wanglab/gogpt-training-data huggingface dataset:
Protein: Taste receptor type 2 member 134 (T2R134) (T2R34) (Taste receptor type 2 member 23) (T2R23) (Q67ES7)
Organism: Rattus norvegicus (Rat)
Function: Putative taste receptor which may play a role in the perception of bitterness.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRCSLRGCVQGRGGKSGVSLSKFSPKKMSFFFIFMVIFCIQSLVALLQNGFLATVLGREWVRSQGLPAGDMIVACLAASRFCLHGVAIVNNFLTFVKLWSQKIYFSVLWDFVNTVNFWCTTWLAIFYCVKISSFSHPIFFWIKWRISRSVPRLLLGSLVIGGLSAVSSATGNTIAFQMTACENYTLAYRTRAFYAYYFRCHAMLMWIIPFFLFLLSVILLMFSLYRHLEHMRYRRPWSHDYSTQAHTMALKSLAFFLVFYTSYVLFLVISVTRVVNVHSSWHWAWEVITYMGILLHSTILTLSNPKMRKALKIKFPDLCVARSQDKRRG
Protein: Sorting nexin (B0BNM3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}.
Interaction partners:
Sequence:
MATKARVMYDFAAEPGNNELTVNEGEIITITNPNVGGGWLEGKNSKGEQGLVPTDYVEILPNDGKDPFSCGNSVADQAFLDSLSASTAQANSSSANSNNQVGGGSDPWSAWNAPRSGNWDSSDAWGTRTDGAGAQRNSSANNWDTGFGHPQAYQGPATGDDDEWDEDWDDPKSSSPYFKDSEPAEAGGIQRGNSRAGASSMKLPLNKFPGFAKPGMEQYLLAKQLAKPKEKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVVSESEVFQQFLNFRDEKEWKTGKRKAEKDELVGVMIFSTMEPEAPDLDLIEIEQKCDAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLAAVFSSSGYQGETDLNNAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGAHKGAIEKVKESDKLVATSKITPQDKQTMVKRVGTMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALGRFPVM
Protein: 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31) (C8VUB6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconate dehydrogenase, decarboxylating
- Gluconokinase
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetyl-D-glucosamine kinase
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Transaldolase
Sequence:
MPGPAPNLFSFQDTDALAKQLRPYVLRNQNAALSRHNTFRVAVSGGSLPTVLAKALLAPGDGTPEDTAQFSKWEIFFADERAVPLDHEDSNYRLLKDELLSKIPSELGSPNVHTIDEKHVNGDPQELADLYQEELMRSFAAKDSVKLPVFDLILLGCGPDGHTCSLFPGHELLREKDAWVSAISDSPKPPPKRITLTLPVVTHAVSIAFVATGGGKKDILKQIFDAEEGRSLPSALVNQGGGEKVSWFTDHAAVDGVAFPRRGSL
Protein: Dormancy associated translation inhibitor (DATIN) (P9WMA9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in translation regulation. Inhibits protein synthesis and decreases bacterial growth when expressed in E.coli. Can also stimulate macrophages and peripheral blood mononuclear cells (PBMC) to secrete important cytokines that may be significant in granuloma formation and its maintenance. Increases secretion of IFN-gamma, TNF-alpha, IL-1 beta and IL-8 through human Toll-like receptor 2 (TLR2) signaling pathway.
Interaction partners:
- Uncharacterized protein Rv0080
- Universal stress protein Rv3134c
- Uncharacterized protein Rv1738
- Small ribosomal subunit protein uS9
- Universal stress protein Rv1996
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS7
Sequence:
MEPKRSRLVVCAPEPSHAREFPDVAVFSGGRANASQAERLARAVGRVLADRGVTGGARVRLTMANCADGPTLVQINLQVGDTPLRAQAATAGIDDLRPALIRLDRQIVRASAQWCPRPWPDRPRRRLTTPAEALVTRRKPVVLRRATPLQAIAAMDAMDYDVHLFTDAETGEDAVVYRAGPSGLRLARQHHVFPPGWSRCRAPAGPPVPLIVNSRPTPVLTEAAAVDRAREHGLPFLFFTDQATGRGQLLYSRYDGNLGLITPTGDGVADGLA
Protein: Small proline-rich protein 2A (SPR-2A) (2-1) (P35326)
Organism: Homo sapiens (Human)
Function: Gut bactericidal protein that selectively kills Gram-positive bacteria by binding to negatively charged lipids on bacterial membranes, leading to bacterial membrane permeabilization and disruption. Specifically binds lipids bearing negatively charged headgroups, such as phosphatidic acid, phosphatidylserine (PS), cardiolipin (CL), and phosphatidylinositol phosphates, but not to zwitterionic or neutral lipids. Induced by type-2 cytokines in response to helminth infection and is required to protect against helminth-induced bacterial invasion of intestinal tissue (By similarity). May also be involved in the development of the cornified envelope of squamous epithelia; however, additional evidences are required to confirm this result in vivo.
Subcellular location: Secreted {ECO:0000269|PubMed:34735226}. Secreted, extracellular space {ECO:0000269|PubMed:34735226}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:34735226}. Note=Present in intestinal secretory epithelial cells and is secreted into the intestinal lumen. {ECO:0000269|PubMed:34735226}.
Interaction partners:
- Cornifin-A
- Cornifin-B
- Late cornified envelope protein 3D
- Small proline-rich protein 2E
- Late cornified envelope protein 3E
- Small proline-rich protein 2D
- Small proline-rich protein 2F
- Small proline-rich protein 3
- Late cornified envelope protein 3A
- Late cornified envelope protein 2D
Sequence:
MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPCPPQQCQQKYPPVTPSPPCQSKYPPKSK
Protein: Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B) (P62995)
Organism: Homo sapiens (Human)
Function: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:9212162, ECO:0000269|PubMed:9546399}.
Interaction partners:
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 3
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 9
- Serine/arginine-rich splicing factor 7
- Serine/arginine-rich splicing factor 6
- RNA-binding motif protein, X chromosome
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Serine/arginine-rich splicing factor 10
Sequence:
MSDSGEQNYGERESRSASRSGSAHGSGKSARHTPARSRSKEDSRRSRSKSRSRSESRSRSRRSSRRHYTRSRSRSRSHRRSRSRSYSRDYRRRHSHSHSPMSTRRRHVGNRANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHTPTPGIYMGRPTYGSSRRRDYYDRGYDRGYDDRDYYSRSYRGGGGGGGGWRAAQDRDQIYRRRSPSPYYSRGGYRSRSRSRSYSPRRY
Protein: EF-hand calcium-binding domain-containing protein 9 (Q9DAM2)
Organism: Mus musculus (Mouse)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. pH-dependent Ca(2+) sensor required to activate the CatSper channel. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Associates with the CatSper complex via direct interaction with CATSPERZ, and senses intracellular Ca(2+). Together with CATSPERZ, associates with the CatSper channel pore and is required for the two-row structure of each single CatSper channel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31056283}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:31056283}. Note=Localizes to the principal piece of the sperm tail. {ECO:0000269|PubMed:31056283}.
Interaction partners:
- Cation channel sperm-associated auxiliary subunit zeta
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated protein 3
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated protein 2
- Solute carrier organic anion transporter family member 6C1
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated auxiliary subunit gamma 2
Sequence:
MKLTPGCFLWYLYMDKIYCLLSLRNVKALMVYFHLLDVHHRNTLNDVLFFHFLQHVTNLNKSQIGMIFDLLDWTAVGEIGFDQFYVLICILLAHQDHLEDHFMYRHSRPVFELLDLDGEMNIGAANFQNYRFLFNIKKQELRDLFHDFDITGDRLLNYKEFKLYTIFCTDKSIDRKKRRKDREAAREREKEKGKDKEKYLHLKKIYSSMLSHRSIL
Protein: AGAP007033-PA (A7URS6)
Organism: Anopheles gambiae (African malaria mosquito)
Interaction partners:
- AGAP006348-PA
- AGAP010815-PA
- AGAP010815-PA
- TEP1-F
- TEP1-F
Sequence:
MCWLHAVSLISVIFFTCGSVAAVGGNNYWYTEEQPVATTKPSFHVNGYNIYGSQPANGGLPANGGPTYRSETNFGGQPANGGLPANGGLPANGGLPANGGLLANGGLPANGGLPAKRGQLPYGTPTHIGQTIYRSQPNYGGQQRYNARPRQLEYKCIEGNLQYDCVFYDVHIDMQTQDVYFGFEDITLNNQKIVTFKNSTMRKLPAALLASFRQVEVLNLNGLQIEQIDTNAFAYAHTIQKLYMGFNAIRYLPPYVFQNVPLLTVLVLERNDLTSLPRGIFHNTPKLSMLSMSNNNLERIEDDTFQATTALQNLQLSSNRLTHVDLSLIPSLFHVNVSYNLLSTLAIPIAVEELDASHNSINAVRGPVNVELTILKLQHNNLTDTAWLLNYPGLVDVDLSYNQLEKITYQHFVKMQRLERLYVSNNHLVALNLYSQPIPTLKVLDLSHNHLLHVERNQPQFDRVEYLYLDHNSIVTLKLSTSHTLKNLTLSHNDWDCNSLRALFRNVAHPAVHDADQHCKIDYQLEQGLCCKESDKPYLDRLLQYIALTSVVEKLQRAQGRCSATDTINSVQSLSHYITQQGDVPLQGNEQLEAEVNELRAEVQQLTNEQIQQEQLLQGLHAEIDTNLRRYRLPKDGLARSSDNLNKVFTHLKERHAFKLRETQARRTEANAKQKETEDLEQENIALEKQLDNKKAKQAELRQETSQKRQKVKQLEAKKNRNPDTRRVTK
Protein: RE17490p (Q5BIB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
STFVFLAKMMRNALLVSGKLRHLLSCSIGRNSTRSSSTAKSLDAGTQKEVRHHENHASEWWNQNGTMGALHALNEIRVPFIRDGIVSRGTVKPGYVNTTKVLLGQNILEVGCGGGLLTEHLARLGAQVAGIDLGEKLIEAAREHLKCSSPELASNVVYKIEPVDQHAKANCECYDAVIVSEVLEHVKDKVSLLEASVRSLKPGGSIFITTLNKTIPSWFGGVLLSEYVLNLVPRGTHHWDKMISPLDVQRILDTMNCQTVLVNGSTYDFWSNTWRWINNNQMCYALQAVKQAQREYN
Protein: Endoplasmic reticulum oxidoreductins 2 (F4IU09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004367}; Lumenal side {ECO:0000256|ARBA:ARBA00004367}.
Interaction partners:
Sequence:
MAETDVGSVKGKEKGSGKRWILLIGAIAAVLLAVVVAVFLNTQNSSISEFTGKICNCRQAEQQKYIGIVEDCCCDYETVNRLNTEVLNPLLQDLVKTPFYRYFKVKLWCDCPFWPDDGMCRLRDCSVCECPESEFPEVFKKPLSQYNPVCQEGKPQATVDRTLDTRAFRGWTVTDNPWTSDDETDNDEMTYVNLRLNPERYTGYIGPSARRIWEAIYSENCPKHTSEGSCQEEKILYKLVSGLHSSISVHIASDYLLDEATNLWGQNLTLLYDRVLRYPDRVQNLYFTFLFVLRAVTKAEDYLGEAEYETGNVIEDLKTKSLVKQVVSDPKTKAACPVPFDEAKLWKGQRGPELKQQLEKQFRNISAIMDCVGCEKCRLWGKLQILGLGTALKILFTVNGEDNLRHNLELQRNEVIALMNLLHRLSESVKYVHDMSPAAERIAGGHASSGNSFWQRIVTSIAQSKVPSEVNIEWVEKRE
Protein: Dammarenediol 12-hydroxylase (EC 1.14.14.120) (Cytochrome P450 CYP716A47) (Protopanaxadiol synthase) (PgPPDS1) (H2DH16)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway. Catalyzes the hydroxylation of dammarenediol-II at the C-12 position to yield protopanaxadiol in ginsenoside biosynthesis, a class of tetracyclic triterpenoid saponins.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAAMVLFFSLSLLLLPLLLLFAYFSYTKRIPQKENDSKAPLPPGQTGWPLIGETLNYLSCVKSGVSENFVKYRKEKYSPKVFRTSLLGEPMAILCGPEGNKFLYSTEKKLVQVWFPSSVEKMFPRSHGESNADNFSKVRGKMMFLLKVDGMKKYVGLMDRVMKQFLETDWNRQQQINVHNTVKKYTVTMSCRVFMSIDDEEQVTRLGSSIQNIEAGLLAVPINIPGTAMNRAIKTVKLLTREVEAVIKQRKVDLLENKQASQPQDLLSHLLLTANQDGQFLSESDIASHLIGLMQGGYTTLNGTITFVLNYLAEFPDVYNQVLKEQVEIANSKHPKELLNWEDLRKMKYSWNVAQEVLRIIPPGVGTFREAITDFTYAGYLIPKGWKMHLIPHDTHKNPTYFPSPEKFDPTRFEGNGPAPYTFTPFGGGPRMCPGIEYARLVILIFMHNVVTNFRWEKLIPNEKILTDPIPRFAHGLPIHLHPHN
Protein: Uncharacterized protein (Q381L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTSITNFVKRVGTSLQHDVRTFTVWDPIGNKVHCAARDAVYLVMDCPKFFMYTHGAYGAMRRYIRQARINKGKVNPEDFRDVDTNVLRESLIRYAQWKGPLQKIDFRVFYWMYVLMIGYVFWQGLALNRMLEEKIDRSGVSLDKRRSMFDDDYEEDLRPQ
Protein: cAMP responsive element binding protein 1 (cDNA, FLJ93156, Homo sapiens cAMP responsive element binding protein 1 (CREB1),transcript variant B, mRNA) (Q5U0J5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQSSCKDLKRLFSGTQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD
Protein: Na(+)-translocating NADH-quinone reductase subunit B (Na(+)-NQR subunit B) (Na(+)-translocating NQR subunit B) (EC 7.2.1.1) (NQR complex subunit B) (NQR-1 subunit B) (Q56587)
Organism: Vibrio alginolyticus
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00426}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- Ion-translocating oxidoreductase complex subunit A
- FAD:protein FMN transferase
- Electron transport complex subunit RsxE
- NADP-dependent oxidoreductase
- Quinone oxidoreductase
Sequence:
MALKKFLEDIEHHFEPGGKHEKWFALYEAVATVFYTPGIVTNKSSHVRDSVDLKRIMIMVWFAVFPAMFWGMYNAGGQAIAALNHMYAGDQLATVISGNWHYWLTEMLGGTIAADAGVGSKMLLGATYFLPIYATVFLVGGFWEVLFCMVRKHEVNEGFFVTSILFALIVPPTLPLWQAALGITFGVVVAKEIFGGTGRNFLNPALAGRAFLFFAYPAQISGDVVWTAADGFSGATALSQWAQGGNGALVNTVTGSPITWMDAFIGNIPGSIGEVSTLALMIGAAMIVYMRIASWRIIAGVMIGMIAVSTLFNVIGSDTNPMFNMPWHWHLVLGGFAFGMFFMATDPVSASFTNKGKWWYGILIGAMCVMIRVVNPAYPEGMMLAILFANLFAPLFDHVVIEKNIKRRLARYGK
Protein: Homeotic protein bicoid (PRD-4) (P09081)
Organism: Drosophila melanogaster (Fruit fly)
Function: Segment polarity protein that provides positional cues for the development of head and thoracic segments. Regulates the expression of zygotic genes, possibly through its homeodomain, and inhibits the activity of other maternal gene products. May also bind RNA. Interacts with Bin1 to repress transcription of bicoid target genes in the anterior tip of the embryo; a process known as retraction.
Subcellular location: Nucleus.
Interaction partners:
- Protein hunchback
- Maternal effect protein oskar
- Zygotic gap protein knirps
- Poly
- Maternal effect protein staufen
- Protein tailless
- Maternal protein exuperantia
- Protein gurken
- LD47944p
- Transcription factor Zelda
Sequence:
MAQPPPDQNFYHHPLPHTHTHPHPHSHPHPHSHPHPHHQHPQLQLPPQFRNPFDLLFDERTGAINYNYIRPYLPNQMPKPDVFPSEELPDSLVMRRPRRTRTTFTSSQIAELEQHFLQGRYLTAPRLADLSAKLALGTAQVKIWFKNRRRRHKIQSDQHKDQSYEGMPLSPGMKQSDGDPPSLQTLSLGGGATPNALTPSPTPSTPTAHMTEHYSESFNAYYNYNGGHNHAQANRHMHMQYPSGGGPGPGSTNVNGGQFFQQQQVHNHQQQLHHQGNHVPHQMQQQQQQAQQQQYHHFDFQQKQASACRVLVKDEPEADYNFNSSYYMRSGMSGATASASAVARGAASPGSEVYEPLTPKNDESPSLCGIGIGGPCAIAVGETEAADDMDDGTSKKTTLQILEPLKGLDKSCDDGSSDDMSTGIRALAGTGNRGAAFAKFGKPSPPQGPQPPLGMGGVAMGESNQYQCTMDTIMQAYNPHRNAAGNSQFAYCFN
Protein: Bifunctional arginine demethylase and lysyl-hydroxylase psr-1 (EC 1.14.11.-) (Phosphatidylserine receptor 1) (Q9GYI4)
Organism: Caenorhabditis elegans
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cell death abnormality protein 2
- CED-5
- Transthyretin-like protein 52
- Cell death protein 6
- ABC transporter ced-7
- Cell death abnormality protein 1
- Cell death abnormality protein 12
- Ras-related protein ced-10
- Histone H4
Sequence:
MSLGRDRYSLPRTYKRVSHAKDKARPELRKFGWETLGYSESFNLPPFRDSIQRVDGNNLTVEEFRRDFERPRIPVIITGLTDNWAAKDKWTVERLSKKYRNQNFKCGEDDNGNSVRMKMKYYHDYMLNNKDDSPLYIFDSSFAERRKTKKLSEDYSVPKFFEDDLFHYADDKKRPPHRWFVMGPARSGTAIHIDPLGTSAWNSLLQGHKRWVLIPPIAPRDLVKPMAHEKGKHPDEGITWFQTVYKRVRSPSWPKEYAPIECRQGPGETMFVPSGWWHVVINEEYTIAVTHNYCSVENLHLVWPKTVKGRPKLSKHWVKRLTEQRPELLEIIKSASEIPLYDMNESSSDSSSSSSSSDDSSDESDCDDSGRCGGRKRKNDDRSNECPEKMSTTYFQNSLV
Protein: Large ribosomal subunit protein eL15 (60S ribosomal protein L15) (P61313)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein eS10
Sequence:
MGAYKYIQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSVAEERAGRHCGALRVLNSYWVGEDSTYKFFEVILIDPFHKAIRRNPDTQWITKPVHKHREMRGLTSAGRKSRGLGKGHKFHHTIGGSRRAAWRRRNTLQLHRYR
Protein: Large-conductance mechanosensitive channel (P0A742)
Organism: Escherichia coli (strain K12)
Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. Participates in the regulation of osmotic pressure changes within the cell. Opens at a pressure just below that which would cause cell disruption and death. The force required to trigger channel opening depends on the membrane lipids composition.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00115, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23416054, ECO:0000269|PubMed:7511799, ECO:0000269|PubMed:8890153, ECO:0000269|PubMed:9632260, ECO:0000305|PubMed:21151884, ECO:0000305|PubMed:23875651}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00115, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8890153}.
Interaction partners:
- Small-conductance mechanosensitive channel
- Mechanosensitive channel MscK
- Mechanosensing system component YbdG
- Moderate conductance mechanosensitive channel YbiO
- Low conductance mechanosensitive channel YnaI
- Miniconductance mechanosensitive channel MscM
- Aquaporin Z
- 6,7-dimethyl-8-ribityllumazine synthase
- S-adenosylmethionine synthase
- Trk system potassium uptake protein TrkA
Sequence:
MSIIKEFREFAMRGNVVDLAVGVIIGAAFGKIVSSLVADIIMPPLGLLIGGIDFKQFAVTLRDAQGDIPAVVMHYGVFIQNVFDFLIVAFAIFMAIKLINKLNRKKEEPAAAPAPTKEEVLLTEIRDLLKEQNNRS
Protein: Kinesin-like protein KIN-14A (Geminivirus Rep-interacting motor protein) (Geminivirus replication protein-interacting protein) (Kinesin CDKA-1-associated protein 1) (Kinesin-like protein KCA1) (Kinesin-like protein for actin-based chloroplast movement 1) (Q9LX99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinesin-like protein required for chloroplast movements and anchor to the plasma membrane. Mediates chloroplast movement via chloroplast actin (cp-actin) filaments. Required for the chloroplast avoidance response under high intensity blue light. Mediates redundantly with CHUP1 the nuclear avoidance response under high intensity blue light. May act as a mitotic kinesin. Probably involved in division plane determination.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome. Cell membrane. Cytoplasm, cytoskeleton, phragmoplast. Note=Localizes to the spindle apparatus and condensed chromosomes in mitotic cells. Localizes in the forming cell plate and the cortical division zone (CDZ) during cytokinesis.
Interaction partners:
- Protein CHUP1, chloroplastic
- Protein PLASTID MOVEMENT IMPAIRED 1
- Protein PLASTID MOVEMENT IMPAIRED 1-RELATED 1
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Plastid division protein CDP1, chloroplastic
- Protein WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT 1
- Uncharacterized protein At1g66480
- Plastid division protein PDV1
- Cyclin-dependent kinase A-1
- Kinesin-like protein KIN-10A
Sequence:
MADQRSKTNRWNWEVSGFEPRKSSSNASFAESTGHRTTGPLLRRNSISTPSLPPKQAIASKVNGLKEKVKLAKEDYLELRQEATDLQEYSNAKLDRVTRYLGVLAEKSRKLDQFVLETEARISPLINEKKRLFNDLLTAKGNIKVFCRARPLFEDEGPSVIEFPGDCTICVNTSDDTLSNPKKDFEFDRVYGPHVGQAALFSDVQPFVQSALDGSNVSILSYGQTNAGKTYTMEGSNHDRGLYARCFEELFDLANSDSTSTSRFSFSLSVFEIYNEQIRDLLSETQSNLPNINMDLHESVIELGQEKVDNPLEFLGVLKSAFLNRGNYKSKFNVTHLIVSIHIYYSNTITGENIYSKLSLVDLAGSEGLIMENDSGDHVTDLLHVMNSISALGDVLSSLTSGKDSIPYDNSILTRVLADSLGGSSKTLMIVNICPSVQTLSETISCLNYAARARNTVPSLGNRDTIKKWRDVASDARKELLEKERENQNLKQEVVGLKKALKDANDQCVLLYSEVQRAWKVSFTLQSDLKSENIMLVDKHRLEKEQNSQLRNQIAQFLQLDQEQKLQMQQQDSAIQNLQAKITDLESQVSEAVRSDTTRTGDALQSQDIFSPIPKAVEGTTDSSSVTKKLEEELKKRDALIERLHEENEKLFDRLTERSMAVSTQVLSPSLRASPNIQPANVNRGEGYSAEAVALPSTPNKNNGAITLVKSGTDLVKTTPAGEYLTAALNDFDPEEYEGLAAIADGANKLLMLVLAAVIKAGASREHEILAEIRDSVFSFIRKMEPRRVMDTMLVSRVRILYIRSLLARSPELQTIRVSPVECFLEKPNTGRSKSTSRGSSPGRSPVRYLDTQIHGFKVNIKAERRNKLASVVSRMRGLEQDAGRQQVTGVKLREMQDEAKSFAIGNKALAALFVHTPAGELQRQIRLWLAENFEFLSVTSDDVSGGNGGQLELLSTAIMDGWMAGLGAAVPPHTDALGQLLSEYAKRVYTSQMQHMKDIAGTLAAEEAEDAGQVSKLRSALESVDHKRRKILQQMKSDAALLNLEEGSSPIPNPSTAAEDSRLASLISLDGILKQVKEITRQASVHVLSKSKKKALLESLDELTERMPSLLDIDHPCAQREIATAHQLVETIPEQEDTNILEQSHDRRPSLESISSGETDVSQWNVLQFNTGSSAPFIIKCGGNNNSELVIKADARVQEPKGGEIVRVVPRPSVLVNMSLEEMKQMFVQLPEALSLLALARTADGTRARYSRLYKTLAMKVPSLKDLVSELE
Protein: Decapping protein 2, isoform B (Decapping protein 2, isoform D) (SD14939p) (Q86NM7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MELNNLIRMCFQIELAHWFYLDFFCAPESGEDGETPKCVQRKLPSVGIKQFAMQLFQHIPFLNKHFGTVDQILDEWKNYKLSVPTYGAILVSEDHNHCLLVQSYFARNSWGFPKGKINENEDPAHCATREVYEETGFDITDLIDANDYIEAFINYQYTRLYVVRNIPMDTQFAPRTRNEIKCCDWFRIDALPVNKNDAISKAKLGKTSNSFFMIMPFVKRLKKWVNDRKAGIEPRRRKFSGQQSPKAASPTNMNGNCKKDVTGVRNESQRQRHKSMGDLDGVKLNNLNGKGTVGTGAGSAASASATAAINSMNICNSNGKRNKQNAAAGSNQATPTTIATPMTSNGAVVGGTVSSKRQLFHSQSQNDAQQSASNEKIVSSFDLIRKEKQQQLKAAKAQKQQQQQQQRSRTKSQSDKQYNPQQPVKILGQQQPTTGMDLIAMLSAAAAAQKTPNNEQQTQEKQQQQQRPRPASVSLNLGAGSATGATTSAPDAQYMHRLQRMASGTNLRILKRAQSQQPQQHHQQQLQLEQQQQQQQQLGIDFTPNLNSWTNFSFTKNFIANVFC
Protein: 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH) (Q5SIY4)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MKVAVLPGDGIGPEVTEAALKVLRALDEAEGLGLAYEVFPFGGAAIDAFGEPFPEPTRKGVEEAEAVLLGSVGGPKWDGLPRKIRPETGLLSLRKSQDLFANLRPAKVFPGLERLSPLKEEIARGVDVLIVRELTGGIYFGEPRGMSEAEAWNTERYSKPEVERVARVAFEAARKRRKHVVSVDKANVLEVGEFWRKTVEEVGRGYPDVALEHQYVDAMAMHLVRSPARFDVVVTGNIFGDILSDLASVLPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLEHAFGLVELARKVEDAVAKALLETPPPDLGGSAGTEAFTATVLRHLA
Protein: DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (Q587G4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367076}.
Interaction partners:
- RNA polymerase III subunit Rpc25 domain-containing protein
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase III subunit RPC6
- DNA-dependent RNA polymerases, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases II subunit, putative
Sequence:
MSRRAEALGALNPQQQQQIIHDEHPRMIGVQNELLETSVSEQLSPLAGFLVRTLNRCGPLTLKALAEAVRQEPFGNPLRSSKGGGASVSGGSVNEAVKQVSSPIPLPVTAPSDIVTDAAIKEIMTRLLLHRVVQHDPSSSTYSVALGYGLFLRTLFPVVVQFFQRNFGETGVTILMVFYQLAVVPWEAALRLATERRPALGEALRHCAREMEKLGLIEFLPDKLPGQAATASPSNAGSGTRVEGPGETVAADACLQELCRLHVPNILFEMLRDAIHRHLLAERFADGSGSNGGGSVASAIVEAFTASARCRRFSERVSGFPAARPPSSASMPLRALLREVPHPEPTVTEVLNRMCRAEGDNIMSCGGGAGVDALEGPYRFRYDAAVEAMQRDCCERMVFARHGVLGVRLIKLLLQHHHMEDRMLAEEAIATLPRTREVLHAMMRDGYVRQQEVPKTSTLTDRLPKNSIFLWGCNMESDLLPTVRLQVAMALRLTITRLAMERNNGVGPGTAMPTPMNIVASATATINGDVHPTGGSYESKHAVAALESSATALMDMMLVLDFY