wanglab/gogpt-training-data huggingface dataset:
Protein: Phototropic-responsive NPH3 family protein NPY1 (Protein ENHANCER OF PINOID) (Protein MACCHI-BOU 4) (Protein NAKED PINS IN YUC MUTANTS 1) (Q8H1D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Coregulates with PID the auxin-mediated plant organogenesis. Regulates cotyledon development through control of PIN1 polarity. May play an essential role in root gravitropic responses.
Subcellular location: Late endosome {ECO:0000269|PubMed:17913786}. Cell membrane {ECO:0000269|PubMed:21490067, ECO:0000269|PubMed:33705718}. Cytoplasm, cytosol {ECO:0000269|PubMed:21490067, ECO:0000269|PubMed:33705718}. Note=Colocalized with PID (PubMed:17913786). PIN1- and PIN2-dependent polar localization at the cell periphery almost identical to PIN proteins polarity, starting in protodermal cells at the early heart stage and later converging to the tips of cotyledon primordia; this localization is enhanced by PID (PubMed:21490067). {ECO:0000269|PubMed:17913786, ECO:0000269|PubMed:21490067}.
Interaction partners:
- Mitochondrial carnitine/acylcarnitine carrier-like protein
- Style cell-cycle inhibitor 1
- Probable indole-3-pyruvate monooxygenase YUCCA1
- Serine/threonine-protein kinase WAG2
- Serine/threonine-protein kinase WAG1
- Serine/threonine-protein kinase D6PK
- Bystin
- Probable indole-3-pyruvate monooxygenase YUCCA4
- Probable carboxylesterase 11
- PX domain-containing protein EREX
Sequence:
MKFMKLGSKPDTFESDGKFVKYAVSDLDSDVTIHVGEVTFHLHKFPLLSKSNRMQRLVFEASEEKTDEITILDMPGGYKAFEICAKFCYGMTVTLNAYNITAVRCAAEYLEMTEDADRGNLIYKIEVFLNSGIFRSWKDSIIVLQTTRSLLPWSEDLKLVGRCIDSVSAKILVNPETITWSYTFNRKLSGPDKIVEYHREKREENVIPKDWWVEDVCELEIDMFKRVISVVKSSGRMNNGVIAEALRYYVARWLPESMESLTSEASSNKDLVETVVFLLPKVNRAMSYSSCSFLLKLLKVSILVGADETVREDLVENVSLKLHEASVKDLLIHEVELVHRIVDQFMADEKRVSEDDRYKEFVLGNGILLSVGRLIDAYLALNSELTLSSFVELSELVPESARPIHDGLYKAIDTFMKEHPELTKSEKKRLCGLMDVRKLTNEASTHAAQNERLPLRVVVQVLYFEQLRANHSPVASVAASSHSPVEKTEENKGEEATKKVELSKKSRGSKSTRSGGGAQLMPSRSRRIFEKIWPGKGEISNKSSEVSSGSSQSPPAKSSSSSSRRRRHSIS
Protein: General transcriptional corepressor trfA (O77033)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as component of the trfA-tupA corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex (By similarity). Required for normal growth and for aggregation in early development. Required for a proper chemotactic response to cAMP.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL3
- ATP-dependent DNA helicase PIF1
Sequence:
MNVQQTQQQQAMAAQQQSMVAQQQQQIAQQQSAIAQQQIAQQQQIAQQQQIAQQQQQHQQHQQHQQQHQQQQQHQQQHQQQQHIQQQQQPQQQQPQQQQSQQQQQQHQQQQQPQQQQPPQQQQQQPPQQQQQPQQQQQQQQQQQQQPQQQQQQQQQDQLSGVTGKIRDLNESIWIHLGGYAESIGEQDKALASYENALRHNPFSIKALTQIASLFRIKEQYSKAAEYFQRIVTIESKNGEVWGALGHCYLMMDDLQKAYTAYQQALYHLPNPKDPNLWYGIGILYDRYGSYDHAEEAFTAVLKMDNKFEKSTEIYFRLGVLYKHQGKYDQSLEYFQHLVKNPPLPLTTSDIWFQIGHVYELQKEYHKSKDAYEKVLKDNATHSKVLQQLGWLYHHNPLFTNQEYAINYLMRSIDSDSSDAQTWYLLGRCYMTQQKYKKAYDAYQQAVYRDGRNPTFWCSIGVLYYQINQYRDALDAYTRAIRLNPFLSEVWYDLGTLYESCHQHTDSLDAYQRAAELDPHNKHIQSRLATLRAQVSGKPIGKDGYDLQNGEHGEHGGKSTPMIIEPNSPGTGAMESLGKGGQNNRNGNNNGNNSFVPELAEINSHLPEDMRNNSSLPSSNELNSSLIDRKTERGRGEDMHNSHHSQYSNSMSMNNMNNNNNNMNMNNNMNNNMNNMNNNNNNMNSMNNMNNNNNNINNNMSNNNNNNHNNHQMNQYNNNNNNSNINNNNNNHHNMNDNVNSKNNDVLDRRYKGILEREKTSPNGDGRDNRDNIRDNRDNRDSRDGRDNRDGRDSRDRIQEYTREYNNNNNNNNSISSINNNNNNNNNNYNNNNNNNNNNNNNNNNNGLRATSPLPSHNDRRSYERDNKERINNNNNNNNNMNNNMNNNMNNMNNNNNNSNISRFEHQNNRTSSPFENNSNNNNNNNNNNNNNINYNNIGQRALSPQSSQHKDRREIILDEESDINERSKTRSPSIVKEAEEKRETVIVDKERSPTPIITEKPDEKQVEKVTDKESSLVEKVDKENEKESPSSSSSSKEIEKETEKEKEKEKEKEKEVEKEVEKEIENDKEKEKEKEVEKDVEENKSVEKSSEKPVEKESTTTTTNDEDEEGELSEPTTTTKKDDSSKLPTDEKKLSSVSPTTTAVEQSRDETKELEMDTKEDSEKEKKSSTTTTAAASESVKPIDEEKKSPTTTTTTTTNTTTVEPTHKDKESSKNDDTTTTTTTTTTKSAKSPNSSPTRSDEVVEPHQDASQEEINKRKLEDDITSTPSKRLKPDSTPSSATTASTPSEQPESPLKKENPVGETLSPEIKDSKSSSSSSSSSSSSTNTGSSSTNSSAKNERDRDRERERERERDREREREREREREREREKNKQPTRAPIKPSSRKLER
Protein: E3 ubiquitin-protein ligase MARCHF5 (EC 2.3.2.27) (Membrane-associated RING finger protein 5) (Membrane-associated RING-CH protein V) (MARCH-V) (Mitochondrial ubiquitin ligase) (MITOL) (RING finger protein 153) (RING-type E3 ubiquitin transferase MARCHF5) (Q9NX47)
Organism: Homo sapiens (Human)
Function: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:16874301}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000255}. Note=Authors show that the protein can be detected in endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show its presence only in mitochondria (PubMed:16874301). {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:16874301}.
Interaction partners:
- Mitofusin-2
- Dynamin-1-like protein
- Mitochondrial fission 1 protein
- Mitofusin-1
- E3 ubiquitin-protein ligase MARCHF2
- Mitochondrial antiviral-signaling protein
- Ubiquitin-conjugating enzyme E2 D2
- FUN14 domain-containing protein 1
- TRAF family member-associated NF-kappa-B activator
- Mitochondrial ubiquitin ligase activator of NFKB 1
Sequence:
MPDQALQQMLDRSCWVCFATDEDDRTAEWVRPCRCRGSTKWVHQACLQRWVDEKQRGNSTARVACPQCNAEYLIVFPKLGPVVYVLDLADRLISKACPFAAAGIMVGSIYWTAVTYGAVTVMQVVGHKEGLDVMERADPLFLLIGLPTIPVMLILGKMIRWEDYVLRLWRKYSNKLQILNSIFPGIGCPVPRIPAEANPLADHVSATRILCGALVFPTIATIVGKLMFSSVNSNLQRTILGGIAFVAIKGAFKVYFKQQQYLRQAHRKILNYPEQEEA
Protein: Ribosomal lysine N-methyltransferase set10 (EC 2.1.1.-) (SET domain-containing protein 10) (O74738)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates ribosomal protein L23 (rpl23a and rpl23b).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MEKLLHEALQNGCKLHKSVEFIQSRDDNACFGSYIAVAQNDIAPDQLLISCPFEYAITYNKAKEELKKLNPNFESCNPHITLCTFLALESLKGIQSKWYGYIEYLPKTFNTPLYFNENDNAFLISTNAYSAAQERLHIWKHEYQEALSLHPSPTERFTFDLYIWSATVFSSRCFSSNLIYKDSESTPILLPLIDSLNHKPKQPILWNSDFQDEKSVQLISQELVAKGNQLFNNYGPKGNEELLMGYGFCLPDNPFDTVTLKVAIHPDLPHKDQKAAILENDCQFQLSNLVFFLPKSPDKEIFQKILQCLAVVTASSLELRKLTAHLLTGDLASYVPSLRGQIKSLEVLLMYIDSRADLLLKSNPQVSPTSERQVWAKIYRDSQINILQDSITYVKNYMEESLQKTYKPLPNLLQYLILNSISIFLLQHPLFAPLSHAIESLYGSTDAEALVATDEQDILMILICVYCLSISEKLPFSISMLVEGYPAVANPEGVEVFEILDEMFFQQFTNVFGESKHFNKENVSWALQLVNDESLDFSGFTFIIAHN
Protein: Polyubiquitin 14 [Cleaved into: Ubiquitin] (Q3E7T8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Actin-2
- E3 ubiquitin-protein ligase UPL4
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase PRT1
- Small ribosomal subunit protein uS7y
- E3 ubiquitin-protein ligase UPL3
- Actin-7
- Protein PEROXIN-4
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Small ribosomal subunit protein uS7z
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGF
Protein: Zinc finger and BTB domain-containing protein 32 (FANCC-interacting protein) (Fanconi anemia zinc finger protein) (Testis zinc finger protein) (Zinc finger protein 538) (Q9Y2Y4)
Organism: Homo sapiens (Human)
Function: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor. Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10572087}. Note=Located in nuclear speckles.
Interaction partners:
- Trans-acting T-cell-specific transcription factor GATA-3
- Fanconi anemia group C protein
- Alpha-
- Rhox homeobox family member 2
Sequence:
MSLPPIRLPSPYGSDRLVQLAARLRPALCDTLITVGSQEFPAHSLVLAGVSQQLGRRGQWALGEGISPSTFAQLLNFVYGESVELQPGELRPLQEAARALGVQSLEEACWRARGDRAKKPDPGLKKHQEEPEKPSRNPERELGDPGEKQKPEQVSRTGGREQEMLHKHSPPRGRPEMAGATQEAQQEQTRSKEKRLQAPVGQRGADGKHGVLTWLRENPGGSEESLRKLPGPLPPAGSLQTSVTPRPSWAEAPWLVGGQPALWSILLMPPRYGIPFYHSTPTTGAWQEVWREQRIPLSLNAPKGLWSQNQLASSSPTPGSLPQGPAQLSPGEMEESDQGHTGALATCAGHEDKAGCPPRPHPPPAPPARSRPYACSVCGKRFSLKHQMETHYRVHTGEKPFSCSLCPQRSRDFSAMTKHLRTHGAAPYRCSLCGAGCPSLASMQAHMRGHSPSQLPPGWTIRSTFLYSSSRPSRPSTSPCCPSSSTT
Protein: Signal recognition particle receptor subunit beta (Q59N43)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle 54 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP14
- Signal recognition particle SEC65 subunit
- Signal recognition particle subunit
- Serine/threonine-protein kinase MEC1
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL4
Sequence:
MDAVLISLLTILLGFVLILIIFFIQTGGLKSLVSTTTSKKSSLYHPTFLILGANNSGKTSFFYKLLQLSNDDEIDDKANTTTVAATVSSLEPNVTKINLPISNPSIGKPFQLIDYPGHLKLQKVFERLIIDEITLKNLKGVVYMIDSSSVNINDDTNLESIVKFLYNLFSITERIPNGVDFLIAINKTDLFDSVPVHKIKTKLELEINKLIRHEIENVEKTSGIDDNDNDNGNQNSNGGGGNSSNGDNSDGINGESLRAFWMSVVGSGNFTFDKLEGNVDFVGGSVLKNKISQWENWFDEKVVNP
Protein: Citrate lyase acyl carrier protein (Citrate lyase gamma chain) (P69330)
Organism: Escherichia coli (strain K12)
Function: Covalent carrier of the coenzyme of citrate lyase.
Subcellular location: Cytoplasm.
Interaction partners:
- [Citrate [pro-3S]-lyase] ligase
- Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase
- Citrate lyase subunit beta
- Citrate lyase alpha chain
- 2-
- Citrate/succinate antiporter
- Transcriptional regulatory protein DpiA
Sequence:
MKINQPAVAGTLESGDVMIRIAPLDTQDIDLQINSSVEKQFGDAIRTTILDVLARYNVRGVQLNVDDKGALDCILRARLEALLARASGIPALPWEDCQ
Protein: GH08783p (Q961T5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYKLPPETSVQLVPSSPTEQEPQPVRHKKAVSVPTVKRHQRKMRALDLPAVDKTRRIISLSTSKAAYVSNELSNINSVLFSQFESNPADAINEALISLLKQQQQETKDQRKTRQSCIGSDSAVNLEDIVLIDPQPPLAVDPHNVKYLEDDYVSPQSQPGSQYNFKRRKTDIRSSEPSEVVVLDNSGSPNEKNSKEVFPSTKQTLSRETKKSAVTVRKESLGQLKQAPTSTVPEDICDPKARAINAKENPEVCEPVPDNGGSDDIDDSKAGSVSVRKSEVKAALGQKLLEAIGLSQLGADAAPENSRDTLRSALKRSIKQAQEQQLQLKRGNHEEPVKQLADSTTKLSAAESADEHKKAIAERELALLNRGFKAGEENTISLKDDKWERTDVSSSSSRNRRGRKSKIDSNVEDFGDEEKKDSRWDEDDDLPLKADTEKPSERNSTNARPTRTSKTLSKYYKGPTSKSHHSMGTRSTRQR
Protein: NADPH--hemoprotein reductase (EC 1.6.2.4) (Q7Z270)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
METKAIMLLVVSAIGVVMLTWLFVSICTRKSKADDMHNEPLLSKHANSKLMGVDGRVLVLYGSQTGTAEMFARNLTREGSRRGFPLKVLDIEKYQASNLVKEKRVIIVCATYGDGEPTDPMVEFHDWLMSDSRVMGEELSGVRYTVFGLGDRQYVNFCREGITVDRRMSELGAQRFYPLGRGDYSDDIEEDFDKWRSGLWPALSTELALDVKSGEEGPVAPECCMKALESSDEAPLPFPKADPRQEPTQRLPSWVPVKVNKELLSNATGRSTRLIEFDTSETVISYQAGDHLGVLPSNPSEMVNTYLRVLGVSEQESSQVISLENKNTGECVFPCRASIRTALTWYIDLAGPPKKSTLRAFAHHCTDPVEKDTLLKLLSTEPESVEAYGKLVLELRTVLGFLQRFKSMSPPLSFFLEMMPRIAPRYFSISSDSLTHPTSVAITVAVVEGGLCTNLLQQAAVGQNIPVFVRKSNFHLPLRAKDRQIIMIGPGTGVAPFIGFLHRRSAWLEKGNKVGDALLFFGCRRREEDHIYADFMEKCLSNGALSVRDVAYSREQADKVYVQHRLAARGKEVWEIISRGGNVYVCGDAKNMARDVEKQLLDIAQKYGAMKEDEATALLEKLATDERYLKDVWTA
Protein: Heat shock protein HSP 90-alpha 1 (Q90474)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.
Subcellular location: Melanosome {ECO:0000250|UniProtKB:P07900}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Shuttles between the Z line and A band in response to stress conditions and fibril damage.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock cognate 71 kDa protein
- Cell division cycle 37 homolog
- E3 ubiquitin-protein ligase CHIP
- Heat shock cognate 71 kDa protein
- Heat shock cognate 71 kDa protein
- Protein SGT1 homolog
- Stress-induced-phosphoprotein 1
- peptidylprolyl isomerase
- Receptor
Sequence:
MPEKSAQPVMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSCKDLKIELIPDQKERTLTIIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIKLYVRRVFIMDNCEELIPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLDLFTELAEDKDNYKKYYEQFSKNIKLGIHEDSQNRKKLSDLLRYYTSASGDEMVSLKDYVSRMKDTQKHIYYITGETKDQVANSAFVERLRKAGLEVIYMIEPIDEYCVQQLKEYDGKNLVSVTKEGLELPEDEEEKKKQDELKAKYENLCKIMKDILDKKIEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKSQALRDNSTMGYMTAKKHLEINPAHPIVETLREKAEADKNDKAVKDLVILLFETALLSSGFTLDDPQTHANRIYRMIKLGLGIDDDDSVVEEISQPAEEDMPVLEGDDDTSRMEEVD
Protein: Tyrosine-protein phosphatase non-receptor type 9 (EC 3.1.3.48) (Protein-tyrosine phosphatase MEG2) (PTPase MEG2) (P43378)
Organism: Homo sapiens (Human)
Function: Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- SEC14-like protein 1
- 6-pyruvoyl tetrahydrobiopterin synthase
Sequence:
MEPATAPRPDMAPELTPEEEQATKQFLEEINKWTVQYNVSPLSWNVAVKFLMARKFDVLRAIELFHSYRETRRKEGIVKLKPHEEPLRSEILSGKFTILNVRDPTGASIALFTARLHHPHKSVQHVVLQALFYLLDRAVDSFETQRNGLVFIYDMCGSNYANFELDLGKKVLNLLKGAFPARLKKVLIVGAPIWFRVPYSIISLLLKDKVRERIQILKTSEVTQHLPRECLPENLGGYVKIDLATWNFQFLPQVNGHPDPFDEIILFSLPPALDWDSVHVPGPHAMTIQELVDYVNARQKQGIYEEYEDIRRENPVGTFHCSMSPGNLEKNRYGDVPCLDQTRVKLTKRSGHTQTDYINASFMDGYKQKNAYIGTQGPLENTYRDFWLMVWEQKVLVIVMTTRFEEGGRRKCGQYWPLEKDSRIRFGFLTVTNLGVENMNHYKKTTLEIHNTEERQKRQVTHFQFLSWPDYGVPSSAASLIDFLRVVRNQQSLAVSNMGARSKGQCPEPPIVVHCSAGIGRTGTFCSLDICLAQLEELGTLNVFQTVSRMRTQRAFSIQTPEQYYFCYKAILEFAEKEGMVSSGQNLLAVESQ
Protein: Bombesin receptor-activated protein C6orf89 (Amfion) (Q6UWU4)
Organism: Homo sapiens (Human)
Function: Exhibits histone deacetylase (HDAC) enhancer properties. May play a role in cell cycle progression and wound repair of bronchial epithelial cells.
Subcellular location: [Isoform 1]: Golgi apparatus membrane {ECO:0000269|PubMed:23460338}; Single-pass type II membrane protein {ECO:0000269|PubMed:23460338}. Midbody {ECO:0000269|PubMed:23460338}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:23460338}; Single-pass type II membrane protein {ECO:0000269|PubMed:23460338}. Midbody {ECO:0000269|PubMed:23460338}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:21857995}. Nucleus, nucleolus {ECO:0000269|PubMed:21857995, ECO:0000269|PubMed:23460338}. Note=Retained in nucleolar organiser regions (NORs) in mitotic cells (PubMed:23460338). {ECO:0000269|PubMed:23460338}.
Interaction partners:
- Bombesin receptor subtype-3
Sequence:
MDLAANEISIYDKLSETVDLVRQTGHQCGMSEKAIEKFIRQLLEKNEPQRPPPQYPLLIVVYKVLATLGLILLTAYFVIQPFSPLAPEPVLSGAHTWRSLIHHIRLMSLPIAKKYMSENKGVPLHGGDEDRPFPDFDPWWTNDCEQNESEPIPANCTGCAQKHLKVMLLEDAPRKFERLHPLVIKTGKPLLEEEIQHFLCQYPEATEGFSEGFFAKWWRCFPERWFPFPYPWRRPLNRSQMLRELFPVFTHLPFPKDASLNKCSFLHPEPVVGSKMHKMPDLFIIGSGEAMLQLIPPFQCRRHCQSVAMPIEPGDIGYVDTTHWKVYVIARGVQPLVICDGTAFSEL
Protein: Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 1) (2-phosphoglycerate dehydratase 1) (Q88YH3)
Organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:25721875}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
Interaction partners:
- Pyruvate kinase
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
- Fructose-bisphosphate aldolase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- phosphoenolpyruvate carboxykinase
- Phosphoenolpyruvate synthase
Sequence:
MSIITDIYAREVLDSRGNPTVEVELYTESGAFGRGIVPSGASTGEHEAVELRDGDKSRFMGKGVTKAVDNVNKLIAKEIVGYDVTDQRAIDQAMIKLDGTPNKAKLGANAILGVSIAAARAAADELEMPLYNYLGGFNAHVLPTPMMNVINGGAHANNDVDFQEFMIMPVGASSVKEAIRMGSETFHNLKAILNERGYSTAVGDEGGFAPDLKNNEEPFEILVEAIERAGYKPGKDIAIAFDCAASEFYNEETGKYDLKGEGENGQSFTAEEFVDLLDSIVDKYPIVSIEDPLDENNWEDWQMATAKLGKKVQIVGDDLFVTNTDYLAKGIKMGVANSILIKVNQIGTLTETVEAIEMAKEAGYTAIVSHRSGETEDTTIADLVVAMNAGQIKTGSMSRTERIAKYNQLMRIEDQLESTSEYKGIHGFYNLDEAARNTITSK
Protein: TNF receptor superfamily member 11A (F1M8Z6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Tumor necrosis factor ligand superfamily member 11
- TNF receptor-associated factor 6
- TNF receptor-associated factor
Sequence:
MAPRARRRRQFPAPLLALCVLLLPLQVTLQVTLPCTQERHYEHLGRCCSRCEPGKYLSSKCTPTSDSVCLPCGPDEYLDTWNEEDKCLLHKVCDAGKALVAVDPGNHTAPRRCACTAGYHWNADCECCRRNTECAPGFGAQHPLQLNVDTVCTPCLLGFFSDVFSSTDKCKPWTNCTVLGKMEAHQGTTESDVVCSSSLTLIKPPKEAQVYLPSLIVLLLFISVVVVAAIVFSIYYRKGGKTLTANLWNWVNDACSSLSGNKESSGDHCVGSHSANSSQQEVCEGILLMTREEKMVPEDCAGVCGPVRAASGPWAEGRDARTFTLVSEVETQGNLSRKIPTEDEYTDRPSQPPNGSLFLIQPGSRSTPPFQEPLEVGENDSLSQCFTGTESMVDSEGCDFTEPPSRTDYMPASPEKLLTKEIEDDSCLPWVANSNSTDGYTGSGNTPGEDHEPLPGSLKCGPLPQCAYSIGLPSEAAASLAEVGAQPQDRADAKLPSSERGASGSGSSPSEQPPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGPGPAEPEPEPEPVGRPVQEETLAHRDSFAGTAPRFPDACTTGAGLQEKGASRPKDWASRPVQEQGGAQASLNTQGSGQCAE
Protein: Uncharacterized protein (Q5AX93)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MKFLPLILPVVFALCAQAVEWHAHYRMTSDEYQSTANSYIDQGFRIKSVSGYERDGEDNYAAIFEKNNGVAWVSHHRMTSASYQDKFDKYIADGYRLLQVNGYTVGDNVYFAAVWDKSPAPGAWVARHNIDAASLQKYTDTYIEQGYRVTHVSAYEVNGEARFAALWEKINDGTAWWAWAKMTAAEYQKKFDTYLKDGYRLINVNGYSIGNTVYYAGIWDTSASGAWVARHGMDSPTFQNLFDEYKAAGYVLQVLSGYNTGTADRYAALWIKP
Protein: Protein frg1 (Q9P7X3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May have a role in processing of pre-rRNA or in the assembly of rRNA into ribosomal subunits. May be involved in pre-mRNA splicing (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cwf22
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-processing factor 19
Sequence:
MSMRLTFKGDKKIQKKKKKNTKSLQSSLESAENDPFWTDANELNELEGPAVIYKIDDDAGVSLGIEEVKESCVLLPLDKVSLEPELTRQVFLLSILNNTILLKSCLGKYMSCSKSGDLYCTQEAVGSQEQWIAENLGSGFWAWKSVSTKKYLTLSREKQDQAIACVSDTVIPEAKWRIRVQTRFLKKNKSSLFDNPTIHSRQLESMAGRKLSTDEKKTLKKAFKEGVLHEALLDLRVSSRSDKYG
Protein: Replication factor C subunit 2 (Activator 1 40 kDa subunit) (A1 40 kDa subunit) (Activator 1 subunit 2) (Replication factor C 40 kDa subunit) (RF-C 40 kDa subunit) (RFC40) (Replication factor C subunit 4) (DmRfc4) (P53034)
Organism: Drosophila melanogaster (Fruit fly)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. Subunit 2 binds ATP.
Subcellular location: Nucleus {ECO:0000269|PubMed:11438670, ECO:0000269|PubMed:7789770}. Note=Localizes to all replicating nuclei, it is dispersed from chromatin in mitosis.
Interaction partners:
- Replication factor C subunit 2
- Replication factor C subunit 3
- Activator 1 subunit 5
- Enhanced level of genomic instability 1
- Rad17
- Replication factor C subunit 1
- Chromosome transmission fidelity protein 18 homolog
- Proliferating cell nuclear antigen
- Cell cycle checkpoint control protein Rad9
- Checkpoint protein Hus1-like
Sequence:
MPEEPEKTADDKRSHLPWIEKYRPVKFKEIVGNEDTVARLSVFATQGNAPNIIIAGPPGVGKTTTIQCLARILLGDSYKEAVLELNASNERGIDVVRNKIKMFAQQKVTLPRGRHKIVILDEADSMTEGAQQALRRTMEIYSSTTRFALACNTSEKIIEPIQSRCAMLRFTKLSDAQVLAKLIEVAKWEKLNYTEDGLEAIVFTAQGDMRQGLNNLQSTAQGFGDITAENVFKVCDEPHPKLLEEMIHHCAANDIHKAYKILAKLWKLGYSPEDIIANIFRVCKRINIDEHLKLDFIREIGITHMKIIDGINSLLQLTALLAKLCIAAEKH