wanglab/gogpt-training-data huggingface dataset:
Protein: D-galactonate dehydratase family member RspA (EC 4.2.1.-) (D-mannonate dehydratase) (EC 4.2.1.8) (Starvation sensing protein RspA homolog) (D8ADB5)
Organism: Escherichia coli (strain MS 21-1)
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
Sequence:
MHHDKRCKESNMKIVKAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELSVASYLQDHLCPQLIGRDAHRIEDIWQFFYKGAYWRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHSIDEALDDYARHQELGFKAIRVQCGIPGMKTTYGMSKGKGLAYEPATKGQWPEEQLWSTEKYLDFMPKLFDAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRMFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLSPVCMAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHNWTFDNGYMHSGDKPGLGIEFDEKLAAKYPYEPAYLPVARLEDGTLWNW
Protein: Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) (Q61166)
Organism: Mus musculus (Mouse)
Function: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules. Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (By similarity). May play a role in cell migration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:24706950}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15691}. Note=Associated with the microtubule network at the growing distal tip of microtubules (PubMed:21357749). In addition to localizing to microtubule plus-ends, also exhibits some localization along the length of the microtubules (By similarity). Also enriched at the centrosome (By similarity). {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:21357749}.
Interaction partners:
- CAP-Gly domain-containing linker protein 1
- Dynactin subunit 1
- Microtubule-associated protein RP/EB family member 3
- Serine/threonine-protein kinase PLK1
- CLIP-associating protein 2
- Cyclin-dependent kinase 1
- Kinesin-like protein KIF2C
- Microtubule-associated tumor suppressor candidate 2 homolog
- Mitotic checkpoint protein BUB3
- Kinesin-like protein KIF17
Sequence:
MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETAVAPSLVAPALSKPKKPLGSSTAAPQRPIATQRTTAAPKAGPGMVRKNPGVGNGDDEAAELMQQVKVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY
Protein: YTH domain-containing family protein 3 (Q8BYK6)
Organism: Mus musculus (Mouse)
Function: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3. The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. Acts as a negative regulator of type I interferon response by down-regulating interferon-stimulated genes (ISGs) expression: acts by binding to FOXO3 mRNAs. Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification. Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation (By similarity). Recognizes and binds m6A-containing circular RNAs (circRNAs); circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons (By similarity). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (By similarity). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (By similarity). May also recognize and bind N1-methyladenosine (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:32943573}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q7Z739}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q7Z739}.
Interaction partners:
- Eukaryotic translation initiation factor 4 gamma 2
- N
- YTH domain-containing family protein 2
- N
- YTH domain-containing family protein 1
- Pre-mRNA-splicing regulator WTAP
- RNA demethylase ALKBH5
- Protein virilizer homolog
- Alpha-ketoglutarate-dependent dioxygenase FTO
- RNA-binding protein 15
Sequence:
MSATSVDQRPKGQGNKVSVQNGSIHQKDAVNDDDFEPYLSSQTNQNNSYPPMSDPYMPSYYAPSIGFPYSLGEAAWSTAGDQPMPYLTTYGQMSNGEHHYIPDGVFSQPGALGNTPPFLGQHGFNFFPGNADFSTWGTSGSQGQSTQNSAYSSSYGYPPSSLGRAITDGQAGFGNDTLSKVPGISSIEQGMTGLKIGGDLTAAVTKTVGTALSSSGMTSIATNNVPPVSSAAPKPTSWAAIARKPAKPQPKLKPKGNVGIGGSAVPPPPIKHNMNIGTWDEKGSVVKAPPTQPVLPPQTIIQQPQPLIQPPPLVQSQLPQQQPQPPQPQQQQGPQPQAQPHQVQSQQPQLQNRWVAPRNRGTGFNQNNGTGSENFGLGVVPVSASPSSVEVHPVLEKLKAINNYNPKDFDWNLKNGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDAAYRSLNGKGPLYLLFSVNGSGHFCGVAEMKSVVDYNAYAGVWSQDKWKGKFEVKWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIIATFKHTTSIFDDFAHYEKRQEEEEAMRRERNRNKQ
Protein: Terminal flower 1a (B4XEW0)
Organism: Gossypium arboreum (Tree cotton) (Gossypium nanking)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAKLSDPLVVGRVIGDVIDALSPSVKMSVTFNTNKQVYNGHEFFPSAVTNKPKVEVHGGDMRSFFTLVMTDPDVPGPSDPYLREHLHWIVTDIPGTTDATFGREMVNYEMPRPNIGIHRFVFLLFKQKGRQTVRSIPSSRDRFDTRKFAEENELGVPVAAVYFNAQRETASRRR
Protein: Cadherin 96Cb, isoform B (Q9VBV6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MRINHQWIYYAILSLCWFNKATLGAILDSRCYLEGGGSAESFLATEDLAVGSIIGKLRINGDANAETGDINLSLREKNAPVEIHPGTKELALSVELDKEGVRGPSSIYVNVICIRRHSTDPSFVIPVNVRVTDVNDNAPQWIGTPYTLTLSEVTVPGTRILQGARAEDADQPGPFSTVEYQVLPGPYSEYVQFLNPLEGTLVLKKALDYEQLQNFTVKLRAQDQGTPPRHSDTLLRVVITDADDQNPKFQRESYSAEIPADGRPGELRMRPEPLKAVDQDEGICAPIQYTIVQSQDAKYFRIHPHNGAISLLTPIGYADVANGATLVVKATQIDNPDRYALTTVQLTRPGSHSDLSTLAFVQKRFVMRIREDTAVGNRILALPTNKPGKHLKYVIPDPVNSQFFSVGSLGELVLAKPLDYEKMTKHEFQVLATDGMTNSTAELTLEVIDVNDWEPRFRETHYEFMVPKSQSLQSRADSFEGVLIGKVEAADGDRNDKLELSLRGQHAGLFEIDSTGNIYMRPEQLQSLNESTVHLIAIATDTGVPPRSTSVPVSVTMEGLTLARSGWNSNMLGMFGMIMGLFLMIIVALSCYIVRSKKQGKSASSGLGLGRNRVHSQAHSSVSSANLVTHEKLAGNGNGNGASVTSGGVSVLHMKHGGNITMANPMNNGLHHVASGASSSMALGSSAALLERERERERDRERQRESYAATVRSIVSRASANGQLFEEDEIEHDSLQTENNNRKVAATGVASGGVTTISTTPANAGSNLLSATDAMGSSENNLTVYF
Protein: Eyes absent homolog (EC 3.1.3.48) (A0A8I6A7V1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDTQDLNEQSVKKTCPESDVSEPQNSRSMEMQDLASPHALVGGSDTPGSSKLDKSGLSSTSVTTNGTGVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPAYDLGVMLPAIKTESGLPQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTSSSTSTYQLQESLQGLTSQPGEFDTVQSPSTPIKDLDDRTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHATASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL
Protein: Antigen peptide transporter 2 (APT2) (EC 7.4.2.14) (ATP-binding cassette sub-family B member 3) (Peptide supply factor 2) (Peptide transporter PSF2) (PSF-2) (Peptide transporter TAP2) (Peptide transporter involved in antigen processing 2) (Really interesting new gene 11 protein) (RING11) (Q03519)
Organism: Homo sapiens (Human)
Function: ABC transporter associated with antigen processing. In complex with TAP1 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules. Uses the chemical energy of ATP to export peptides against the concentration gradient. During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle. Typically transports intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome. Binds peptides with free N- and C-termini, the first three and the C-terminal residues being critical. Preferentially selects peptides having a highly hydrophobic residue at position 3 and hydrophobic or charged residues at the C-terminal anchor. Proline at position 2 has the most destabilizing effect. As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1589036, ECO:0000269|PubMed:22638925}; Multi-pass membrane protein {ECO:0000255}. Note=The transmembrane segments seem to form a pore in the membrane.
Interaction partners:
- Antigen peptide transporter 1
- Tapasin
- HLA class I histocompatibility antigen, A alpha chain
- Beta-2-microglobulin
- Proteasome subunit beta type-9
- Protein disulfide-isomerase A3
- Calreticulin
- Proteasome subunit beta type-8
- HLA class I histocompatibility antigen, B alpha chain
- ABC-type oligopeptide transporter ABCB9
Sequence:
MRLPDLRPWTSLLLVDAALLWLLQGPLGTLLPQGLPGLWLEGTLRLGGLWGLLKLRGLLGFVGTLLLPLCLATPLTVSLRALVAGASRAPPARVASAPWSWLLVGYGAAGLSWSLWAVLSPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQALQDWNSRGDRTVLVIAHRLQTVQRAHQILVLQEGKLQKLAQL
Protein: dual-specificity kinase (EC 2.7.12.1) (A0A8I6G1T6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGGRHVAVKIVKNVDRYCEAAQSEIQVLEHLNATDPHSTFRCVQMLEWFEHRGHICIVFELLGLSTYDFIKENSFLPFRMDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVKSDYTEAYNPKMKRDERTIVNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSREHLAMMERILGPLPKHMIEKTRKRTYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDAEHELLFDLIGKMLEYDPAKRITLKEALKHPFFYPLKKHT
Protein: P2X purinoceptor 1 (P2X1) (ATP receptor) (Purinergic receptor) (P51575)
Organism: Homo sapiens (Human)
Function: Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10816552, ECO:0000269|PubMed:11809854}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}. Note=Detected at plasma membrane lipid rafts. {ECO:0000269|PubMed:20699225}.
Interaction partners:
- P2X purinoceptor 6
- P2X purinoceptor 3
- P2X purinoceptor 7
- P2X purinoceptor 5
- P2X purinoceptor 4
- P2Y purinoceptor 12
- P2Y purinoceptor 1
- P2Y purinoceptor 2
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 1
Sequence:
MARRFQEELAAFLFEYDTPRMVLVRNKKVGVIFRLIQLVVLVYVIGWVFLYEKGYQTSSGLISSVSVKLKGLAVTQLPGLGPQVWDVADYVFPAQGDNSFVVMTNFIVTPKQTQGYCAEHPEGGICKEDSGCTPGKAKRKAQGIRTGKCVAFNDTVKTCEIFGWCPVEVDDDIPRPALLREAENFTLFIKNSISFPRFKVNRRNLVEEVNAAHMKTCLFHKTLHPLCPVFQLGYVVQESGQNFSTLAEKGGVVGITIDWHCDLDWHVRHCRPIYEFHGLYEEKNLSPGFNFRFARHFVENGTNYRHLFKVFGIRFDILVDGKAGKFDIIPTMTTIGSGIGIFGVATVLCDLLLLHILPKRHYYKQKKFKYAEDMGPGAAERDLAATSSTLGLQENMRTS
Protein: Solute carrier family 15 member 3 (F5GZ36)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPASPLGPACPSAGCPRSSPSPYCAPVLYAGLLLLGLAASSVRSNLTSFGADQVMDLGRDATRRFFNWFYWSINLGAVLSLLVVAFIQQNISFLLGYSIPVGCVGLAFFIFLFATPVFITKPPMGSQVSSMLKLALQNCCPQLWQRHSARDRQCARVLADERSPQPGASPQEDIANFQVLVKILPVMVTLVPYWMVYFQMQSTYVLQGLHLHIPNIFPANPANISVALRAQGSSYTIPEAWLLLANVVVVLILVPLKDRLIDPLLLRCKLLPSALQKMALGMFFGFTSVIVAGVLEMERLHYIHHNETVSQQIGEVLYNAAPLSIWWQIPQYLLIGISEIFASIPGLEFAYSEAPRSMQGAIMGIFFCLSGVGSLLGSSLVALLSLPGGWLHCPKDFGNINNCRMDLYFFLLAGIQAVTALLFVWIAGRYERASQGPASHSRFSRDRG
Protein: Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] (P48831)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular location: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000250|UniProtKB:P21754}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Zona pellucida glycoprotein 4.
- Oviductal glycoprotein 1
- Beta-1,4-galactosyltransferase 1.
- Folliculogenesis specific bHLH transcription factor.
- Growth differentiation factor 9.
Sequence:
MGLSYGIFICFLLLGGMELCCPQTIWPTETYYPLTSRPPVMVDCLESQLVVTVSKDLFGTGKLIRPADLTLGPENCEPLVSMDTDDVVRFEVGLHECGSRVQVTDNALVYSTFLIHSPRPAGNLSILRTNRAEVPIECHYPRHSNVSSQAILPTWVPFRTTMLFEEKLVFSLRLMEEDWGSEKQSPTFQLGDIAHLQAEVHTGSHMPLRLFVDHCVATLTPDRNAFLHHKIVDFHGCLVDGLYNSSSAFKAPRPRPETLQFTVDVFHFAKDSRNTIYITCHLKVTPADRVPDQLNKACSFIKSTKRWYPVEGSADICRCCNKGSCGLPGRSRRLSHLERGWRKSVSHTRNRRHVTEEAEITVGPLIFLGKASDHGIEGSTSPHTSVMLGLGLATVVSLTLATIVLVLAKRHRTASHPVICPASVSQ
Protein: Actin-10 (EC 3.6.4.-) (Q54GX7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 1
Sequence:
MEGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF
Protein: Twinkle homolog protein, chloroplastic/mitochondrial (DNA helicase) (EC 3.6.4.12) (DNA primase) (EC 2.7.7.-) (B5X582)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has both DNA primase and DNA helicase activities and may be involved in organelle DNA replication. Capable of producing RNA primers of 9 to 18 bases from a single-stranded DNA template.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:23452619}. Mitochondrion {ECO:0000269|PubMed:19036033, ECO:0000305|PubMed:23452619}.
Interaction partners:
- Sucrase-like protein
- DNA polymerase I B, chloroplastic/mitochondrial
- DNA polymerase I A, chloroplastic/mitochondrial
- Protein PLASTID MOVEMENT IMPAIRED 2
- DNA-directed primase/polymerase protein
- LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.8
- Cellulose synthase-like protein E1
Sequence:
MRFLLRLPQIHFRKLSCSMSVLMGSKQFLEFCLLPSFASYPSSPSYSSSRQVSSVSRRFRPVLASRPVSKNSPYYQRTNGLSSYNSIPRVPTPVDTEVEADKRVVLSRLVTLRRKLAEQGVDAENCPPGQHSGLICPTCEGGNSGEKSLSLFIAPDGSSATWNCFRGKCGLKGGVRADGGLASADPIEKVERKITVEGIELEPLCDEIQDYFAARAISRKTLERNRVMQKRIGDEIVIAFTYWQRGELVSCKYRSLTKMFFQERKTRRILYGLDDIEKTSEVIIVEGEIDKLAMEEAGFLNCVSVPDGAPAKVSSKEIPSEDKDTKYKFLWNCNDYLKKASRIVIATDGDGPGQAMAEEIARRLGKERCWRVKWPKKSEDEHFKDANEVLMSKGPHLLKEAILDAEPYPILGLFSFKDFFDEIDAYYDRTHGHEYGVSTGWKNLDNLYSVVPGELTVVTGIPNSGKSEWIDAMLCNLNHSVGWKFALCSMENKVRDHARKLLEKHIKKPFFDADYGRSVQRMSVEEKDEGKKWLNDTFYPIRCEMDSLPSIDWVLERAKAAVLRYGIRGLVIDPYNELDHQRTPRQTETEYVSQMLTKIKRFSQHHSCHVWFVAHPKQLQHWDGGAPNLYDISGSAHFINKCDNGIIVHRNRDENAGPLDLVQIGVRKVRNKVAGQIGDAYLCYDRTTGSYSDSPVTPGMPERRSPKRY
Protein: 2-methyl-aconitate isomerase (EC 5.3.3.-) (Cis-trans isomerase) (Q937N7)
Organism: Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Function: Catalyzes the isomerization of 2-methyl-trans-aconitate to yield 2-methyl-cis-aconitate through a base-catalyzed proton abstraction coupled with a rotation about C2-C3 bond of 2-methyl-aconitate.
Interaction partners:
Sequence:
MTHVPQIKIPATYIRGGTSKGVFFRLQDLPETAQVPGPARDALLMRVIGSPDPYGKQIDGMGAATSSTSKTVILSKSTRPDHDVDYLFGQVSIDQPFVDWSGNCGNLSAAVGPFAISAGLVDASRIPHNGVAVVRIWQANIGKTIIGHVPVTNGEVQETGDFELDGVTFPAAEVQLEFMDPAAEEEGAGGAMFPTGNVVDDLEVPAVGTLKATMINAGIPTIFVNAESIGYTGTELQDAINSDTRALAMFEDHPCYGALRMGLIKNVDEAAKRQHTPKVAFVRQAGDYVASSGKKVAAADVDLLVRALSMGKLHHAMMGTAAVAIGTAAAIPGTLVNLAAGGGERNAVRFGHPSGTLRVGAEAQQVDGEWAVKKAIMSRSARVLMEGWVRVPGDAF
Protein: Oligophrenin-1 (P0CAX5)
Organism: Rattus norvegicus (Rat)
Function: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function, in hippocampal neurons. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at pre-synaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation.
Subcellular location: Postsynapse {ECO:0000269|PubMed:15034583, ECO:0000269|PubMed:19487570}. Presynapse {ECO:0000269|PubMed:15034583, ECO:0000305|PubMed:19481455}. Cell projection, axon {ECO:0000269|PubMed:15034583}. Cell projection, dendritic spine {ECO:0000269|PubMed:15034583}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99J31}. Cytoplasm {ECO:0000250|UniProtKB:Q99J31}.
Interaction partners:
- Cell division control protein 42 homolog
- FYVE, RhoGEF and PH domain-containing 1.
- Rho guanine nucleotide exchange factor 6
- Transforming protein RhoA
Sequence:
MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGSALISAMRSYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVQNASDLLIKPLETFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLLEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCRYEKETRTLTMTPTEQKPGAKQGPVDLTLKYCVRRKTESIDKRFCFDIEANERTGTITLQAPSEANRRLWMEAMDGKEPIYHSPITKQEEMELNEVGFKFVRKCINFIETKGIKTEGLYRTVGSNIQVQKLLNAFFDPKCPGDVDFYNSDWDIKTITSSLKFYLRNLSEPVMTYKLHKELVSAAKSDNLDYRLGAIHSLVYKLPEKNREMLELLIKHLVNVCEHSKENLMTPSNMGVIFGPTLMRAQEDTVAAMMNIKFQNIVVEILIEHFGKIYLGPPEDSQVPPVPPPRVTARRHKPITISKRLLREKAVFYTPSLDDVEDEIHHPTPNGTIASNLDPPKQLQHLKLPMQKSGEMDPGRKSPSRPVSDCQTEPCLEADMGKLVYRLQDGGTKAIPKASNGPVPGSGHTKTSSFHIKRPAPRPIVHHKEGDTDCFSKVRPPGEKQTIIRPPVRPPDPPCRSSTSQKPESKPETVSSNAEEIPSSVVASRTRFFETASRKTGSSQGKLPGDES
Protein: Centromere protein H C-terminal domain-containing protein (Q5B994)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTSSKGRSLPQLSSGEITLLDLAADDPRDTLSFSDKEALIIQLYHQTQELELEKALLEQELEVISTNNVEELAAAERELLDARATYTVRKKAVSTVLITDPILKAVHLKGTSPAERSLFRLVNRRDVLSLALENFTEAQASTLKKLSSLEVENLQLHRQNQELVRELLELTEDDESWREQLDDPELKQQLEQLEAEHKQSKAKWETMKSVASAIIVGSGVDWAEDEDLTALVLDDLND
Protein: Hepatocyte growth factor-regulated tyrosine kinase substrate (I3L1P5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004469}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004469}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004469}.
Interaction partners:
Sequence:
MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVNSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKDLLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVMTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLNRKAEGKATSTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERLRQKSTYTSYPKAEPMPSASSAPPASSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPAAQPGEGHAAPTNVVENPLPETDSQPIPPSGGPFSEPQFHNGESEESHEQFLKALQNAVTTFVNRMKSNHMRGRSITNDSAVLSLFQSINGMHPQLLELLNQLDERRRRCPRHGASAQGQPVYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQ
Protein: Pentatricopeptide repeat-containing protein OTP51, chloroplastic (Protein ORGANELLE TRANSCRIPT PROCESSING 51) (OsOTP51) (Q6ZHJ5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Promotes the splicing of group II introns in chloroplasts. Required for the splicing of intron 2 of plastid ycf3 transcripts, a factor required for the assembly of photosystem I (PSI). Involved in the splicing of atpF, ndhA, petB and rps16 chloroplastic transcripts. Required for the assembly of PSI.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MATTSPCAAPSPSLRCPLALSHPFASPPPPPALRLAGPKLLPGRLAVSPPPGIPAVASALESLILDLDDDEEDEDEETEFGLFQGEAWAAADEREAVRSPELVVPELEELPEQWRRSRIAWLCKELPAYKHSTFTRILNAQRKWITQDDATYVAVHCLRIRNNDAAFRVYSWMVRQHWFRFNFALATRVADCLGRDGKVEKCREVFEAMVKQGRVPAESTFHILIVAYLSVPKGRCLEEACTIYNQMIQMGGYKPRLSLHNSLFRALVSKTGGTAKYNLKQAEFVYHNVVTTNLDVHKDVYAGLIWLHSYQDVIDRERIIALRKEMKQAGFDEGIDVLVSVMRAFSKEGNVAETEATWHNILQSGSDLPVQAYVCRMEAYARTGEPMKSLDMFKEMKDKNIPPNVASYHKIIEIMTKALEVDIVEQLMNEFIESDMKHLMPAFLDLMYMYMDLDMHEKLELTFLKCIARCRPNRILYTIYLESLVKVGNIEKAEEVFGEMHNNGMIGTNTKSCNIMLRGYLSAEDYQKAEKVYDMMSKKKYDVQADSLEKLQSGLLLNKKVIKPKTVSMKLDQEQREILIGLLLGGTRMESYAQRGVHIVHFQFQEDSNAHSVLRVHIHERFFEWLSSASRSFDDGSKIPYQFSTIPHQHFSFFVDQFFLKGQPVLPKLIHRWLTPRVLAYWFMFGGSKLPSGDIVLKLSGGNSEGVERIVNSLHTQSLTSKVKRKGRFFWIGFQGSNAESFWRIIEPHVLNNFASLVTQEGSSIGSDGTQDTDTDSDDDMQMSDTERDE