
- Sperm annulus positionning complex subunit Chibby3
Sequence:
MSPLECSECFGDQLLHRTYTWQLTLHSRPNYTRKRDTRSESLEIPISVVLPQRGTAEPFPRLHNLYSTPRCAQQAALPRLSRRMASQHSYPLNRFSSVPLDPMERPMSQADLELDYNPPRVQLSDEMFVFQDGRWVNENCRLQSPYFSPSASFHHKLHHKRLAKECMLQEENKSLREENKALREENRMLSKENKILQVFWEEHKASLGREESRAPSPLLHKDSASLEVVKKDHVALQVPRGKEDSTLQLLREENRALQQLLEQKQAYWAQAEDTAAPAEESKPAPSPHEEPCSPGLLQDQGSGLSSRFEEPKGPPARQEDSKELRALRKMVSNMSGPSGEEEAKVGPGLPDGCQPLQLLREMRQALQALLKENRLLQEENRTLQVLRAEHRGFQEENKALWENNKLKLQQKLVIDTVTEVTARMEMLIEELYAFMPARSQDPKKPSRV
Protein: Ephrin B3 (G3V7D4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- receptor protein-tyrosine kinase
- receptor protein-tyrosine kinase
- Ephrin type-B receptor 1
- Ephrin type-B receptor 6
- Ephrin type-B receptor 3
- Ephrin type-B receptor 4
- Cytoplasmic protein
- Regulator of G-protein signaling 3
- Ephrin type-A receptor 1
- Ephrin-B1
Sequence:
MGGPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVGGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSQEPGKDSIPGDPNSNATSRGAEGPLPPPSMPAVAGAAGGLALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGAADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV
Protein: Carboxysome shell protein CcmK4 (Carbon dioxide-concentrating mechanism protein CcmK4) (P73407)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: A probably minor shell protein component of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. The central pore probably regulates metabolite flux, as might the gaps between assembled homohexamers. Homohexamers make sheets that probably form the facets of the polyhedral carboxysome (Probable). This subunit probably makes both homohexamers and heterohexamers with CcmK3 (Probable).
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000305|PubMed:16081736, ECO:0000305|PubMed:17993516, ECO:0000305|PubMed:19844993}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000305|PubMed:17993516}.
Interaction partners:
- Carboxysome shell vertex protein CcmL
- Carboxysome assembly protein CcmM
- Carboxysome assembly protein CcmN
- Ribulose bisphosphate carboxylase small subunit
- Ribulose bisphosphate carboxylase large chain
- Carboxysome shell protein CcmK3
Sequence:
MSAQSAVGSIETIGFPGILAAADAMVKAGRITIVGYIRAGSARFTLNIRGDVQEVKTAMAAGIDAINRTEGADVKTWVIIPRPHENVVAVLPIDFSPEVEPFREAAEGLNRR
Protein: Cystatin-8 (Cystatin-related epididymal spermatogenic protein) (Cystatin-related epididymal-specific protein) (P32766)
Organism: Mus musculus (Mouse)
Function: Performs a specialized role during sperm development and maturation.
Subcellular location: Secreted.
Interaction partners:
- Cystatin E2
- Cystatin-12
Sequence:
MAKPLWLSLILFIIPVALAVGVDQSKNEVKAQNYFGSINISNANVKQCVWFAMKEYNKESEDKYVFLVDKILHAKLQITDRMEYQIDVQISRSNCKKPLNNTENCIPQKKPELEKKMSCSFLVGALPWNGEFNLLSKECKDV
Protein: NAD(+) kinase (EC 2.7.1.23) (A0A8I5ZN26)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEMEQEKMNLSKELNPDSASYNCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKIRDASLLQPFKELCIYLMEENNMIVYVEKKVLEDPAIVGDENFGPVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFNFENFQSQVNQVIEVRSRLKVRVVKEPRDKKTAIHNGLSENGLDTEGGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMVHPNVPAIMVTPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVCDPVSDWFESLAQCLHWNVRKKQAHFPEDEEDQDEEDS
Protein: H2-M beta chain (Q7JFR0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
GGFVAHVESTCVLNDAGTPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISNILNEQESLIHRLQNGLQDCATHTQPFWDVLTHRTRAPSVRVAQTTPFNTREPVMLACYVWGFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDW
Protein: Protein LSD1 (Protein LESION SIMULATING DISEASE 1) (OsLSD1) (Putative zinc finger LSD1) (Q0J7V9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Negative regulator of programmed cell death and hypersensitive response (HR). Positive regulator of callus differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15915636}.
Interaction partners:
- ESCRT-related protein CHMP1
- Os07g0479400 protein
- Os03g0108400 protein
- Os02g0596500 protein
- Os01g0103000 protein
- Os05g0102900 protein
- Os02g0159900 protein
- Os01g0141300 protein
- Os01g0141100 protein
- Os07g0490700 protein
Sequence:
MHLSAGFLSCRERKGDFSCLTAARICEASTSDAVVQAAGTAMPVPLAPYPTPPVPFTPPNGAQSQLVCSGCRNLLMYPAGATSVCCAVCSTVTAVPAPGTEMAQLVCGGCHTLLMYIRGATSVQCSCCHTVNLAMEANQVAHVNCGNCRMLLMYQYGARSVKCAVCNFVTSVGASPGTDQKPSS
Protein: dTDP-4-dehydro-6-deoxyglucose reductase (EC 1.1.1.266) (dTDP-4-dehydro-6-deoxy-D-glucose reductase) (dTDP-4-keto-6-deoxyglucose reductase) (dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase) (Q6E7F2)
Organism: Escherichia coli
Function: Catalyzes the stereospecific reduction of the C-4 keto group of dTDP-4-dehydro-6-deoxy-D-glucose, leading to dTDP-D-fucopyranose. This is a step in the biosynthesis of D-fucofuranose, a component of E.coli O52 O antigen. Is more efficient using NADH than NADPH as cosubstrate.
Interaction partners:
Sequence:
MDARKNGVLITGGAGFIGKALITEMVERQIPLVSFDISDKPDSLPELSEYFNWYKFSYLESSQRIKELHEIVSRHNIKTVIHLATTMFPHESKKNIDKDCLENVYANVCFFKNLYENGCEKIIFASSGGTVYGKSDTPFSEDDALLPEISYGLSKVMTETYLRFIAKELNGKSISLRISNPYGEGQRIDGKQGVIPIFLNKISNDIPIDIIGSIESKRDYIYISDLVQAFMCSLEYEGHEDIFNIGSGESITLKKLIETIEFKLNKKAVIGFQDPIHTNANGIILDIKRAMAELGWRPTVVLDDGIDKLIKSIRCK
Protein: Probable aminotransferase gliI (EC 2.6.1.-) (Gliotoxin biosynthesis protein I) (Q4WMJ9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Probable aminotransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Interaction partners:
- Acetylglutamate kinase, putative
- Multifunctional tryptophan biosynthesis protein
Sequence:
MPSETITPLLAHRARTNIQWFTHKHMRQVSRLNAKQHRVNMMTAENWSIRDELVDQYKTLFAQHLSPRHLSYADGMGGDAELLQAAADFFNRVFAAHSRVQPAHLVVGAGCSSLLENLLYDICEPGEGVLIETPFWGGFETSFVLRSNVTAVHVRPPCHGNGSADLDRLVSAYIEAYERALRQAPCRIKAILVCNPHNPCGHIYPPRVIQALLQFAQRHDLFYISDEIYALSTLDEQTAFTSVLSIDVAALGVDLARVFTLYSISKDLGSSGLRLGFGITQAHPDLRLSLAISNHSRVSTFTSLVITALLHDPEAATAILHQNRAALQRSAKLISDFLAFHQIPFVPPAAGVYVWARLGWRSSSRPGDEPSWDEEARLNDRFEAAGVSVGAGQGYCASEPGWFRITFAIPREELVAGLRRIEQVVGMEGQKWTAI
Protein: Histone PARylation factor 1 (Q9NWY4)
Organism: Homo sapiens (Human)
Function: Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response. Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins. Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. HPF1 acts by completing the active site of PARP1 and PARP2: forms a composite active site composed of residues from HPF1 and PARP1 or PARP2. While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains. HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1.
Subcellular location: Chromosome {ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:32939087}. Nucleus {ECO:0000269|PubMed:27067600}. Note=Localizes to DNA damage sites; chromatin localization is dependent on PARP1 and PARP2. {ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:32939087}.
Interaction partners:
- Poly [ADP-ribose] polymerase 2
- Poly [ADP-ribose] polymerase 1
- Histone H2A type 1-C
- Histone H2B type 1-J
- Histone H2B type 1-K
- Histone H2B type F-S
- ADP-ribosylhydrolase ARH3
- Poly
Sequence:
MVGGGGKRRPGGEGPQCEKTTDVKKSKFCEADVSSDLRKEVENHYKLSLPEDFYHFWKFCEELDPEKPSDSLSASLGLQLVGPYDILAGKHKTKKKSTGLNFNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSPDEFPVYVGINEAKKNCIIVPNGDNVFAAVKLFLTKKLREITDKKKINLLKNIDEKLTEAARELGYSLEQRTVKMKQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKTIVEAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEEHLANRSQENIDQLAA
Protein: Protein single-minded (P05709)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord. Required to correctly specify the formation of the central brain complex, which controls walking behavior. Also required for correct patterning of the embryonic genital disk and anal pad anlage. Plays a role in synapse development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:3345560}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator homolog
Sequence:
MTNHRRVRKDCYESRLHDIAKTCAMKEKSKNAARTRREKENTEFCELAKLLPLPAAITSQLDKASVIRLTTSYLKMRQVFPDGLGEAWGSSPAMQRGATIKELGSHLLQTLDGFIFVVAPDGKIMYISETASVHLGLSQVELTGNSIFEYIHNYDQDEMNAILSLHPHINQHPLAQTHTPIGSPNGVQHPSAYDHDRGSHTIEIEKTFFLRMKCVLAKRNAGLTTSGFKVIHCSGYLKARIYPDRGDGQGSLIQNLGLVAVGHSLPSSAITEIKLHQNMFMFRAKLDMKLIFFDARVSQLTGYEPQDLIEKTLYQYIHAADIMAMRCSHQILLYKGQVTTKYYRFLTKGGGWVWVQSYATLVHNSRSSREVFIVSVNYVLSEREVKDLVLNEIQTGVVKREPISPAAQAAQAAQAAQAAQAAQAAQAAQAAQAAQAAHVAQAVQAQVVVVPQQSVVVQPQCAGATGQPVGPGTPVSLALSASPKLDPYFEPELPLQPAVTPVPPTNNSSSSSNNNNGVWHHHHVQQQQQSGSMDHDSLSYTQLYPPLNDLVVSSSSSVGGGTASSAGGGSSASASSSGVYSTEMQYPDTTTGNLYYNNNNHYYYDYDATVDVATSMIRPFSANSNSCSSSSESERQLSTGNASIVNETSPSQTTYSDLSHNFELSYFSDNSSQQHQHQQQQQHLMEQQHLQYQYATW
Protein: Mitogen-activated protein kinase mpkC (MAP kinase C) (EC 2.7.11.24) (Q4WUN7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Mitogen-activated protein kinase required for growth on media where sorbitol or mannitol is the sole carbon source.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26878695, ECO:0000269|PubMed:27538790}. Nucleus {ECO:0000269|PubMed:26878695, ECO:0000269|PubMed:27538790}. Note=Translocates to the nucleus upon osmotic stress and cell wall damage. {ECO:0000269|PubMed:26878695, ECO:0000269|PubMed:27538790}.
Interaction partners:
- Basic leucine zipper
- mitogen-activated protein kinase kinase
- protein-tyrosine-phosphatase
- Protein phosphatase 2C, putative
- Mitogen-activated protein kinase sakA
- Protein arginine N-methyltransferase
- Transcription factor
- High osmolarity signaling protein sho1
- F-box domain-containing protein
- Calcium/calmodulin-dependent protein kinase, putative
Sequence:
MAEFVRAEVLGTKFEYTTRYVNPQPIGMGSFGLVCSAFDQITQQPVALKKIMKPFDSSSLAKRTYREIRLLKYLRHENLICMRDIFISPLEDIYIATELLGTDLGRLLSIKPLDSKFSQYFIYQILRGLKYIHSANVIHRDLKPTNILINENCDLKICDFGLARLQEPQMTGYVATRYYRAQEIMLTWQRYGVQVDVWSAGCILAEMLRRKPLFPGKDHVHQFHLITNILGNPPDAVIEKITSKNTVNFVKSLPSREPRDLSTVVPKDTDFDAIDLLKKMLVIDPDTRISAQDALRYPYLAPYHDPTDEPVASGPFDWSFDSADFPKETWKIMIYSEVLDYLNVDNPADPAPFDPSTPFDPSALEREFSEFLSDSGQI
Protein: L-type lectin-domain containing receptor kinase V.5 (Arabidopsis thaliana lectin-receptor kinase a1) (Ath.lecRK1) (AthlecRK-a1) (LecRK-V.5) (EC 2.7.11.1) (Q96285)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Confers resistance to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici, but confers susceptibility to the pathogenic bacteria Pseudomonas syringae.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10350082}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Protein kinase PINOID 2
- Concanavalin A-like lectin family protein
- Concanavalin A-like lectin family protein
- Concanavalin A-like lectin family protein
Sequence:
MSRELIILCQPILVLFLTLFYNSHGYFVSQGSVGIGFNGYFTLTNTTKHTFGQAFENEHVEIKNSSTGVISSFSVNFFFAIVPEHNQQGSHGMTFVISPTRGLPGASSDQYLGIFNKTNNGKASNNVIAIELDIHKDEEFGDIDDNHVGININGLRSVASASAGYYDDKDGSFKKLSLISREVMRLSIVYSQPDQQLNVTLFPAEIPVPPLKPLLSLNRDLSPYLLEKMYLGFTASTGSVGAIHYLMGWLVNGVIEYPRLELSIPVLPPYPKKTSNRTKTVLAVCLTVSVFAAFVASWIGFVFYLRHKKVKEVLEEWEIQYGPHRFAYKELFNATKGFKEKQLLGKGGFGQVYKGTLPGSDAEIAVKRTSHDSRQGMSEFLAEISTIGRLRHPNLVRLLGYCRHKENLYLVYDYMPNGSLDKYLNRSENQERLTWEQRFRIIKDVATALLHLHQEWVQVIIHRDIKPANVLIDNEMNARLGDFGLAKLYDQGFDPETSKVAGTFGYIAPEFLRTGRATTSTDVYAFGLVMLEVVCGRRIIERRAAENEEYLVDWILELWENGKIFDAAEESIRQEQNRGQVELVLKLGVLCSHQAASIRPAMSVVMRILNGVSQLPDNLLDVVRAEKFREWPETSMELLLLDVNTSSSLELTDSSFVSHGR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I5ZYG3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRNTSPRAISRADRERKVSMRLHRGAPANVSSSDLTGRQEVSRIAASQVRTRMKGPLAKASSG
Protein: tRNA-intron lyase (EC 4.6.1.16) (Q8IP11)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- tRNA splicing endonuclease subunit 54
- tRNA-splicing endonuclease subunit Sen34
- tRNA splicing endonuclease subunit 15, isoform A
Sequence:
MQFTFECKRKRCFNKNANFTPLPSGQDGERYKGRFTGLSVEIVDPEQAKSLHDNGCFGKGSKSRGGPASGDENETLFLGMEESCFLAHYLNVLDITNSAGYLMDFCMFVEVAKEHNEKFVENLASYVYLKSKNWVIKSGIKFGGDFLIYKQSPRLYHASFLVIVQKPGDTDHYQSKNLKGVQRVAETSDKDVLLLTVQPPKKISSSRDLQEATVTETIVRRFNYLTFVQSKQQ
Protein: Prolyl 4-hydroxylase subunit alpha 2 (E7ERI1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYH