wanglab/gogpt-training-data huggingface dataset:
Protein: Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A) (xFEN-1a) (P70040)
Organism: Xenopus laevis (African clawed frog)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
Sequence:
MGIHGLAKLIADVAPAAIKEHDIKSYFGRKVAVDASMCIYQFLIAVRQDGNTLQNEEGETTSHLMGMFYRTIRMVEHGIKPVYVFDGKPPQMKSGELAKRSERRAEAEKLLEAAEEAGEVENIEKFTKRLVKVTKQHNEECKKLLTLMGIPYVDAPCEAEATCAALVKAGKVYAAATEDMDALTFGTPVLLRHLTASEAKKLPIQEFHLNRVIQDIGITHEQFVDLCILLGSDYCETIRGIGPKRAIDLIRQHKTIDEIIDNIDLKKYPVPENWLHKEAKHLFLEPEVVDTDITELKWIEPDEEGLVAFMCGEKQFSEDRIRNGAKKLAKNRQGSTQGRLDDFFKVTGSVSSTKRKEAESKGSAKKKAKTGGTPAGKFKRGK
Protein: Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (Q05506)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54136}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
Interaction partners:
- Lysine--tRNA ligase, cytoplasmic
- U3 small nucleolar RNA-associated protein 8
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
Sequence:
MASTANMISQLKKLSIAEPAVAKDSHPDVNIVDLMRNYISQELSKISGVDSSLIFPALEWTNTMERGDLLIPIPRLRIKGANPKDLAVQWAEKFPCGDFLEKVEANGPFIQFFFNPQFLAKLVIPDILTRKEDYGSCKLVENKKVIIEFSSPNIAKPFHAGHLRSTIIGGFLANLYEKLGWEVIRMNYLGDWGKQFGLLAVGFERYGNEEALVKDPIHHLFDVYVRINKDIEEEGDSIPLEQSTNGKAREYFKRMEDGDEEALKIWKRFREFSIEKYIDTYARLNIKYDVYSGESQVSKESMLKAIDLFKEKGLTHEDKGAVLIDLTKFNKKLGKAIVQKSDGTTLYLTRDVGAAMDRYEKYHFDKMIYVIASQQDLHAAQFFEILKQMGFEWAKDLQHVNFGMVQGMSTRKGTVVFLDNILEETKEKMHEVMKKNENKYAQIEHPEEVADLVGISAVMIQDMQGKRINNYEFKWERMLSFEGDTGPYLQYAHSRLRSVERNASGITQEKWINADFSLLKEPAAKLLIRLLGQYPDVLRNAIKTHEPTTVVTYLFKLTHQVSSCYDVLWVAGQTEELATARLALYGAARQVLYNGMRLLGLTPVERM
Protein: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS) (Q9CDZ7)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
Interaction partners:
Sequence:
MNKKIRVRYAPSPTGLLHIGNARTALFNYLFARHHGGDFIIRIEDTDRERHVEDGERSQLENLRWLGMDWDESPETHENYRQSERLPLYQKYIDQLLTEGKAYYSYKTPEELEADHAKQEAAGIAPHYINEYAGMSDDEKAAYIAERKAQNIEPVVRISVDEKAIYKWNDIVKGDIEFEGKNIGGDWVIQKRDGYPTYNFAVVVDDHDMQISHVIRGDDHIANTPKQLVVYDALGWEAPQFGHMTLIINSETGKKLSKRDTNTLQFIEDYRKKGYMSDAIFNFIALLGWNPGGEKEIFSREELIELFDEHRLSKSPAAFDQKKLDWLDNEYIKNADFAKVFELTKPFLVAANRFDERAEELVKLYQPQMKSADEIVELTDLFYGDFPELTDEAREMLAAETTPLALSTFRAKLAELPENDFTVENIFPLFKATQKETGVKGKMLWMPIRIAASGSMHGPELPETIALLGKEKVLAHLDAALNK
Protein: Ceramide kinase-like isoform 10 (G0XYF9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFRGRRRSRVGALEEAPPENPKAAAEPERVLLRGIFEIRRESCDVALGERALRWRRIQPELPAGGTRHDLLSKEESLELEDIFSVKLKRRCWAKHPGRDTLLGITLFICLKEQRNKLKDSTLDLINFSEDHCDIWFRQFKKILDVTEYEGHALSLLDECELRGFDGVVCVGGDGSASEAARALLLRAQKNAGVEMDCIPTLVGAELPLGFIPAGKA
Protein: Coiled-coil domain containing 141 (J3QNK9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XLGGSLQSTSDLRRRWIAMKPQLQLVHLIKPRELELLAQPMELASSEEVQMQLGRSQERRAHVDHLHQLALTLGVDIISSVQQPNCSNISAKNLQQQLEALELESRSWSAQAKEHERVLSCSLEYCTARDEISELKESFKDIKKKFNNLKFNYS
Protein: Atrial natriuretic peptide receptor 2 (EC 4.6.1.2) (Atrial natriuretic peptide receptor type B) (ANP-B) (ANPR-B) (NPR-B) (Guanylate cyclase B) (GC-B) (P16067)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20594}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20594}.
Interaction partners:
- C-type natriuretic peptide
- Natriuretic peptides A
- Atrial natriuretic peptide receptor 1
- Natriuretic peptides B
- Inosine triphosphate pyrophosphatase
- cGMP-specific 3',5'-cyclic phosphodiesterase
- cGMP-dependent 3',5'-cyclic phosphodiesterase
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A
- High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
- Phosphodiesterase
Sequence:
MALPSLLLVVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRALPVDLRFVSSELDGACSEYLAPLRAVDLKLYHDPDLLLGPGCVYPAASVARFASHWHLPLLTAGAVASGFAAKNEHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPHYFTIEGVFEALQGSNLSVQHQVYTREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQAQRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTQEQAQALREAFQTVLVITYREPPNPEYQEFQNRLLIRAREDFGVELAPSLMNLIAGCFYDGILLYAQVLNETIQEGGTREDGLRIVEKMQGRRYHGVTGLVVMDKNNDRETDFVLWAMGDLESGDFQPAAHYSGAEKQIWWTGRPIPWVKGAPPLDNPPCAFDLDDPSCDKTPLSTLAIVALGTGITFIMFGVSSFLIFRKLMLEKELASMLWRIRWEELQFGNSDRYHKGAGSRLTLSLRGSSYGSLMTAHGKYQIFANTGHFKGNVVAIKHVNKKRIELTRQVLFELKHMRDVQFNHLTRFIGACIDPPNICIVTEYCPRGSLQDILENDSINLDWMFRYSLINDLVKGMAFLHNSIISSHGSLKSSNCVVDSRFVLKITDYGLASFRSTAEPDDSHALYAKKLWTAPELLSGNPLPTTGMQKADVYSFAIILQEIALRSGPFYLEGLDLSPKEIVQKVRNGQRPYFRPSIDRTQLNEELVLLMERCWAQDPTERPDFGQIKGFIRRFNKEGGTSILDNLLLRMEQYANNLEKLVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNFDVYKVETIGDAYMVVSGLPGRNGQRHAPEIARMALALLDAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGQALKIHVSSTTKDALDELGCFQLELRGDVEMKGKGKMRTYWLLGERKGPPGLL
Protein: Uncharacterized protein F8D11.10 (Q9C843)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MYTYDSDKTQDGEENLKCSLEKLAKKIIQNAGDTNGNNSTPNSNDDFAQVFGRERPGRVRCVGLGPTPSSFIQNRTTTTLSKEQEVLSLNNRVRELEDKLVKMSDLEDKVDKMNEVIYISTCRRQQQLHYMTSTMDRRRWLQVEGNDFK
Protein: Uncharacterized transcriptional regulatory protein TBS1 (Thiabendazole sensitive protein 1) (P38114)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in tolerance to thiabendazole.
Subcellular location: Nucleus membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
Sequence:
MNMDSGITSSHGSMDKTQKQSSEWAANQKHNQRVENTRVLMGPAVPAMPPVPSNFPPVPTGTIMSPQLSPFPDHRLRHHPLAHMMPADKNFLAYNMESFKSRVTKACDYCRKRKIRCTEIEPISGKCRNCIKYNKDCTFHFHEELKRRREEALNNKGNGKSVKKPRLDKENKFKDENFDIAVRSRNTSSTDSSPKLHTNLSQEYIGVSAGKSASDKEDTWPDFVPIDRTVLEKIELNHTKVAGKVFVLEEICKNMKGTIEKLAEKSKIDVIDKEYMKRPKRKQYSKALLTKQKMFHFRQNVLSHLTDEEFLSPINEMFTTTFKYSILQTKLVLDFSFRSASSPSSDNILYPLPRLAIAKRLLKNIKCPSLASLLHIVDVDQCLQFADVHFDPAKGRLTSSQAFLLNICLCLGATVTNFEEKQELVDEDNHETYYFEKFELWRLRSFTFLNSVYYYHKLSVARADMTALKALLLLAKFAQQKISASSAVKVLSVAIKVALDLRLNLHSTYEDLELDEIIKRRRLWCYCFSTDKFFSVVLSRPPFLKEENTDVLTDESYVELFRDKILPNLSIKYDDSKLEGVKDIVSVVNLLANHLEYVPYIQSYFLSRLSLIESQIYYSCFSIRTTLDDTLDEIIENVLENQKALDRMRDDLPTILSLENYKENMRILSLDSSKLDFEVSCCTTILLHLRWYHQKITLSLFVISIIGDNLDQRESSRHDIAEIIRRSRLDFKRNCIEVLNILKDFEYYPTVQNEFLYFSLTTVFSMFLYLSEIMVNDEHAMETGYIIGLLRDTHTRMLGSEERCLSVHNLKWQTSLFFYTFFLRSTMEKFNLTSKYAKFYAFDSNYYEGVLNRLVKHTRESKDDMVELLKTSFINKEKMAAFGSFVTEDQEKMEVSFNIFNEITIQDLNFLQFSSIPKLWENKTLEPGEEYHHSNGTNTDNNETTGADDTDDNNNNNNNNNKNGNNSSSTINNNNNNYSNSNNNDNDNNINDDDDDDDDDDDDDDDDDDDDDNDDDYSNNGADDDEEDDDYDRSLFPTGLASLLDASYPERTANDYRDENEQSNKLFEKIEGHLEHGVFFYDRDFFFKNVCVKM
Protein: Class A basic helix-loop-helix protein 15 (bHLHa15) (Class B basic helix-loop-helix protein 8) (bHLHb8) (Muscle, intestine and stomach expression 1) (MIST-1) (Q7RTS1)
Organism: Homo sapiens (Human)
Function: Plays a role in controlling the transcriptional activity of MYOD1, ensuring that expanding myoblast populations remain undifferentiated. Repression may occur through muscle-specific E-box occupancy by homodimers. May also negatively regulate bHLH-mediated transcription through an N-terminal repressor domain. Serves as a key regulator of acinar cell function, stability, and identity. Also required for normal organelle localization in exocrine cells and for mitochondrial calcium ion transport. May function as a unique regulator of gene expression in several different embryonic and postnatal cell lineages. Binds to the E-box consensus sequence 5'-CANNTG-3' (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MKTKNRPPRRRAPVQDTEATPGEGTPDGSLPNPGPEPAKGLRSRPARAAARAPGEGRRRRPGPSGPGGRRDSSIQRRLESNERERQRMHKLNNAFQALREVIPHVRADKKLSKIETLTLAKNYIKSLTATILTMSSSRLPGLEGPGPKLYQHYQQQQQVAGGALGATEAQPQGHLQRYSTQIHSFREGT
Protein: Major capsid protein VP4 (A0A346LU62)
Organism: Sulfolobus filamentous virus 1 (SFV1) (Sulfolobus virus SFV-1)
Function: Self-assembles to form a helical, filamentous nucleocapsid (Probable). Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular location: Virion {ECO:0000269|PubMed:32759221}.
Interaction partners:
Sequence:
MPSRRTGITTEDAITKYSVKAKTEQTAYKNATKDMVVQAQNIMNFYSVVNQALIPWLNAHGVGGNLRILYRQLANEYVKVLNTKQSGEVIKRLKIALRHKYWLRGLDEAMLDEFMDYIDSLKSTTTNYIIFNMQSSK
Protein: Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit MB1) (Proteasome subunit X) (Proteasome subunit beta-5) (beta-5) (P28074)
Organism: Homo sapiens (Human)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- Proteasome subunit beta type-7
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Proteasome subunit alpha type-1
- 26S proteasome regulatory subunit 8
- 26S proteasome regulatory subunit 6B
- 26S proteasome regulatory subunit 6A
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 7
- Proteasome subunit alpha type-7
Sequence:
MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP
Protein: Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (Neural RAP guanine nucleotide exchange protein) (PDZ domain-containing guanine nucleotide exchange factor 1) (RA-GEF-1) (Ras/Rap1-associating GEF-1) (Q17RH5)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
MGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQYSLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAVASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVARSSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDDEQVSAV
Protein: Uncharacterized protein (Q72DS8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Heterodisulfide reductase, iron-sulfur-binding subunit, putative
- Heterodisulfide reductase, putative
- Heterodisulfide reductase, transmembrane subunit, putative
Sequence:
MSDEGRRMFKMDAVLGLIAGKNGAAVSDLLGYLAQRDLAAEDEAAVAPIAKGWLFSQHPPFMQCAYSEVGSYEDWVKKECGRLGDNVSLQPIPAAELAAINGVLDRIAEYKATIAAQAGEIEGLKGQVKELTPFKGQAADLEKKLAQSEQKVQGLNGDIGNLRKELAPFQGKVAIDEKEIESSVKDIVSRAVKDALKNLPVAAAGAAAVAGDAAAEPAGFEESSSSDGGVPDTFGFGASGASDDGFGF
Protein: BAI1-associated protein 3 (BAP3) (Brain-specific angiogenesis inhibitor I-associated protein 3) (O94812)
Organism: Homo sapiens (Human)
Function: Functions in endosome to Golgi retrograde transport. In response to calcium influx, may interact with SNARE fusion receptors and membrane phospholipids to mediate endosome fusion with the trans-Golgi network. By promoting the recycling of secretory vesicle transmembrane proteins, it indirectly controls dense-core secretory vesicle biogenesis, maturation and their ability to mediate the constitutive and regulated secretion of neurotransmitters and hormones. May regulate behavior and food intake by controlling calcium-stimulated exocytosis of neurotransmitters including NPY and serotonin and hormones like insulin. Proposed to play a role in hypothalamic neuronal firing by modulating gamma-aminobutyric acid (GABA)ergic inhibitory neurotransmission (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28626000}. Recycling endosome membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Late endosome membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Cell membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Note=Rapidly recruited to the plasma membrane and to Golgi structures in response to increased intracellular calcium concentration. {ECO:0000269|PubMed:28626000}.
Interaction partners:
- Adhesion G protein-coupled receptor B1
- Importin-13
- Secretin receptor
Sequence:
MRPRGAAFAAGPPGDLHLGTAIGFAGAIWRSRSPAMSTLLDIKSSVLRQVQVCPSFRRRTEQDPGSASADPQEPATGAWKPGDGVEFFAHMRLMLKKGEGRQGLPCLEVPLRSGSPAPPEPVDPSLGLRALAPEEVEMLYEEALYTVLYRAGTMGPDQVDDEEALLSYLQQVFGTSLEEHTEAIERVRKAKAPTYALKVSVMRAKNLLAKDPNGFSDPYCMLGILPASDATREPRAQKEQRFGFRKGSKRGGPLPAKCIQVTEVKSSTLNPVWKEHFLFEIEDVSTDQLHLDIWDHDDDVSLVEACRKLNEVIGLKGMGRYFKQIVKSARANGTAGPTEDHTDDFLGCLNIPVREVPVAGVDRWFKLEPRSSASRVQGHCHLVLKLITTQRDTAMSQRGRSGFLSHLLLLSHLLRLEHSAEEPNSSSWRGELSTPAATILCLHGAQSNLSPLQLAVLHWQVSSRHHQTCTLDYSYLLGLLEDMQAHWEEAPSLPQEQEESLADSLSAFSEFGLQLLRQLRDYFPATNSTAVHRLELLLKCLGKLQLFQPSFEICPFESELNMDIAAALKRGNREWYDRILNDKSPREQPGPQRLPGLVVLADAVYDDLQFCYSVYASLFHSILNVDVFTLTFRQLERLVAEEAWVLTEELSPKMTLEVASGLFELYLTLADLQRFWDSIPGRDSRSLALAGIHAPFLPAVKLWFQVLRDQAKWRLQGAVDMDTLEPVDASSRHSSSAATAGLCLSHIQELWVRLAWPDPAQAQGLGTQLGQDVCEATLFYTELLRKKVDTQPGAAGEAVSEALCVVLNNVELVRKAAGQALKGLAWPEGATGPEGVLPRPLLSCTQALDDDLQREAHTVTAHLTSKMVGDIRKYVQHISLSPDSIQNDEAVAPLMKYLDEKLALLNASLVKGNLSRVLEALWELLLQAILQALGANRDVSADFYSRFHFTLEALVSFFHAEGQGLPLESLRDGSYKRLKEELRLHKCSTRECIEQFYLDKLKQRTLEQNRFGRLSVRCHYEAAEQRLAVEVLHAADLLPLDANGLSDPFVIVELGPPHLFPLVRSQRTQVKTRTLHPVYDELFYFSVPAEACRRRAACVLFTVMDHDWLSTNDFAGEAALGLGGVTGVARPQVGGGARAGQPVTLHLCRPRAQVRSALRRLEGRTSKEAQEFVKKLKELEKCMEADP
Protein: Inner membrane protein YghQ (Q46841)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- O-antigen ligase
- Putative frv operon regulatory protein
- Putative lipopolysaccharide heptosyltransferase 4
Sequence:
MAGFNIKHWFADGAFRTIIRNSAWLGSSNVVSALLGLLALSCAGKGMTPAMFGVLVIVQSYAKSISDFIKFQTWQLVVQYGTPALTNNNPQQFRNVVSFSFSLDIVSGAVAIVGGIALLPFLSHSLGLDDQSFWLAALYCTLIPSMASSTPTGILRAVDRFDLIAVQQATKPFLRAAGSVVAWYFDFGFAGFVIAWYVSNLVGGTMYWWFAARELRRRNIHNAFKLNLFESARYIKGAWSFVWSTNIAHSIWSARNSCSTVLVGIVLGPAAAGLFKIAMTFFDAAGTPAGLLGKSFYPEVMRLDPRTTRPWLLGVKSGLLAGGIGILVALAVLIVGKPLISLVFGVKYLEAYDLI
Protein: F-box protein 2 (A0A8I6AAF5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
GTPFLRASESVSHPEEASPEEQPEEAGAEASAEEEQPREEEEEETEAVEYLAELPEPLLLRVLAELPATELVQACRLVCLRWKELVDGAPLWLLKCQQEGLVPEGSADDERDHWQQFYFLSKRRRNLLRNPCGEEDLEGWCDVEHGGDGWRVEELPGDSGVEFTHDDSVKKYFASSFEWCRKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRTDAGSLYELTVRLLSEHEDVLAEFNTGQVAVPEDGSWMEISHTFTDYGPGVRYVRFEHGGQDSVYWKGWFGARVTNSSVWVEP
Protein: Polyphosphate kinase (EC 2.7.4.1) (ATP-polyphosphate phosphotransferase) (Polyphosphate kinase 1) (PPK1) (Polyphosphoric acid kinase) (Q54BM7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Produces polyP in a broad range of chain lengths (50-300 Pi residues). Involved in development (growth and fruiting body formation), sporulation, phagocytosis, cell division and the late stages of cytokinesis.
Subcellular location: Vesicle {ECO:0000269|PubMed:17940044}.
Interaction partners:
- Inorganic pyrophosphatase
Sequence:
MITNSKMENKILDEFDEEELNKLKINSNNKESTTTTTSTTTTTTTTTSTSGEESDDEHTGSSSSTAAMELHRYKISQECPVDFEDDYDEESSSFDEEDEDSAAESNGGNGKLIPNPNDKKKKRSSKSSSKSSKSKSKSKNKETTANPVQNCQLMESGTLFSPTEFVKSSTVNPSKSPVQPIKLSSMLGLSELGTSNVLTVQNPQPISEPLKNDISSGSSSSSSSNNNNSNSNSNGNCNSDSTKSKFTSLNSWDAPPLANVLPDPSYCQDIVDSENNFIVPSVKHTILDVDNLFNNLIQNTNNNNNNDFKSSTMIGKPFSSGGDGSTSPLISGLSSSSIIPNGNGSLAEQQQQQQQSIPESEIPIDIKVLQLSGSRMFFNRELSELIYFYRILYEAYNPTYPILERVRFIAITSQNLDMYFCKRALKLRLGYISTRKTLKPEEHYINMVLNTTRNLINEIYNIYMNILAPELSNNNVFIIKYSDLTEPEKIQLRGFFLQHVFPLMTPLVVDAGHPFPNLSNLSLNIAVLLKHDEDTTRFVRIKVPQRIPRFVHIKQRSNYSIIPMEEIILANLDTLFPNTKILTKSLFRVSRHNDLKLSGEDQANDLLELIKTELHKRKFAPMVRLEVSHNMPAEILDMLKTQLALDAYDVYVINGPLGLQDLFELCKLNLPHLKFQPWVPHIPSRLVNLAKYPSEDVFSVIRKGELLVNLPYLSFNSSVQFFIESAVKDPKVLAIKIAIYRTNSNSQLIRALCEAASHKEVMVLVDLKASGDEEQNTKFARLLEQAGCHVSYGLVGLKTHAKIAMVVREEENGLREYLNISTGNYNASTSDVYADICLFSCDPDLGEDMCNLFNYLTGYSRVSSFKKLLIAPMNMRSTLIQLIDNEAKNAREGKDATINAVMNGLDDKRLVNALYQASIAGVKITLVVRGRCRILPGIKGISENIKVISILGRFLEHSRIYCFHNNGKPKAYIASADWLHRNLKRRVEVMVPVDDANNIKQLYEIINVYCNDSNAWEMLSDGRYKKRSSPIDEDSQTQFMNQTNQKHPVIWSK
Protein: High mobility group protein B4 (Q8WW32)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6P8W9}. Chromosome {ECO:0000250|UniProtKB:Q6P8W9}. Note=Interacts specifically with the sex chromosomes. {ECO:0000250|UniProtKB:Q6P8W9}.
Interaction partners:
Sequence:
MGKEIQLKPKANVSSYVHFLLNYRNKFKEQQPNTYVGFKEFSRKCSEKWRSISKHEKAKYEALAKLDKARYQEEMMNYVGKRKKRRKRDPQEPRRPPSSFLLFCQDHYAQLKRENPNWSVVQVAKATGKMWSTATDLEKHPYEQRVALLRAKYFEELELYRKQCNARKKYRMSARNRCRGKRVRQS
Protein: UPF0398 protein SP_0371 (Q97SJ0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MATALVLGYSAFDLGLFSDKDPRLKLIKKAIRKDLEAMAADGVSWLVFTGSLGFEYWVLEVAQEMKTEYGFQLATIFAFETHGENWNEGNQMKLSRFKQVDFVKYAYPRYEHKGQLRDYQQFLLENTTSSYLFYDEENETKLAYFYQKMKNQEDYFIKRLTFDELNELAENFSEN
Protein: Adagio protein 3 (F-box only protein 2a) (FBX2a) (Flavin-binding kelch repeat F-box protein 1) (Q9C9W9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO3) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. Forms a complex with 'GIGANTEA' (GI) to regulate 'CONSTANS' (CO) expression. Promotes CO expression during the light period of long days by decreasing the stability of CDF1 and CDF2 and by interacting directly with the CO protein and stabilizing it. ADO3 function is mainly GI dependent. Does not act as a regulator of CDF1 transcription. The interactions of ADO1/ZTL and ADO2 with ADO3 prevent its interaction with CDF1.
Subcellular location: Nucleus. Cytoplasm. Note=Moves from the nucleus into cytosolic speckles upon interaction with ADO1 and ADO2.
Interaction partners:
- Protein GIGANTEA
- Cyclic dof factor 1
- Two-component response regulator-like APRR1
- Two-component response regulator-like APRR5
- E3 ubiquitin-protein ligase COP1
- UPF0235 protein At5g63440
- Cryptochrome-2
- Phytochrome A
- Protein LHY
- Two-component response regulator-like APRR9
Sequence:
MAREHAIGEATGKRKKRGRVEEAEEYCNDGIEEQVEDEKLPLEVGMFYYPMTPPSFIVSDALEPDFPLIYVNRVFEVFTGYRADEVLGRNCRFLQYRDPRAQRRHPLVDPVVVSEIRRCLEEGIEFQGELLNFRKDGTPLVNRLRLAPIRDDDGTITHVIGIQVFSETTIDLDRVSYPVFKHKQQLDQTSECLFPSGSPRFKEHHEDFCGILQLSDEVLAHNILSRLTPRDVASIGSACRRLRQLTKNESVRKMVCQNAWGKEITGTLEIMTKKLRWGRLARELTTLEAVCWRKFTVGGIVQPSRCNFSACAVGNRLVLFGGEGVNMQPLDDTFVLNLDAECPEWQRVRVTSSPPGRWGHTLSCLNGSWLVVFGGCGRQGLLNDVFVLDLDAKHPTWKEVAGGTPPLPRSWHSSCTIEGSKLVVSGGCTDAGVLLSDTFLLDLTTDKPTWKEIPTSWAPPSRLGHSLSVFGRTKILMFGGLANSGHLKLRSGEAYTIDLEDEEPRWRELECSAFPGVVVPPPRLDHVAVSMPCGRVIIFGGSIAGLHSPSQLFLIDPAEEKPSWRILNVPGKPPKLAWGHSTCVVGGTRVLVLGGHTGEEWILNELHELCLASRQDSDL