wanglab/gogpt-training-data huggingface dataset:
Protein: Metalloreductase STEAP3 (EC 1.16.1.-) (Six-transmembrane epithelial antigen of prostate 3) (pHyde) (Q5RKL5)
Organism: Rattus norvegicus (Rat)
Function: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also mediates reduction of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP (By similarity). May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q8CI59}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- BCL2/adenovirus E1B interacting protein 3-like.
- Natural resistance-associated macrophage protein 2
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Transferrin receptor protein 1
- Ferroportin
- Ferrochelatase
Sequence:
MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKERLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICGDQLEAKHTVSEMARAMGFTPLDMGSLASAREVEAIPLRLLPSWKVPTLLALGLFVCFYAYNFIRDVLQPYIRKDENKFYKMPLSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYSFCLPLRRSHRYDLVNLAVKQVLANKSRLWVEEEVWRMEIYLSLGVLALGMLSLLAVTSIPSIANSLNWKEFSFVQSTLGFVALMLSTMHTLTYGWTRAFEENHYKFYLPPTFTLTLLLPCVIILAKGLFLLPCLSHRLTKIRRGWERDGAVKFMLPAGHTQGEKTSHV
Protein: Short-chain dehydrogenase/reductase ABA4 (EC 1.1.1.-) (Abscisic acid biosynthesis protein 4) (L7I518)
Organism: Pyricularia oryzae (strain Y34) (Rice blast fungus) (Magnaporthe oryzae)
Function: Short-chain dehydrogenase/reductase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity).
Interaction partners:
Sequence:
MGSIENPEIMASTMLHILPLAGKVYGITGGASGIGLATAQILSRRGATVCIADVDPKAMASAEVYFSGQSGAKYSITKVDISKRSEVNAWVDGIISQFGRLDGAANVAGVIGKIHGAVPVSEMDDDEWDKIVAVNLTGTMYCMRAQLRNIVDGGSIVNVASIHGLKGFANHAAYDASKHGVIGLTKAAAQENGAREIRVNAVAPGAIYTPLMQKNWDITGRPKDAPFDDPSAFRRQGTAMETGNVIAFLLGPDSTFVSGSVYSVDGAWI
Protein: Heat shock 70 kDa protein 4 (Heat shock 70-related protein APG-2) (Q2TFN9)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- STIP1 homology and U-box containing protein 1.
- Tight junction protein 1
- Stress induced phosphoprotein 1.
- BCL2 associated athanogene 1.
- Cellular tumor antigen p53
- GrpE protein homolog
- DnaJ heat shock protein family
- BCL2 associated athanogene 3.
- Alpha-synuclein
- DnaJ heat shock protein family
Sequence:
MSVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACISFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVEAEKSNLAYDIVQLPTGLTGIKVKYMEEERNFTTEQVTAMLLSKLKETAESVLKKPVVDCVVSVPCFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSSYQVSVCAFNRGKLKVLATAFDTTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLSQECEKLKKLMSANASDLPLSIECFMNDVDVSGTMNRGKFLEMCDDLLARVEPPLRSVLEQAKLRKEDIYAVEIVGGATRIPAVKEKISKFFGKELSTTLNADEAVTRGCALQCAILSPAFKVREFSITDVVPYSISLRWNSPAEEGSSDCEVFTKNHSAPFSKVLTFYRKEPFTLEAYYSSPQDLPYPDPAIAQFLVQKVTPQSDGSSSKVKVKVRVNVHGIFSVSSASLVEVLKFEENEEPMETDQNAKEEEKMQVDQEEPHAEEQQQQTPAENKAESEEMETSQAASKDKKMDQPPQAKKAKVKTSTVDLPIENQLLWQIDREMLNLYIENEGKMIMQDKLKKERNDAKNAVEEYVYEMRDKLSGEYEKFVSEDDRNSFTLKLEDTENWLYEDGEDQPKQVYVDKLAELKNLGQPIKMRFQESEERPKLFEELGKQIQQYMKVISSFKNKEDQYDHLDAADMLKVEKSTNEAMEWMNNKLNLQNKQSLTVDPVVKAKEIEAKIKELMSVCGPIISKPKPKVEPPKEEQKNAEQNGPVDGQGDSPGPQAAEQGTDTAVPSDSDKKLPEMDID
Protein: Uncharacterized protein, isoform B (Q8I934)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLHINPKDFVNFNSKNAEATMTIKSIATSAVTYKIQTTSPEKFRVRPRCGIIQPNQEATINIWLKSEHKLSDDSKDKFLVMAMVAPGGECGGADVTELWRSKSPTSADVEQHRLVCRFDENKSKAQLDCASKSSKASVDCSKKSGAGVDPATAMERQLAFTQNLQYVTLALLFLLFAGFGFLMYQQLGQHAATCPKATAYSCAKRK
Protein: Adenosine 3'-phospho 5'-phosphosulfate transporter 1 (PAPS transporter 1) (Putative MAPK-activating protein PM15) (Putative NF-kappa-B-activating protein 48) (Solute carrier family 35 member B2) (Q8TB61)
Organism: Homo sapiens (Human)
Function: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF-kappa-B and MAPK pathways.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12716889, ECO:0000269|PubMed:35325049}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sulfotransferase 4A1
- Nucleotide sugar transporter SLC35D1
- Solute carrier family 35 member D3
- Large ribosomal subunit protein eL15
- Nucleotide sugar transporter SLC35D2
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Beta-1,4-galactosyltransferase 7
- Exostosin-2
- Protein-tyrosine sulfotransferase 2
- Exostosin-like 3
Sequence:
MDARWWAVVVLAAFPSLGAGGETPEAPPESWTQLWFFRFVVNAAGYASFMVPGYLLVQYFRRKNYLETGRGLCFPLVKACVFGNEPKASDEVPLAPRTEAAETTPMWQALKLLFCATGLQVSYLTWGVLQERVMTRSYGATATSPGERFTDSQFLVLMNRVLALIVAGLSCVLCKQPRHGAPMYRYSFASLSNVLSSWCQYEALKFVSFPTQVLAKASKVIPVMLMGKLVSRRSYEHWEYLTATLISIGVSMFLLSSGPEPRSSPATTLSGLILLAGYIAFDSFTSNWQDALFAYKMSSVQMMFGVNFFSCLFTVGSLLEQGALLEGTRFMGRHSEFAAHALLLSICSACGQLFIFYTIGQFGAAVFTIIMTLRQAFAILLSCLLYGHTVTVVGGLGVAVVFAALLLRVYARGRLKQRGKKAVPVESPVQKV
Protein: Small ribosomal subunit protein uS7 (40S ribosomal protein S5) [Cleaved into: Small ribosomal subunit protein uS7, N-terminally processed (40S ribosomal protein S5, N-terminally processed)] (P46782)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS4, X isoform
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS6
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MTEWETAAPAVAETPDIKLFGKWSTDDVQINDISLQDYIAVKEKYAKYLPHSAGRYAAKRFRKAQCPIVERLTNSMMMHGRNNGKKLMTVRIVKHAFEIIHLLTGENPLQVLVNAIINSGPREDSTRIGRAGTVRRQAVDVSPLRRVNQAIWLLCTGAREAAFRNIKTIAECLADELINAAKGSSNSYAIKKKDELERVAKSNR
Protein: Chaperone protein DNAJ, putative (Q38E01)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PRP8 protein homologue
- U5 small nuclear ribonucleoprotein component, putative
- RNA helicase
- PRP1 splicing factor N-terminal domain-containing protein
- Uncharacterized protein
- Spliceosomal U5 snRNP-specific protein, putative
- Pretranslocation protein, alpha subunit, putative
- Small nuclear ribonucleoprotein E
- Sm protein F
- Small nuclear ribonucleoprotein SmD1
Sequence:
MVESGIGGSDESFISFCFAIVSVIVTIVYIPWVIRHVRSIIEYYTTPSKRQRMMNNPLEDMWKSIIYVPLVAAKILTEPSMLPVGARICIKEKHFFFTSLLPRFLRFIIRPKIFILWLWVVLFSSAMYVTLTFDAHAILGVSTTASTGEIKKAYRMLSRRYHPDHNKTEEARLIYVQVRRAYKALVDREAFEEEEAKNTHEFTVGVALPRFLTSREHDGLVLFGLLGILVAVPVAIWYNFRDQGGISQQLRHIQRGRERLESFLKHLGIPEDQKYVERRDSRRYLVRLLVSLGMLPPNTDENASLNLPSYPDFITRCVEIDKNITFLRNFFDDSDIEVLHEYLVKNGVRLLDEYDAAHLGHHQGEGTLQLASPTEYKVISYFLFLHIEEIDKALEELLEKVGSGVPSARKLMNLHEEVRDLLHLVFEGDNKQVKNHIQKLTTVPQRANDIVDAMGPEIEAVYKKMYKNYLQMQVGSKNEKRLLKASLRRL
Protein: Kv channel-interacting protein 4 (KChIP4) (A-type potassium channel modulatory protein 4) (Calsenilin-like protein) (Potassium channel-interacting protein 4) (Q6PHZ8)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6PIL6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6PIL6}. Cytoplasm {ECO:0000250|UniProtKB:Q6PIL6}. Peroxisome {ECO:0000250|UniProtKB:Q6PIL6}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- A-type voltage-gated potassium channel KCND2
- Voltage-gated potassium channel KCNC1
- A-type voltage-gated potassium channel KCND1
- A-type potassium channel modulatory protein KCNIP1
- Potassium voltage-gated channel subfamily A member 4
Sequence:
MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI
Protein: Yellow-emperor, isoform B (Q8IMS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALRLTTIALLHRAPLLVVPKLKATPPTRTLLLRKNLVPFLDDDPCVFSKKAVMHHWGAVPIIAISFLSFTAEVITWLIIALTRHDVSYTANSAHYECLETRSSLYYPAKYLKFMRFNQKCEVPQGLIQANQGDTAGPSFDDKKKK
Protein: Sec-independent protein translocase protein TATC, chloroplastic (Protein ALBINO AND PALE GREEN 2) (Protein TWIN-ARGININE TRANSLOCATION C) (Protein UNFERTILIZED EMBRYO SAC 3) (Q9SJV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:11526245}; Multi-pass membrane protein {ECO:0000305|PubMed:11526245}. Note=The N-terminus is located in the stroma. {ECO:0000250}.
Interaction partners:
- Sec-independent protein translocase protein TATA, chloroplastic
- Sec-independent protein translocase protein TATB, chloroplastic
- Peptide chain release factor APG3, chloroplastic
- Magnesium-chelatase subunit ChlI-1, chloroplastic
Sequence:
MSSTSTSSALIHHFRLTTRNLGSPTKQRCPYAVTFCNSWREAGLRYSVTQRRSKGFGPVSALNDDDSPTETTPGVGSAVEDRPPDSSEDRSSSVYEFLYPRKEELPDDKEMTIFDHLEELRERIFVSVLAVGAAILGCFAFSKDLIVFLEAPVKTQGVRFLQLAPGEFFFTTLKVSGYCGLLLGSPVILYEIIAFVLPGLTRAERRFLGPIVFGSSLLFYAGLAFSYWVLTPAALNFFVNYAEGVVESLWSIDQYFEFVLVLMFSTGLSFQVPVIQLLLGQVGVVSGDQMLSIWRYVVVGAVVAAAVVTPSTDPVTQMLLATPLLGLYLGGAWMVKLTGR
Protein: PRA1 family protein G1 (AtPRA1.G1) (Q9ZWD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- PRA1 family protein A2
- PRA1 family protein A1
- PRA1 family protein C
- PRA1 family protein H
- PRA1 family protein A3
Sequence:
MLAPGESVLIPAEEISLSAGDVISLSVHNLIASVSSYRPWWSEFLAFGSIDRPSSFSPAVSRVKLNLHHFAVNYVLLTAASITLFLIGDPMALVTVASFVAMWLLLYFYRDHPLVLYGRHISDRVIVFGLILGSLWALWFINSLQCLILGVVTSVLLCLVHAIIRNSDDLFVQEKDVVVPSNFLHWS
Protein: Synaptic vesicle glycoprotein 2B (Synaptic vesicle protein 2B) (Q8BG39)
Organism: Mus musculus (Mouse)
Function: Probably plays a role in the control of regulated secretion in neural and endocrine cells.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q63564}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q63564}. Note=Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin-secreting cells of the pancreas (By similarity). Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids (By similarity). {ECO:0000250|UniProtKB:Q63564}.
Interaction partners:
- Synaptic vesicle glycoprotein 2C
- Synaptic vesicle glycoprotein 2A
- Synaptotagmin-1
- Laminin subunit gamma-2
- Laminin subunit gamma-3
- Laminin subunit gamma-1
Sequence:
MDDYRYRDNYEGYAPSDGYYRSNEQNQEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKSKQTKMAPSRADGLGGQADLMAERMEDEEELAHQYETIIDECGHGRFQWTLFFVLGLALMADGVEIFVVSFALPSAEKDMCLSSSKKGMLGLIVYLGMMAGAFILGGLADKLGRKKVLSMSLAINASFASLSSFVQGYGAFLFCRLISGIGIGGSLPIVFAYFSEFLSREKRGEHLSWLGIFWMTGGIYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPATVSMVALKFMPESPRFLLEMGKHDEAWMILKQVHDTNMRAKGTPEKVFTVSHIKTPKQMDEFIEIQSSTGTWYQRWLVRFMTIFKQVWDNALYCVMGPYRMNTLILAVVWFTMALSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVHGATINFTMENQIHQHGKLVNDKFIKMYFKHVLFEDTFFDKCYFEDVTSTDTYFKNCTIESTTFYNTDLYKHKFINCRFINSTFLEQKEGCHMDFEEDNDFLIYLVSFLGSLSVLPGNIISALLMDRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKFGAILGNTIFASFVGITKVVPILLAAASLVGGGLIALRLPETREQVLM
Protein: Catalase-3 (EC 1.11.1.6) (Q42547)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Peroxisome {ECO:0000269|PubMed:25700484}.
Interaction partners:
- Glycolate oxidase 2
- Glycolate oxidase 3
- Peroxisomal
- Glycolate oxidase 1
- Peroxisomal
- Calcium-dependent protein kinase 8
- Catalase-1
- Catalase-2
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- Enoyl-CoA hydratase 2, peroxisomal
Sequence:
MDPYKYRPSSAYNAPFYTTNGGAPVSNNISSLTIGERGPVLLEDYHLIEKVANFTRERIPERVVHARGISAKGFFEVTHDISNLTCADFLRAPGVQTPVIVRFSTVVHERASPETMRDIRGFAVKFYTREGNFDLVGNNTPVFFIRDGIQFPDVVHALKPNPKTNIQEYWRILDYMSHLPESLLTWCWMFDDVGIPQDYRHMEGFGVHTYTLIAKSGKVLFVKFHWKPTCGIKNLTDEEAKVVGGANHSHATKDLHDAIASGNYPEWKLFIQTMDPADEDKFDFDPLDVTKIWPEDILPLQPVGRLVLNRTIDNFFNETEQLAFNPGLVVPGIYYSDDKLLQCRIFAYGDTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEINYYPSKFDPVRCAEKVPTPTNSYTGIRTKCVIKKENNFKQAGDRYRSWAPDRQDRFVKRWVEILSEPRLTHEIRGIWISYWSQADRSLGQKLASRLNVRPSI
Protein: Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1) (P21873)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Interaction partners:
Sequence:
MGVKTFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRMVYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYRDVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAGVALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNRFAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAINGEGPTLIETLCFRYGPHTMSGDDPTRYRSKELENEWAKKDPLVRFRKFLEAKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPFNLKEQYEIYKEKESK
Protein: High mobility group nucleosome-binding domain-containing protein 3 (Q9DCB1)
Organism: Mus musculus (Mouse)
Function: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MPKRKSPENTEGKDGTKLTKQEPTRRSARLSAKPVPPKPESKPRKTSAKKEPGTKISRGAKGKKEEKQEAGEEGTAPSANGDTKVEEAQRTESIEKEGE
Protein: LD35640p (P-element somatic inhibitor, isoform B) (A1ZAK7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDFQQQGINQSQALAQAIQRAKQIAAKIQPSQQGGGTAGPSPPSSGGGPGFKRINDDGDSGPESKRSLGSPEYANNSSNMSSGSGGGGGGGGGPGGASITQAIAQAAAVAARLAASAGTSCEEQIRLPESVAGAFMGRSSNDTITHIQAESGVKVQVMQDQDRVIMLRGQRDTVTKGREMIQNMANRAGGGQVEVLLTINMPPPGPSGYPPYQEIMIPGAKVGLVIGKGGDTIKQLQEKTGAKMIIIQDGPNQELIKPLRISGEAQKIEHAKQMVLDLIAQKDAQGQQQGGRGGGGGGGGPGMGFNNFNNGNGGESTEVFVPKIAVGVVIGKGGDMIRKIQTECGCKLQFIQGKNDEMGDRRCVIQGTRQQVDDAKRTIDGLIENVMQRNGMNRNGNGGGGGPGGDSGNSNYGYGYGVNHAQGGREEITFLVPASKCGIVIGRGGETIKLINQQSGAHTEMDRNASNPPNEKLFKSKGTTDQVEAARQMISEKINMELNVISRKPIGGGPGGGGGNSGGGQNNSHHNQQQGGYGGQNQMQGGDPNSGAGYQQQPWGGPYGQQGWDPSGQQQQMAMANQGGSAAGGASGGQDYSAQWIEYYKQMGCHREAEMIEQQMKAKQAGGSSGPVQQQQPQQQQQSQQQTGGAGAGGADYSAQWAEYYRSVGKIEEAEAIEKTLKNKQNGSGGQSSTPNPSQGGSGQQQPNPAAAAAAAAAAAAAAGGYGQSMTPTQYAQYSQYYAAAAAAGGQPQGAPQPGGGQSGGPPGNYPGNYPGAGYGGYPGAPGQQQQKSHKNDNH
Protein: Calcium-dependent protein kinase 3 (EC 2.7.11.1) (Calcium-dependent protein kinase isoform CDPK6) (AtCDPK6) (Q42479)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger. Functions in abscisic acid (ABA) regulation of guard cell S-type anion- and Ca(2+)-permeable channels and stomatal closure.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12913141}. Nucleus {ECO:0000269|PubMed:12913141}.
Interaction partners:
- Guard cell S-type anion channel SLAC1
- Ricin B-like lectin EULS3
- LRR receptor-like serine/threonine-protein kinase GHR1
- Calcineurin B-like protein 1
- Respiratory burst oxidase homolog protein D
- Respiratory burst oxidase homolog protein F
- Calcium-binding protein CP1
- S-type anion channel SLAH3
- Respiratory burst oxidase homolog protein B
- Calcineurin B-like protein 9
Sequence:
MGHRHSKSKSSDPPPSSSSSSSGNVVHHVKPAGERRGSSGSGTVGSSGSGTGGSRSTTSTQQNGRILGRPMEEVRRTYEFGRELGRGQFGVTYLVTHKETKQQVACKSIPTRRLVHKDDIEDVRREVQIMHHLSGHRNIVDLKGAYEDRHSVNLIMELCEGGELFDRIISKGLYSERAAADLCRQMVMVVHSCHSMGVMHRDLKPENFLFLSKDENSPLKATDFGLSVFFKPGDKFKDLVGSAYYVAPEVLKRNYGPEADIWSAGVILYILLSGVPPFWGENETGIFDAILQGQLDFSADPWPALSDGAKDLVRKMLKYDPKDRLTAAEVLNHPWIREDGEASDKPLDNAVLSRMKQFRAMNKLKKMALKVIAENLSEEEIIGLKEMFKSLDTDNNGIVTLEELRTGLPKLGSKISEAEIRQLMEAADMDGDGSIDYLEFISATMHMNRIEREDHLYTAFQFFDNDNSGYITMEELELAMKKYNMGDDKSIKEIIAEVDTDRDGKINYEEFVAMMKKGNPELVPNRRRM
Protein: Transcription factor dpl-1 (Q22703)
Organism: Caenorhabditis elegans
Function: Synthetic multivulva class B (synMuvB) protein. SynMuvB proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that represses transcription. May also negatively regulate vulval development in association with other SynMuv class B proteins such as lin-15A. Can stimulate E2F-dependent transcription. Plays a role in negatively regulating the progression through the G1 phase of the cell cycle during postembryonic development, most likely by acting as a transcriptional repressor in association with the cell cycle regulatory factor efl-1 and the transcriptional repressor lin-35, but may also act as a positive regulator of cell cycle entry. Involved in the regulation of intestinal cell division during postembryonic development, most likely in complex with efl-1 and lin-35. Promotes germ cell programmed cell death, probably together with efl-1, by positively regulating the expression of the apoptosis proteins ced-3 and ced-4. In particular, positively regulates the expression of ced-4 in response to starvation. Its role in programmed cell death may be in conjunction with cell cycle regulatory factor efl-1 and the synthetic multivulva class B proteins lin-35, lin-37 and lin-52, and is independent of the ced-1, ced-8 and ced-9 pathways.
Subcellular location: Nucleus {ECO:0000269|PubMed:11463372, ECO:0000269|PubMed:23347407}.
Interaction partners:
- E2F/DP family winged-helix DNA-binding domain-containing protein
- Retinoblastoma-like protein homolog lin-35
- E2F_TDP domain-containing protein.
- Uncharacterized protein
- Protein lin-9
- Protein lin-52
- Protein lin-54
- Probable histone-binding protein lin-53
- Transcription factor efl-3
- BSD domain-containing protein
Sequence:
MNPTNYDPRIGQPAQSRPQVSLSMGRRIVQMPTGLPRSYQDESHNEPVGWDEPSGVGGSSGAGGQQSDKPTGLRHFSTKVCEKVKEKGLTNYNEVADELVADYFQNNLIKQIDVVKQEYDMKNIRRRVYDALNVLLAMNIITKSKKDIRWIGLPASASQEISRLEEEKSRREASISSKKQALEEMVLQIVSYKNLVERNRKNEHKNGRPENDTVLHLPFLIINTDKEANVECSVSSDKSEFLFSFDKKFEIHDDFEILKKLNLACSLETTNPTAEEVKTAKSFLPTLHQHYVDEIIANRKKVEAEKEEKRKQQQLIADQMSMNLSQAQYVEPTSSLAQMSYSSRFNRQLQEHLINDGSEDRSAAAGIMERDYDMDKNVNQGSASRGPMYNTYSPQKIRAQVNTPLQVPPVTKRYYVQKTQGPMKHDMTPVVRTVNRPYSTVPPDRRLSTGATSVNSGPVKYYVPQGHQPMHQPVGQRYRVRPQQPQMSHMGQPHQVQQRVVYPAGSISGHQLQPGQRIVTQRIVAPGGPHPPGTIVRKVIRKIVVNNPKQSPAQQVIQKKMMEQDMCTFERKTEQPMTSAQAAALIQHPQPEEYDYFQ
Protein: Chromatin component KLETT (Q9GND0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSVGQRVAFLSTHWTSPLQNPNATVKPLIQMPLQAANVQEQQSSPVALYPTSASPVAVQSPQDAFLAVQSPGAPAPVQLANSSDQQNNPDADAIASKLPMPVIIKEEPISVNDEPSVDNIEDNTSASTSASGIGGKIPFKKIFQKRKKSSERTRDKKLRQNRQVRKSMLPKNALMALNEVKGVTISDFTIDSNTDGGFTAVVTVNSNQYEGKGTSKMTAKNAACEKAWRDFIIAKMTPKPPRIHQVEMGSEPMDINEDEADAPDDDLPMLNLASFAIYKLFAEWELEGYVLPEMHPSANAAQQAGGDAGTPVPPLPKEPKKPPVRTELPSGWETMHPATILCIMRPGLNYVDYGSSGDKTNGMQHLGIMVDNQEFHANGRSKKIARRNVAVKVCNSLFGTNFTYTDTT