wanglab/gogpt-training-data huggingface dataset:
Protein: Ataxin-2 homolog (G5ED29)
Organism: Caenorhabditis elegans
Function: Probable RNA-binding protein that negatively regulates the translation of targets. Functions with RNA-binding protein szy-20 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation. Required for gonad development, germ cell proliferation and for the production of oocytes. Regulates whole body growth and fat accumulation in response to food availability, and this may be through the mTOR pathway, upstream of daf-15 and rheb-1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15342467, ECO:0000269|PubMed:27457958, ECO:0000269|PubMed:27689799}. Nucleus {ECO:0000269|PubMed:27457958}. Note=Co-localizes with szy-20 and pab-1 in the cytoplasm. {ECO:0000269|PubMed:27689799}.
Interaction partners:
- AD domain-containing protein
- ATP-dependent RNA helicase cgh-1
- Polyadenylate-binding protein
- Probable small nuclear ribonucleoprotein-associated protein B
- Polyadenylate-binding protein
- RRM domain-containing protein
- Sm domain-containing protein
- Nucleolin homolog 1
- Ras GTPase-activating protein-binding protein gtbp-1
- Protein IMPACT homolog
Sequence:
MSTPTGLPALNGDVLSAINDMIGRVIIINTTDKKRYSGVLGAVSQDFDFGMQCVVEITKENENNLLRTESECRDKMVFHYSDIVDFAYVTQEIKKQHAVSKFVTDRQYHGDTPIEGEELQEWNGGEEDGLGGSIEDDVVVAGGQTAARRSNNHNNGTGWSVNDMFAANEKMNVVSTFKEDLTQYTTVEVVGTDEDRARAERLAREIESNSSSKFMANLENDDDERDLDKITRQEDFENGNGRKRNNNSFNQQQQQRRNPNIAPNGQPVNRRAEGLRGDRRNSGSSSANNSRYGAPAAAQQNYSQNQQQQQGQKGYRRQNEENDWQMAKGKGQNQGHDHSFRQQQKQMLDPRPNNNVKPADDKAQSATTATAAAGGSRVTDLKNWGNEFSIATAPKDQAPAVPAGNSGSAWNRGPPSSLVAKGSSNESTPPPTTNGEEAETKKEEAPSTSVDVAAAPVQNVQNDAEKHQEDDNVSVTSENDSVITSKSSSFKFNINAPEFKPRVAPATPTATTPVQNEYHPQQQPHPAMMAPQQGPPAPGMGMVPPHMGGPQNQGQPPMMMWQQTGQQQQGGGGYPQNHQFPIQHVPMQGVPGQMYGPGAATPVTVAQQPNQQHQVPTSAAGGQNHQLRDGEYREKQPLYMPYGPPQMVPVTSQQFYHSQYQGQMQQAAPYQMKMMPQQAPQGAYQQRYQQPQVYMMPPQGQQQQPRYQGPPPPQQQQQQQPQQQQFSGEQSRPQSHPNSQPTTPGPRGELPKMSGAPQNGNMQAESSSNASHSGSTSSQSGQRSGSPPGAVPPPPPPQQQHQQQQHPPHHAPPHVGAPPPQMMQQQQQHIQQYMVMQGPHQMHPQIPNYYQQPQQVFYPMIMPQQMPMQQNQHPQQSLMGERSDQGFPTSGYFDYRTMPNYQQQQQQQQQQMHRQNSLPQQFQGNQGVNPSGQQSGPPPPPPPSQQGTPRDQQHSQSPP
Protein: Elongator complex protein 6 (AtELP6) (Elongator component 6) (UPF0405 protein ELP6) (Q8L9Y2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Promotes organ development by modulating cell division rate. Involved in oxidative stress signaling. Prevents anthocyanins accumulation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Elongator complex protein 4
- Elongator complex protein 3
- Elongator complex protein 5
- Elongator complex protein 1
- Elongator complex protein 2
- Protein KTI12 homolog
- tRNA ligase 1
Sequence:
MDRSLNLLDLALGFDEQLAIPSPLNGKVILIEDCVETSGSFVLHQLMKRVLSSNSSDALIFLAFARPFSHYDRILRKLGCNLATHKSNNRLVFFDMLMVKCSDGDQMEDNVSAVAKLFREIQETVRKLQSVTSGNITVMVDDMSLLEIATTGSNSDHVLDFLHYCHTLSSESNCSLVILNHEDIYASMERPAFLLQMVCLADVVIKAEPLASGLANDVHGQLTVLNKGISNSGRGSSRNKLQNFQFRIKENGIDYFYPGCRS
Protein: N-chimaerin (A-chimaerin) (Alpha-chimerin) (N-chimerin) (NC) (Rho GTPase-activating protein 2) (Q91V57)
Organism: Mus musculus (Mouse)
Function: GTPase-activating protein for p21-rac and a phorbol ester receptor. May play an important role in neuronal signal-transduction mechanisms (By similarity). Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.
Interaction partners:
- Cell division control protein 42 homolog
- Ubiquitin conjugation factor E4 B
- Ephrin type-A receptor 4
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRVTCTCEVENRPKYYGREYHGMISREETDQLLSVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHIGYTTLNREPAYKQHMAVLKETHDEKEATGQDGVSEKRLTSLVRRATLKENEQIPKYEKVHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLKHVKKVYSCDLTTLVKAHITKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDPMAALNDIRYQRLVVELLIKNEDILF
Protein: Negative elongation factor B (Q9Y113)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II.
Subcellular location: Nucleus {ECO:0000269|PubMed:15741180}. Chromosome {ECO:0000269|PubMed:15741180}. Note=Associates with polytene chromosomes. Associates with the hsp70 promoter when it is inactive, but not when it is activated.
Interaction partners:
- Negative elongation factor D
- Negative elongation factor E
- Transcription elongation factor SPT5
- Negative elongation factor A
- Transcription elongation factor SPT4
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB9
- Cyclin-dependent kinase 9
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MIMSTPAKNNNGTGLEDVNIPGQAYLREALTSCTDPLKAIESFQLENGVLLPSLRPMLPLLDLHGVRRLDFHTSLMEELRDKLIAHINEMGQKEPRERDKKLKELLVKSFPVVRVKSLRPVVMAILRNTQHIDDKYLKILVRDRELYADTDTEVKRQIWRDNQSLFGDEVSPLLSQYIREKEHILFDHTNLNNLFFHPTPKVRRQGEVVQKLANMIGTSVKLYDMVLQFLRTLFLRTRNVHYCTLRAELLMALHDLEVQEIISIDPCHKFTWCLDACIREKNVDIKRSRELQGFLDNIKRGQEQVLGDLSMTLCDPYAINFLATSAIKILHHLINNEGMPRDNQILILLLRMLALGLSAWVMIDSQDFKEPKLDCQVVTKFLPALMSLMVDDQCRSLHAKLPPDERESALTTIEHSGPAPDAVEAYIQESSVASILAMYYTLHTARLKDRVGVLRVLAILSACKDDRAYEDPFLHSLIALLIPMSEEFATEDFCTTLFDEFIFAGLTRENVTSRHMLKLLWYVHNKLPAGRLATLMKAMQPTTAHNEHIHKLYEILQERIGTGAAETPVIEAPPMEFDSPLKSVPTPGPHYNVQ
Protein: Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller) (Q14004)
Organism: Homo sapiens (Human)
Function: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:16721827}.
Interaction partners:
- Cyclin-K
- Cyclin-T1
- Cyclin-T2
- Cyclin-dependent kinase 12
- Matrix metalloproteinase-23
- Transcription elongation factor SPT5
- Cyclin-H
- DNA-directed RNA polymerase II subunit RPB1
- Cyclin-dependent kinase 9
- Matrix metalloproteinase-21
Sequence:
MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKERHREHRRRDGQRGGSEASKSRSRHSHSGEERAEVAKSGSSSSSGGRRKSASATSSSSSSRKDRDSKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRRSLSPLGGRDDSPVSHRASQSLRSRKSPSPAGGGSSPYSRRLPRSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVLRRSGKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEATKAAEAAAKAAKASNTSTPTKGNTETSASASQTNHVKDVKKIKIEHAPSPSSGGTLKNDKAKTKPPLQVTKVENNLIVDKATKKAVIVGKESKSAATKEESVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKEADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHSKRRPKICGPRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPVKTGPGQHLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDDLIQHQDMRILELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKREGGIDYQAGDTYVSTSDYKDNFGSSSFSSAPYVSNDGLGSSSAPPLERRSFIGNSDIQSLDNYSTASSHSGGPPQPSAFSESFPSSVAGYGDIYLNAGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGNLQENPSGPSLMHGQTWTSPAQGPGYSQGYRGHISTSTGRGRGRGLPY
Protein: Putative box C/D snoRNA protein SPCC613.07 (O74906)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P38772}.
Interaction partners:
- Meiotically up-regulated gene 183 protein
- Uncharacterized zinc-finger protein C4F10.19c
- Nucleolar protein 58
Sequence:
MSENRLGICSTCQKNASKYRCPRCDSRFCCLECNLEHKRLTKCSGERDPATFVPKSKLVNHLNSDFNFLSGVERLINRKENGSHQVSNRAERNRLQLKRSLERAGINIKFAPPSNKKRRLNRTHYDKKSHLIKWSIEWCLHESSTSKDLTDEASENTIITHSHPESEPLEKIFRKLVEENSEMNSQVSKANIHAPDDMQFMIKSRKSRSKGFIYKKIEPSNSLSSCLRNSFVFEVPTIHVFTSTTQVHTESSYETSSSEQSDDSSSSSSCISDSEESSSDDELNELSNEKKANSPTQNVDTSSKLSSVKFQNEDDEDRRKNSDGSEASYSLPPLFGSYFQKQGQY
Protein: Large ribosomal subunit protein uL24A (60S ribosomal protein L26-A) (L33) (YL33) (P05743)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL19A
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL29A
Sequence:
MAKQSLDVSSDRRKARKAYFTAPSSQRRVLLSAPLSKELRAQYGIKALPIRRDDEVLVVRGSKKGQEGKISSVYRLKFAVQVDKVTKEKVNGASVPINLHPSKLVITKLHLDKDRKALIQRKGGKLE
Protein: RalB-binding protein (Q9DDA3)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
TKFPGLYRTGEPSPPHDILHEPPDIVSEDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKIKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEDKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPTPEPESLPVDIPRLRPVFGIPLVEAAEHTMMYDGIRLPAVFRECIDYIEQHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEDYEPYTVASLLKQYLRELPENVLTKDLMPRFEEACGKSTEGERLQECQRLLKELPECNFCLTSWLIVHMDHVIEKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGGVQIKRVIKPLRWSNMATMPALPETQETIKEEIRRQEFLLNCLHRELQAGIKDLSKEERLWEVQRILTALKRKLREAKRQDCETKIAQEIASLSKEDVSKEEMTENEEEVLNILLAQENEILTEQEELVAMEQYLRRQIGTEKEEIERLRAEISEIQSRQQHGRSETEEYSSESESESEDEDELQYILEDLQRQNEELEIKNTHLNQAIHEEREAIIELRVQLRLLQMQRVKSEQLPEEEELVRSQLSRDNLPETKAPKDQPKALKEQMRPSPIKDWKETLI
Protein: Heat shock-related 70 kDa protein 2 (Heat shock protein 70.2) (Testis-specific heat shock protein-related) (HST) (P14659)
Organism: Rattus norvegicus (Rat)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P17156}. Note=Colocalizes with SHCBP1L at spindle during the meiosis process. {ECO:0000250|UniProtKB:P17156}.
Interaction partners:
- Mitogen-activated protein kinase 10
- Toll-like receptor 2
- DnaJ heat shock protein family
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- DnaJ
- DnaJ homolog subfamily A member 2
- DnaJ homolog subfamily A member 1
- Stress-induced-phosphoprotein 1
- Heat shock protein 105 kDa
Sequence:
MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGGKVQSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNAVESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQGGPGGGGSSGGPTIEEVD
Protein: Dual specificity testis-specific protein kinase 2 (EC 2.7.12.1) (Testicular protein kinase 2) (Q96S53)
Organism: Homo sapiens (Human)
Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11418599}.
Interaction partners:
Sequence:
MDRSKRNSIAGFPPRVERLEEFEGGGGGEGNVSQVGRVWPSSYRALISAFSRLTRLDDFTCEKIGSGFFSEVFKVRHRASGQVMALKMNTLSSNRANMLKEVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINSGNLEQLLDSNLHLPWTVRVKLAYDIAVGLSYLHFKGIFHRDLTSKNCLIKRDENGYSAVVADFGLAEKIPDVSMGSEKLAVVGSPFWMAPEVLRDEPYNEKADVFSYGIILCEIIARIQADPDYLPRTENFGLDYDAFQHMVGDCPPDFLQLTFNCCNMDPKLRPSFVEIGKTLEEILSRLQEEEQERDRKLQPTARGLLEKAPGVKRLSSLDDKIPHKSPCPRRTIWLSRSQSDIFSRKPPRTVSVLDPYYRPRDGAARTPKVNPFSARQDLMGGKIKFFDLPSKSVISLVFDLDAPGPGTMPLADWQEPLAPPIRRWRSLPGSPEFLHQEACPFVGREESLSDGPPPRLSSLKYRVKEIPPFRASALPAAQAHEAMDCSILQEENGFGSRPQGTSPCPAGASEEMEVEERPAGSTPATFSTSGIGLQTQGKQDG
Protein: Amelotin (Q9D3J8)
Organism: Mus musculus (Mouse)
Function: Is a promoter of calcium phosphate mineralization, playing a critical role in the formation of the compact, mineralized, aprismatic enamel surface layer during the maturation stage of amelogenesis.
Subcellular location: Secreted {ECO:0000269|PubMed:16304441}.
Interaction partners:
- Enamelin
- Odontogenic ameloblast-associated protein
- Ameloblastin
- Amelogenin, X isoform
- Secretory calcium-binding phosphoprotein proline-glutamine-rich 1
- Kallikrein-4
- Matrix metalloproteinase-20
- Pseudokinase FAM20A
- Kallikrein 1-related peptidase-like b4
- Dentin matrix acidic phosphoprotein 1
Sequence:
MKTMILLLCLLGSAQSLPKQLNPASGVPATKPTPGQVTPLPQQQPNQVFPSISLIPLTQLLTLGSDLPLFNPAAGPHGAHTLPFTLGPLNGQQQLQPQMLPIIVAQLGAQGALLSSEELPLASQIFTGLLIHPLFPGAIPPSGQAGTKPDVQNGVLPTRQAGAKAVNQGTTPGHVTTPGVTDDDDYEMSTPAGLRRATHTTEGTTIDPPNRTQ
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) (Q95U38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase
- Cullin 3, isoform F
- 2-oxoglutarate dehydrogenase, mitochondrial
- AT18465p
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- RH44771p
- Isocitrate dehydrogenase
Sequence:
MASFLARTGGPLIETVRPAAIKKILGLAPIAVQQLRNLNVQEHVSYSLLNEAKIPTPRFAVAKNGKEANDIATKLKTDNLVLKAQVLAGGRGKGTFKNGLKGGVRVVYDPQTAEELSSKMIDQLLVTKQTGAAGRICKKVMVAERKFPRREFYFAVMMERAFNGPVLIASKEGGVDIEEVAASSPDAILYEPIDIGTGLTSEQAEKIVKKVGLGGDGEDTHVQMLLNLYDLFVKKDALLVEINPYAEDAMSGCFFALDAKLRFDDNAEFRQKELFALRDWTQEDPKEVEAAKYNLNYIALDGTIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAEAVKAAFKIITSDPKVLCILVNIFGGIMRCDVIAEGIISATKDLNLNMPVVVRLQGTKVKEARELIRTSGLKILARDDLDKAADLAVHLAQIVKLAREMKMDVNFEIPDAQKGKGDCKKDQKQPDSKGGKKSEKKDDKKSDCTKKEEKKKEEKKDICEKKGKK
Protein: GMP phosphodiesterase delta subunit domain-containing protein (Q586Q9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ADP-ribosylation factor-like protein 2
- ADP-ribosylation factor, putative
- ADP-ribosylation factor-like protein 3
- ADP-ribosylation factor 3, putative
Sequence:
MAATTEVTPEHVLQLTAPSTGFLCPITANTYNIEFYSFVVRDADTKQVMFEVERDASTYPSVASLAQLPEEQQQAARTIFYRFPPSMLRKQRVSATLLFGVNGDKPVPDLRMIERHYFRNTLVKTFDFKFGFCIPHSRNTWEAVYDVPQFNAEWLEAIEKGTNEMTSDSFYFADGRLIMHNRAFYDYSAPEEEFTK
Protein: F-box/WD repeat-containing protein 11 (F-box and WD repeats protein beta-TrCP2) (F-box/WD repeat-containing protein 1B) (Homologous to Slimb protein) (HOS) (Q5SRY7)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling regulation. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. SCF(FBXW11) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (By similarity). Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2. SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18782782}. Nucleus {ECO:0000269|PubMed:18782782}.
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- Catenin beta-1
- F-box/WD repeat-containing protein 1A
- S-phase kinase-associated protein 2
- Zinc finger protein GLI1
- F-box only protein 5
- WW domain-containing transcription regulator protein 1
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MEPDSVIEDKTIELMCSVPRSLWLGCANLVESMCALSCLQSMPSVRCLQISNGTSSVIVSRKRPSEGNYQKEKDLCIKYFDQWSESDQVEFVEHLISRMCHYQHGHINSYLKPMLQRDFITALPEQGLDHIAENILSYLDARSLCAAELVCKEWQRVISEGMLWKKLIERMVRTDPLWKGLSERRGWDQYLFKNRPTDGPPNSFYRSLYPKIIQDIETIESNWRCGRHNLQRIQCRSENSKGVYCLQYDDDKIISGLRDNSIKIWDKSSLECLKVLTGHTGSVLCLQYDERVIVTGSSDSTVRVWDVNTGEVLNTLIHHNEAVLHLRFSNGLMVTCSKDRSIAVWDMASATDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWSTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLQAALDPRAPASTLCLRTLVEHSGRVFRLQFDEFQIISSSHDDTILIWDFLNVPPSAQNETRSPSRTYTYISR
Protein: E2F transcription factor-like E2FD (DP-E2F-like protein 2) (E2F-like repressor E2L1) (Q9LFQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibitor of E2F-dependent regulation of gene expression. Binds specifically the E2 recognition site as a monomer without interacting with DP proteins. May be up-regulating E2FA and down-regulating repressors of cell cycle progression. Promotes cell proliferation and represses cell elongation. Regulated by proteolysis via a ubiquitin-proteasome pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:11867638}.
Interaction partners:
- Retinoblastoma-related protein 1
- Transcription factor-like protein DPA
- Transcription factor-like protein DPB
- Cyclin-dependent kinase B1-1
- Protein FIZZY-RELATED 1
- ARM repeat superfamily protein
- DNA-binding protein S1FA1
- GATA transcription factor 27
- Tubulin-tyrosine ligase
Sequence:
MDSLALAPQVYSRKDKSLGVLVANFLTLYNRPDVDLFGLDDAAAKLGVERRRIYDVVNILESIGLVARSGKNQYSWKGFGAVPRALSELKEEGMKEKFAIVPFVAKSEMVVYEKEGEESFMLSPDDQEFSPSPRPDNRKERTLWLLAQNFVKLFLCSDDDLVTFDSATKALLNESQDMNMRKKVRRLYDIANVFSSMKLIEKTHVPETKKPAYRWLGSKTIFENRFIDGSASLCDRNVPKKRAFGTELTNVNAKRNKSGCSKEDSKRNGNQNTSIVIKQEQCDDVKPDVKNFASGSSTPAGTSESNDMGNNIRPRGRLGVIEALSTLYQPSYCNPELLGLFAHYNETFRSYQEEFGREK
Protein: Beta-actin (Q8SPK6)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
TPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANT
Protein: A-kinase anchor protein 10, mitochondrial (AKAP-10) (Dual specificity A kinase-anchoring protein 2) (D-AKAP-2) (Protein kinase A-anchoring protein 10) (PRKA10) (O88845)
Organism: Mus musculus (Mouse)
Function: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic.
Interaction partners:
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- Na
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase type I-beta regulatory subunit
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Ras-related protein Rab-4B
- Ras-related protein Rab-4A
- A-kinase anchor protein 1, mitochondrial
Sequence:
MRGAGPSPRHSPRALRPDPGPAMSFFRRKVKGKEQEKTLDVKSTKASVAVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLRDTVVLPYFLQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKRHETPASSVTEALDRRLGDSSSAPLLVTQSEGTDLSSRTQNPQNHLLLSQEGHSARSLHREVARTGSHQIPTDSQDSSSRLAVGSRNSCSSPLRELSEKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIAKICGEDGQVDPNCFVLAQAVVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLAAHGSVCLPEESHSGGSDGSTAQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMSFGRVSDLGQFIRESEPEPDVKKSKGFMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDVMQQAHHDQPLEKSTKL