wanglab/gogpt-training-data huggingface dataset:
Protein: F-actin-capping protein subunit beta isoforms 1 and 2 (Beta-actinin subunit II) (CapZ 36/32) (CapZ B1 and B2) (P14315)
Organism: Gallus gallus (Chicken)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the regulation of cell morphology and cytoskeletal organization.
Subcellular location: [Isoform 1]: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:7929588}. Note=In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres. {ECO:0000269|PubMed:7929588}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:7929588}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5XI32}. Note=In cardiac muscle, isoform 2 is located at sarcomere intercalated disks. {ECO:0000269|PubMed:7929588}.
Interaction partners:
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit alpha-2
- Twinfilin-2
- F-actin-capping protein subunit alpha
- Uncharacterized protein.
- Dynactin subunit 2
- ARP1 actin-related A, centractin alpha
- Dynactin subunit 4
- Uncharacterized protein.
- Dynactin subunit 1
Sequence:
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN
Protein: Abelson helper integration site 1 (Jouberin) (F1QX08)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPAGQSDVRAKTKARFDEVLKRYTNPPSEKKKAKQISDQSQEIIVLQTLKKNLDLSKDTEDDEAILHNTYDPAQGSPRYTKNRRREREVSEKTNLNNAVSEEESTLTSGKRKSKRKLPQPPPSVQDADDNDRRTDAETDGKPIRRIKKGKNKAANDSSQQKEQTETEDDYLRAYQHQISQEEETAGKKSTRKKAAEKLEEKQLLNNELEKKKKKAKSSKHDAERSQAEVSAENQTEIIQDDVEEFKEDTVKPKVKKKKKRKEVPVEEEQTEEKPAFDDSLVLGVYIHRTDKLKTDLMVSHPMVKVHVVDEVTGQYVKKEDSHRHVSSFYEQENIEHILPIITQPFDFKKHKTTVPEWEEQIIFNERFGYFLQDDDESPRVMLLFEILDFISMEEARTNVSVDRHERGFRKIAWAFLKLVGTNGVLNIDTKLRLQLYCPPPRAKKVPQTVEVFQWWSKYPRNKYTSTLYVTVKGLKPPEHVDPGIRSMMALQQERGSTSYSELNSEMTNKTSTQIQESKAETMKWSRMPGQVCRIPNKPMHSFRGGQMGCFTLCFSHDGRALAAACADRDAFPIIIYEIPSGKVLSSFNGHLSVVYDLCWSRDDKGLLTASSDGTVRVWNVERLQTLAHKTLPHPSFVYCAKFHPQAQSLVATGGYDGVLRVWNVDVQDVNGQLLQEFDGHKTFINTLCFDPEGSRMFSADNSGLIIVWGTKVMPGSRRGATSQWSIEREIKEADLNGISINSLEVHPNGRRLLIHAKDSVLRVMDLRILAVKKYIGATNYRDRINSTFTPCGSFIFAGSEDGLAYVWNSETGDQVAVYSELCYSSALRAVAFHPHENMVAFCCFGQNQPIHLYLYDRKVAQMEVESLRGWSRSENLDSKTGRISSEFMSIQNPTATSMDRFANTARMSLKMQRVKQKLDSVLEPHRSSSNVDMYEQGGMSSLGRSIEGLNSYLPPPSLLSPHSKLQMSSSLSAQLIPQATLTSHTSGYSQAGQPIRRAPSLRQQKSFHDYEFSQQVETDLGQAHQTVVSLYEYRANRSDELSMRRGDVVHVLYKDNDSWWFGRLVSGQEGYFPASYVADEGNFDEELSRALEAQPSLIDQPEEAEHATPVQMSAAISASGELKIISELDTDAEASSTTRKKKKKKVKRIEVPSEDLPPSSGSSRRRRPLPKLGQANGAFEGEGLNLRDLV
Protein: Septin CDC11 (Cell division control protein 11) (G1UB61)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization, and spore wall formation. CDC11 is required for the correct localization of SEC3 at bud tips and bud necks. Plays a key role in invasive growth and virulence.
Subcellular location: Bud neck {ECO:0000269|PubMed:11454197, ECO:0000269|PubMed:12181342, ECO:0000269|PubMed:19915075, ECO:0000269|PubMed:22687514}. Note=Localizes to a tight ring at the bud and pseudohyphae necks and as a more diffuse array in emerging germ tubes of hyphae.
Interaction partners:
- Septin
- Cell division control protein 10
- Septin
- Septation protein 7
- Cyclin-dependent kinase 1
- Septin
- Serine/threonine-protein kinase GIN4
- Serine/threonine-protein kinase CLA4
- G1/S-specific cyclin CCN1
Sequence:
MNYSTENVSSAALRKRKTLKKSINFSIMIIGESGSGRSTLINTLCGGNSIVPTSSTATQDPFTKKLTLRHENVELEDNEGHKISLNIIDTPNFANSINCDDDFKIIVDFIRHQFDEVLLEESRVKRNPRFKDGRIHVLIYMINPTGHGLSDIDVKFLQHVNNLVNIIPIISKADSLTPKELKLNKELILEDLNNYGINFYKFNEYDYEQDYIDEEIIEYNKYLNSLIPFAIIGANEYRSNPNGSEDEDDILKLRILNKDFKPIDIDNAEINDFTILKNVLLVTHLNEFKDITHDSIYENYRTEALSGKQFQYVNKDSAKQEISESDYLMKEEQIKLEEERLRKFEERVHQDLINKRKELLERENELKEIEKRLLAEGLKFDENGDVVKVHEEESSENEVKVI
Protein: Rop guanine nucleotide exchange factor 12 (AtRopGEF12) (Protein MATERNAL EFFECT EMBRYO ARREST 64) (Rho of plants guanine nucleotide exchange factor 12) (Q9CA89)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. May be recruited by PRK2 at the plasma membrane to maintain polar Rop activity in the pollen tube and control polarized pollen tube growth.
Subcellular location: Cytoplasm. Cell membrane {ECO:0000269|PubMed:18000057}. Note=ROPGEF12 colocalizes with PRK2 at the apical plasma membrane of pollen tube. {ECO:0000269|PubMed:18000057}.
Interaction partners:
- Pollen receptor-like kinase 2
- Rac-like GTP-binding protein ARAC11
- Pollen receptor-like kinase 6
- Pollen receptor-like kinase 5
- Ras-related protein RABA4d
- CRIB domain-containing protein RIC1
- Pollen receptor-like kinase 1
- Receptor-like serine/threonine-protein kinase SD1-6
- Rac-like GTP-binding protein ARAC10
- Rac-like GTP-binding protein ARAC1
Sequence:
MVRASEQEQETYRSRLFNFKWRNNDNNSATRHNKSLSVETGLDEAATGSHDAEPLTIIHPSQGPPLSRSAADEAVLAALAASQARERQLLADMEQMKERFSKLLLGEDNSGGGKGVSSALALSNAITNLAASVFGEQRRLEPMPAERRARWRKEIDWLLSVTDYVVEFAPSQQKNKDGTNMEIMTTRQRTDLHMNIPALKKLDAMLIDCLENFKDQSEFSYISKDSPDLDGKRNDEKWWIPTVKVPPDGLSEASRRFLQYQKDCVNQVLKAAMAINAQVLFEMEIPESYIDSLPKNGRASLGDQMYKNITVDFFDPDQFLSSMDMSSEHKIVDLKNRIEASIIIWKRKMVYKDNKSSAPWASGVSLEKREVFEERAETILLILKQRYPGISQSSLDISKIQFNEDVGQAVLESYSRILESLAYTVLSRIDDVLEADRAGNKRNTPLEAEEETLVGSMTLSDFMGWDFDQAANAELESKKDLPDDPLIKEKLSVVTTKKTSYLETLGGVKSPTARH
Protein: AT25873p (Pummelig, isoform B) (Pummelig, isoform C (EC 3.1.1.-, EC 3.1.1.1, EC 3.3.2.10)) (Pummelig, isoform D) (Pummelig, isoform E) (Q7JQU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRAVEKKILSYVKLPYRGFFVDIGPAVGEADKIWTISMNTESKEVPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGGFIASSYALSHPERVKHLILADPWGFPEKPSDSTNGKTIPLWVRAIARVLTPLNPLWALRAAGPFGQWVVQKTRPDIMRKFQSTIEEDINLLPQYIHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRSDIPITFIYGSRSWIDSSSGEKIKSQRGSNMVDIKIVTGAGHHVYADKPDVFNRYVNETCDMYKVAGGKLITPLQLIRESTESDEEREPSLSTAKTVEVQPEVQPVPQPVTAADTSTPTADELAANIKPK
Protein: Dicarboxylate carrier SLC25A8 (Mitochondrial uncoupling protein 2) (UCP 2) (Solute carrier family 25 member 8) (UCPH) (P55851)
Organism: Homo sapiens (Human)
Function: Antiporter that exports dicarboxylate intermediates of the Krebs cycle in exchange for phosphate plus a proton across the inner membrane of mitochondria, a process driven by mitochondrial motive force with an overall impact on glycolysis, glutaminolysis and glutathione-dependent redox balance. Continuous export of oxaloacetate and related four-carbon dicarboxylates from mitochondrial matrix into the cytosol negatively regulates the oxidation of acetyl-CoA substrates via the Krebs cycle lowering the ATP/ADP ratio and reactive oxygen species (ROS) production. Proton transporter activity is debated, but if it occurs it may mediate inducible proton re-entry into the mitochondrial matrix affecting ATP turnover as a protection mechanism against oxidative stress. Proton re-entry may be coupled to metabolite transport to allow for proton flux switching and optimal ATP turnover (By similarity). Regulates the use of glucose as a source of energy. Required for glucose-induced DRP1-dependent mitochondrial fission and neuron activation in the ventromedial nucleus of the hypothalamus (VMH). This mitochondrial adaptation mechanism modulates the VMH pool of glucose-excited neurons with an impact on systemic glucose homeostasis (By similarity). Regulates ROS levels and metabolic reprogramming of macrophages during the resolution phase of inflammation. Attenuates ROS production in response to IL33 to preserve the integrity of the Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). Can unidirectionally transport anions including L-malate, L-aspartate and phosphate. Does not mediate adaptive thermogenesis (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P70406}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Leptin
- Peroxisome proliferator-activated receptor gamma
- Sterol regulatory element-binding protein 1
- Peroxisome proliferator-activated receptor alpha
- Appetite-regulating hormone
- Insulin
- Adiponectin
- Agouti-related protein
- Calcium uptake protein 1, mitochondrial
Sequence:
MVGFKATDVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGESQGPVRATASAQYRGVMGTILTMVRTEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKQFYTKGSEHASIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYQSTVNAYKTIAREEGFRGLWKGTSPNVARNAIVNCAELVTYDLIKDALLKANLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSALGQYSSAGHCALTMLQKEGPRAFYKGFMPSFLRLGSWNVVMFVTYEQLKRALMAACTSREAPF
Protein: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97) (Parahox neighbor) (Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase) (A1L259)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- 5-hydroxyisourate hydrolase
- Zgc:103559.
- 5-hydroxyisourate hydrolase
- Uricase
Sequence:
MDINVVNALAYEDFVKLFGNVVEKCPLISAAIWSYRPFKDLADIEARISEFIHSLPDSGKEGILRCHPDLAGRDLQSGTLTPESQEEQSQAGMTTLDSAEIVHMYRLNSEYKERFGFPFVICARLNNKADIVRQLSERLKNRRTAELECAIEEVKKICSLRLHSIVLSDIQTKL
Protein: DnaJ homolog subfamily C member 17 (D3ZSC8)
Organism: Rattus norvegicus (Rat)
Function: May negatively affect PAX8-induced thyroglobulin/TG transcription.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20160132}. Nucleus {ECO:0000269|PubMed:20160132}. Note=Predominantly nuclear. {ECO:0000269|PubMed:20160132}.
Interaction partners:
- Cell division cycle 5-like protein
Sequence:
MAVTKELLQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRKARKQAAERTQRLDEKRKKVKLDLEARERQAQAQGTEEEEESRSTTTLEQEIARLREEGSRQLEEQQRLIQEQIRQDREQRLRGRTENTEGKGTPKLKLKWKCKKEDESQGGYSRDILLRLLQKYGEVLNLVLSKKKAGNAIVEFATVRAAELAVRNEVGLADNPLKVSWLEGQPQGTVDPSPPGLSKGSVLSERDYESLVMMRMRQAAERQQLIAQMQQEDEGRPT
Protein: Trifunctional enzyme subunit beta, mitochondrial (TP-beta) [Includes: 3-ketoacyl-CoA thiolase (EC 2.3.1.155) (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase)] (Q60587)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P55084}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P55084}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55084}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55084}. Note=Protein stability and association with membranes require HADHA. {ECO:0000250|UniProtKB:P55084}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MTTILTSTFRNLSTTSKWALRFSVRPLSCSSQVQSAPAVQTKSKKTLAKPNLKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAQRLSLLTKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVSKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGAPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK
Protein: Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) (P63074)
Organism: Rattus norvegicus (Rat)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap. Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (By similarity). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development.
Subcellular location: Cytoplasm, P-body {ECO:0000250|UniProtKB:P06730}. Cytoplasm {ECO:0000250|UniProtKB:P06730}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P06730}. Nucleus {ECO:0000250|UniProtKB:P06730}. Nucleus speckle {ECO:0000250|UniProtKB:P06730}. Nucleus, nuclear body {ECO:0000250|UniProtKB:P63073}. Note=Interaction with EIF4ENIF1/4E-T is required for localization to processing bodies (P-bodies). Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism (By similarity). Sequestered in the nucleus by EIF4EBP1 and EIF4EBP2 (By similarity). {ECO:0000250|UniProtKB:P06730, ECO:0000250|UniProtKB:P63073}.
Interaction partners:
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 4 gamma, 3
- Eukaryotic translation initiation factor 4E-binding protein 1
- Eukaryotic translation initiation factor 4 gamma 1
- Cytoplasmic FMR1-interacting protein
- Polyadenylate-binding protein 1
- Eukaryotic translation initiation factor 4, gamma 2.
- RNA helicase
- Nuclear cap-binding protein subunit 1
- Eukaryotic translation initiation factor 4E binding protein 2
Sequence:
MATVEPETTPTTNPPPAEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q8T3C1)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MARAVNISPFASYTVVPITSAWPPDDLKADRVQLASFTTGKALLAIAILAMIIMTTVGNALVCLAVLLVRKLKHPQNFLLVSLAVADFFVGLVVMPLALIDLLFDKWPLGSTMCSVYTTSDLTLCTASIVNLCAISVDRYLVISSPLRYSAKRTTKRIMMYIACVWIIAAIVSISSHIIANLLNDGTYVDDTGTCQVIPHFIYQSYATIISFYAPTFIMVILNIKIWRAAKRLAAQDRLMSHCNSVDASERPRNGSAETKDFLNEKETIDVPKKERANSTNSRLFKLERKYLHRPSAFFSAAKGPLIRQTEKSECKARKTLGVIMSVFIICWLPFFILAIFKSFGMWIPDWLDLLALWLGYSNSTLNPLIYCKYNKEFRIPFREMLACRCATLQTVMRQQSFTSRYGPPVSRRNDSHEASDV
Protein: FCS-Like Zinc finger 13 (Q8GRN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:24600465}. Cytoplasm {ECO:0000269|PubMed:24600465}. Note=Shuttles from the cytoplasm to the nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}.
Interaction partners:
- RING-H2 finger protein ATL75
- Probable LRR receptor-like serine/threonine-protein kinase At4g37250
- AT5g23340/MKD15_20
- At4g27652
- At1g66080
- Protein indeterminate-domain 11
- At4g27654
- GEM-like protein 6
- Vesicle-associated protein 2-1
- Expressed protein
Sequence:
MILSKRPHLMIRKLSEMLVPRSRSAAIKPEEYTASPRSPLDLNFPSPVHSKRFGSGGVGLGIVAALEETSNGINRHDPVRYSGRFRCPEIDLSDEEYTYVTSPNGPTKVYYNDDGFELSENDYRRVHKPMVTVDEPPVIERQSVRGPTEFLSSCCLCKKKLQGKDIYMYKGEMGFCSAECRSVQIMNDERQEQCKTQVSRNADVLSSPYAAGQRLSAGVFVF
Protein: Anaphase-promoting complex subunit SWM1 (Anaphase-promoting complex subunit 13) (Spore wall maturation protein 1) (Q12379)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. SWM1 is required for APC/C activity in meiosis.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit CDC23
- Anaphase-promoting complex subunit CDC26
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit DOC1
Sequence:
MSSSSYRDSYFQYRHLPAPHHILYAEWNQDILALPDEVANITMAMKDNTRTDAEEGRAPQDGERNSNVRESAQGKALMTSEQNSNRYWNSFHDEDDWNLFNGMELESNGVVTFAGQAFDHSLNGGTNSRNDGANEPRKETITGSIFDRRITQLAYARNNGWHELALPQSR
Protein: U6 snRNA-associated Sm-like protein LSm3 (SmX4 protein) (P57743)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM3 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM3, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM3 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Deadenylation-dependent mRNA-decapping factor PAT1
- LSM complex subunit LSM7
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein-associated protein B
- LSM complex subunit LSM6
- Small nuclear ribonucleoprotein E
- Pre-mRNA-splicing helicase BRR2
- Small nuclear ribonucleoprotein F
- U4/U6 snRNA-associated-splicing factor PRP24
Sequence:
METPLDLLKLNLDERVYIKLRGARTLVGTLQAFDSHCNIVLSDAVETIYQLNNEELSESERRCEMVFIRGDTVTLISTPSEDDDGAVEI
Protein: Paraneoplastic antigen-like protein 5 (Tumor antigen BJ-HCC-25) (Q96PV4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:31429579}.
Interaction partners:
Sequence:
MALTLLEDWCKGMDMDPRKALLIVGIPMECSEVEIQDTVKAGLQPLCAYRVLGRMFRREDNAKAVFIELADTVNYTTLPSHIPGKGGSWEVVVKPRNPDDEFLSRLNYFLKDEGRSMTDVARALGCCSLPAESLDAEVMPQVRSPPLEPPKESMWYRKLKVFSGTASPSPGEETFEDWLEQVTEIMPIWQVSEVEKRRRLLESLRGPALSIMRVLQANNDSITVEQCLDALKQIFGDKEDFRASQFRFLQTSPKIGEKVSTFLLRLEPLLQKAVHKSPLSVRSTDMIRLKHLLARVAMTPALRGKLELLDQRGCPPNFLELMKLIRDEEEWENTEAVMKNKEKPSGRGRGASGRQARAEASVSAPQATVQARSFSDSSPQTIQGGLPPLVKRRRLLGSESTRGEDHGQATYPKAENQTPGREGPQAAGEELGNEAGAGAMSHPKPWET
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0K3AYG7)
Organism: Kibdelosporangium sp. MJ126-NF4
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}.
Interaction partners:
Sequence:
MTEDSGIRELAGRYRLITPLGRRMMRGWDLHLRQVVAVRLFGQQNEPELFLDRASALTDLAHPGLVRVLDAGVADDGEPFVVQEFIAGTTLKARLANGVLTANTVTELGSTLGRALAYAHAQGVAHRSIHPGTIMLGPGQEPCFTDVGVTERSPVSYLAPEQAYGEDPTMASDVYSFGLVLLEALTGRTEYAGDSATTALARLSRAPIIDQNLPHAAALRAMLCPNPNDRPDAATCVDLLRGSSARSRVQTRTVLVAAVAAAMAATGITIVMTLSKQQPQPLVEPRVAPQETVTAEVTVPPPAIPTITEFVDRTADRAARQKTDRPAPGTGPAADVRSLAIAQAVHDQPTAPVPTTTPPTSAPDWSPWRPWEQIAHAKKKHRPWPVSPPSPLPRGGDKDDEN
Protein: mgtA leader peptide (Regulatory leader peptide for mgtA) (E2JKY7)
Organism: Escherichia coli (strain K12)
Function: Makes mgtA transcription sensitive to intracellular proline levels. Under low levels of proline this protein cannot be fully translated, and a stem loop forms which permits transcription of the downstream mgtA gene (By similarity).
Interaction partners:
- Magnesium-transporting ATPase, P-type 1
- fur leader peptide
Sequence:
MEPDPTPLPRRRLKLFR
Protein: Somatostatin receptor 1 (Q9GKP7)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
SPSPCPGSCGEXSGSRGPGAGTADGMEEPGRNASQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANPILYGFLS