wanglab/gogpt-training-data huggingface dataset:
Protein: Transactivator/viroplasmin protein (Tav) (Inclusion body matrix protein) (P03558)
Organism: Cauliflower mosaic virus (strain CM-1841) (CaMV)
Function: Enhances the ribosomal termination-reinitiation event leading to the translation of major open reading frames on the polycistronic viral RNAs.
Subcellular location: Host cytoplasm. Note=Found in cytoplasmic occlusion bodies.
Interaction partners:
Sequence:
MENIEKLLMQEKILMLELDLVRAKISLARANGSSQQGDLPLHRETPVKEEAVHSALATFTPTQVKAIPEQTAPGKESTNPLMASILPKDMNPVQTGIRLAVPGDFLRPHQGIPIPQKSELSSIVAPLRAESGIHHPHINYYVVYNGPHAGIYDDWGCTKAATNGVPGVAYKKFATITEARAAADAYTTSQQTDRLNFIPKGEAQLKPKSFAKALTSPPKQKAHWLTLGTKRPSSDPAPKEISFAPEITMDDFLYLYDLGRKFDGEGDDTMFTTDNEKISLFNFRKNADPQMVREAYAAGLIKTIYPSNNLQEIKYLPKKVKDAVKRFRTNCIKNTEKDIFLKIRSTIPVWTIQGLLHKPRQVIEIGVSKKVVPTESKAMESKIQIEDLTELAVKTGEQFIQSLLRLNDKKKIFVNMVEHDTLVYSKNIKDTVSEDQRAIETFQQRVISGNLLGFHCPAICHFIKRTVEKEGGTYKCHHCDKGKAIVQDASADSGPKDGPPPTRSIVEKEDVPTTSSKQVD
Protein: Uncharacterized protein YchH (P0AB49)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Cold shock-like protein CspD
- Surface composition regulator
Sequence:
MKRKNASLLGNVLMGLGLVVMVVGVGYSILNQLPQFNMPQYFAHGAVLSIFVGAILWLAGARVGGHEQVCDRYWWVRHYDKRCRRSDNRRHS
Protein: Small ribosomal subunit protein uS5 (40S ribosomal protein S2) (Protein strings of pearls) (P31009)
Organism: Drosophila melanogaster (Fruit fly)
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. Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity). Has a specific developmental role during oogenesis.
Interaction partners:
- Small ribosomal subunit protein uS11A
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL8
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS8A
Sequence:
MADEAPARSGFRGGFGSRGGRGGRGRGRGRWARGRGKEDSKEWVPVTKLGRLVREGKIKSLEEIYLYSLPIKEFEIIDFFLGSSLKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDNNGHIGLGVKCSKEVATAIRGAIILAKLSVVPVRRGYWGNKIGKPHTVPCKVTGKCGSVSVRLIPAPRGTGIVSAPVPKKLLTMAGIEDCYTSARGSTGTLGNFAKATYAAIAKTYAYLTPDLWKEMPLGSTPYQAYSDFLSKPTPRLHADA
Protein: Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Q8I5A0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit beta
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- dihydrolipoyllysine-residue succinyltransferase
- Pyruvate dehydrogenase E1 component subunit alpha
- 3-methyl-2-oxobutanoate dehydrogenase
- 2-oxoisovalerate dehydrogenase subunit alpha
- Aminomethyltransferase, mitochondrial, putative
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MNSVIFRAHCFFQPLRRCFSTKKDYDVIVIGGGPGGYVCSIRCAQNKLNVLNVNEDKKLGGTCLNRGCIPSKSLLHISHNYYEAKTRFKECGILVDNVKLDIETMHKHKNKCMGNLSDGINFLYKKNNVNHIIGHGSLVDEHTVLIKTEKEEKKVTAERIVIATGSKPIEIPLKKLNDNNFNDADNVNDILEYDHEIIQNSDDILNFKKVPHNISIIGGGVIGLEIGSVFSKLGSDVTVFEYNERLCGFLDADVSKVLQKTLEKIKMKFVFNTSVIGGNIENNQAALFAKNKKTNEIKKTTSEIVLICIGRKANFDNLNLHLLNIELNKNKKIPVDEYFNVIAQPTIKAIGDAIDGPMLAHKAEEEGYLLANILFDELKNNKKKKAHINYDLVPSVIYTHPEVATVGYNEAKCKELNMNFKSVSFPFAANSRSRTIDDYDGLIKLIVEKDTNRILGSQIIGNNASDLILPLSIYVANNGSSKSLSKIIYAHPTFSEVIKEVALQSFDKPIHM
Protein: Large ribosomal subunit protein uL5 (60S ribosomal protein L11) (CLL-associated antigen KW-12) (P62913)
Organism: Homo sapiens (Human)
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. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. Promotes nucleolar location of PML (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:27829214}. Cytoplasm {ECO:0000250|UniProtKB:Q9CXW4}.
Interaction partners:
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS2
Sequence:
MAQDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRRTGCIGAKHRISKEEAMRWFQQKYDGIILPGK
Protein: Meiotic spindle formation protein 2 (O44740)
Organism: Caenorhabditis elegans
Function: Forms a heterodimeric complex in conjunction with mei-1 which severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays. May act to target mei-1 within the cell. Required specifically for meiotic spindle formation in the female germline.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10809666}. Note=Localized to the spindle poles and condensed chromatin during female meiosis. Also localized to the polar body. Correct localization requires mei-1.
Interaction partners:
- Alpha/beta hydrolase fold-3 domain-containing protein
- Non-structural maintenance of chromosomes element 4
- Meiotic spindle formation protein mei-1
- PIP-1
- EGF-like domain-containing protein
- EF-hand domain-containing protein
- RNA-binding protein pos-1
- BTB domain-containing protein
- glucosamine-phosphate N-acetyltransferase
- Chondroitin proteoglycan 4 domain-containing protein
Sequence:
MSGLDDRKKLTHAKNRKPLNDIPKSAENRPNTRSTSSRRGAEKDVPITFIGSSRTVKADLPEFTNTRSRRPLHSESKKELSRNPVSRGEEHSSSLPKSSPESSVSVMSSNASLWSACTEEVNKIGVCAKRESRNLRVYKMKSFTSNMEQILSNDNQLAPTVIRILNSRNSWCLNSCHACLTFIMENITSDNYGKRSACLKALASITNSLLDTIIGFASTKTRRIGVDVVAEERAAKATECIHNFRKIVKNRDKIYKQIDQETIYKLDAILERLKKVSSHK
Protein: Katanin, putative (Q38E06)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Katanin p60 ATPase-containing subunit A-like 2
- Katanin p60 ATPase-containing subunit A1
- Katanin p60 ATPase-containing subunit A1
Sequence:
MPVIDSMTLQLPCQVYHSRFSPDSANRLVGLGCRDGGVHVYPFEDYSRTVLLSAGCSPSTSIAFDPQQRRLVGGTDEGSLHLWDMTTEGVVRTFGDGHKSTVTGVDFHPHTDVIATCSRDSVLRVWDTRKKSCVRSHMEAKAPLCATEFSPSGRWCVSGCADGVVRLYDLQSGKEMHEFRAHSGPVTSICFHPKRYYLAVGSSDGSVSFWELEGFTKIFQSKCLDTPVDAVYLSGKRMLVAASHILRVYDFDMMSDSFAPIIESQWNIIGDLNYSSNTDEALFVEFSGQTAVMGRVPLADGGLTIPPIEKTVKSQQRDPPSFNRGEENAKMSVPVLRAAHQRLHRSPSQVAAASHTGESGELQMDDLLTSSVTTVSVLRQRLTHLRVLRALWVQDNQQALVYLKELYTTNSDYGVTADFLGAMQHLRMKERITLSNLSDLLDVVMYALAGERENQLLAALKVLKSMSSKFRPKLDEARRQAPSFRNGEKNSTSLTMEQYYELSAKFDAVASVVQKLGKRKGPVGEEVREVLNEIPLSS
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC4 (RNA polymerases I, II, and III subunit ABC4) (ABC10-alpha) (P40422)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, the core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. Peroxisome {ECO:0000269|PubMed:35563734}. Note=Peroxisomal localization is dependent on PEX5. {ECO:0000269|PubMed:35563734}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerases I and III subunit RPAC1
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase I subunit RPA43
Sequence:
MSREGFQIPTNLDAAAAGTSQARTATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQFEAR
Protein: FAD-dependent oxidoreductase domain-containing protein 1 (EC 1.-.-.-) (Q96CU9)
Organism: Homo sapiens (Human)
Function: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Involved in mid-late stages of complex I assembly.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:20858599, ECO:0000305|PubMed:25678554}; Single-pass membrane protein {ECO:0000255}. Note=According to a report, it is associated with the matrix face of the mitochondrial inner membrane and does not contain any transmembrane region. However, one transmembrane domain is clearly predicted by different methods (Probable). {ECO:0000305|PubMed:25678554}.
Interaction partners:
- Complex I intermediate-associated protein 30, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
Sequence:
MIRRVLPHGMGRGLLTRRPGTRRGGFSLDWDGKVSEIKKKIKSILPGRSCDLLQDTSHLPPEHSDVVIVGGGVLGLSVAYWLKKLESRRGAIRVLVVERDHTYSQASTGLSVGGICQQFSLPENIQLSLFSASFLRNINEYLAVVDAPPLDLRFNPSGYLLLASEKDAAAMESNVKVQRQEGAKVSLMSPDQLRNKFPWINTEGVALASYGMEDEGWFDPWCLLQGLRRKVQSLGVLFCQGEVTRFVSSSQRMLTTDDKAVVLKRIHEVHVKMDRSLEYQPVECAIVINAAGAWSAQIAALAGVGEGPPGTLQGTKLPVEPRKRYVYVWHCPQGPGLETPLVADTSGAYFRREGLGSNYLGGRSPTEQEEPDPANLEVDHDFFQDKVWPHLALRVPAFETLKVQSAWAGYYDYNTFDQNGVVGPHPLVVNMYFATGFSGHGLQQAPGIGRAVAEMVLKGRFQTIDLSPFLFTRFYLGEKIQENNII
Protein: Poly(U)-binding-splicing factor PUF60 (60 kDa poly(U)-binding-splicing factor) (FUSE-binding protein-interacting repressor) (FBP-interacting repressor) (Ro-binding protein 1) (RoBP1) (Siah-binding protein 1) (Siah-BP1) (Q9UHX1)
Organism: Homo sapiens (Human)
Function: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with RO60. Binds to poly(U) RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10606266, ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:17579712}. Note=Colocalizes partially with RO60. {ECO:0000269|PubMed:10668799}.
Interaction partners:
- Far upstream element-binding protein 1
- Heterogeneous nuclear ribonucleoprotein K
- Splicing factor 3B subunit 3
- Splicing factor 3B subunit 1
- RNA-binding protein FXR2
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Splicing factor 3A subunit 2
- Splicing factor 1
- RNA-binding protein FXR1
- U2 small nuclear ribonucleoprotein A'
Sequence:
MATATIALQVNGQQGGGSEPAAAAAVVAAGDKWKPPQGTDSIKMENGQSTAAKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATPGGLPPAAAVAAAAATAKITAQEAVAGAAVLGTLGTPGLVSPALTLAQPLGTLPQAVMAAQAPGVITGVTPARPPIPVTIPSVGVVNPILASPPTLGLLEPKKEKEEEELFPESERPEMLSEQEHMSISGSSARHMVMQKLLRKQESTVMVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDAEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYDQERFDNSDLSA
Protein: MIP07328p (Semaphorin 1b, isoform A) (Semaphorin 1b, isoform B) (Semaphorin 1b, isoform C) (Semaphorin-like) (Q7KK54)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Plexin A, isoform A
- Plexin-B
Sequence:
MSSKSRPSSAAMLVNAIPMILLITLSGLTIVAGWMPDVKPDLQTKQDKVLAHFIGNSTDYFKILDHNDEFVLVGAKDVIYNVSLNGLKEIARLEWHSTDADRELCALKGKHEWDCHNYLRVYALRPNGEVLLCGTNSYKPRCRHYTPVEVSSEEAGSAGHAHAMRYEVSRDVEAQGLCPYSPAHNSTYAFADGHLYSATVADFSGGDPLIYRENLRTEQYDLKQLNQPDFVGAIERNGYVLFFFRELSMEVMNFGKAVYSRVARVCKNDRGGPYSHGKSWTSFLKARLNCSVPGEFPFYFDEIQAISPIVESGSKSLIYAVFTTSVNAIPGSAVCAFNVDDILAAFDGEFKSQKDSQSHWLPVEREQVPKPRPGQCVEDSRTLTSIAVNFIKNHPLMEEAVPAVHGRPLLTKVNLHHRLTAIAVHPQVKSLSGAYYDVIYSGTDDGKVTKFINILSTHPNSTVDRLKTVVISEMQVLPLGTPIRELVISTSKNSLVVVSDGSLVSVPLHHCSHIVDCLGCLSLQDPICAWDLQTHECKNLATSQHKFGTKTYLQSLNSTKKAAALLCPHIPRDAPGAETVSFVTMAPPPTEEQKLLYSNVGSSQGNQPSLEQQPTGGDDFGLNKITLTSMDPDDIMPNLNDPQKSTASVDEIKYASTPSFMLLTTIVFFTFLVGGIAGICCVKAKSRLMEAQMDESHRNHFGKPMQFKHQNTGKDINLLMGSNAYTTTQKTPNLDLEKDRSHECKNSTEHLEKELPCKTSTLTKVKRTYI
Protein: Thymidine kinase 2 (D3ZGQ2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Thymidine kinase, cytosolic
- Thymidylate synthase
- Thymidine phosphorylase
- dTMP kinase
- Deoxycytidylate deaminase
- 5',3'-nucleotidase, mitochondrial
- Cytidine deaminase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Uridine phosphorylase
- UMP-CMP kinase
Sequence:
MLLRSLRSWAARSLRSMGPGSSGSPGSLDSGAGPLWAPRRACPPDKDREKDKEKKAVVCIEGNIASGKTTCLEFFSNTTDVEVLMEPVLKWRNVHGHNPLSLMYHNASRWGLTLQTYVQLTMLDQHTRPQMSPVRLMERSIYSARYIFVENLYRSGKMPEVDYAILSEWFDWIIKNIDVSVDLIVYLRTTPEICYQRLKMRCREEEKVIPVEYLSAIHHLYEEWLVTGSLFPAAAPVLVIEADHNLEKMLELFEQNRARILTPENWKHGP
Protein: Plasma membrane calcium-transporting ATPase 3 (PMCA3) (EC 7.2.2.10) (Plasma membrane calcium ATPase isoform 3) (Plasma membrane calcium pump isoform 3) (Q64568)
Organism: Rattus norvegicus (Rat)
Function: ATP-driven Ca(2+) ion pump involved in the maintenance of basal intracellular Ca(2+) levels at the presynaptic terminals. Uses ATP as an energy source to transport cytosolic Ca(2+) ions across the plasma membrane to the extracellular compartment. May counter-transport protons, but the mechanism and the stoichiometry of this Ca(2+)/H(+) exchange remains to be established.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27035656}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000269|PubMed:17183553}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at parallel fiber terminals. {ECO:0000269|PubMed:17183553}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Plasma membrane calcium-transporting ATPase 4
- Plasma membrane calcium-transporting ATPase 1
- cGMP-dependent protein kinase 2
- G protein-activated inward rectifier potassium channel 4
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
Sequence:
MGDMANSSIEFHPKPQQQREVPHVGGFGCTLAELRSLMELRGAEALQKIQEAYGDVSGLCRRLKTSPTEGLADNTNDLEKRRQIYGQNFIPPKQPKTFLQLVWEALQDVTLIILEVAAIVSLGLSFYAPPGEESEACGNVSGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRNGQLLQVPVAALVVGDIAQVKYGDLLPADGVLIQGNDLKIDESSLTGESDHVRKSADKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDKKGKQQDGAMESSQTKAKKQDGAVAMEMQPLKSAEGGEMEEREKKKANVPKKEKSVLQGKLTKLAVQIGKAGLVMSAITVIILVLYFVIETFVVDGRVWLAECTPVYVQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQSYLGDTHYKEIPAPSALTPKILDLLVHAISINSAYTTKILPPEKEGALPRQVGNKTECALLGFILDLKRDFQPVREQIPEDQLYKVYTFNSVRKSMSTVIRMPDGGFRLFSKGASEILLKKCTNILNSNGELRGFRPRDRDDMVKKIIEPMACDGLRTICIAYRDFSAIQEPDWDNENEVVGDLTCIAVVGIEDPVRPEVPEAIRKCQRAGITVRMVTGDNINTARAIAAKCGIIQPGEDFLCLEGKEFNRRIRNEKGEIEQERLDKVWPKLRVLARSSPTDKHTLVKGIIDSTTGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTESLLLRKPYGRDKPLISRTMMKNILGHAVYQLTIIFTLLFVGELFFDIDSGRNAPLHSPPSEHYTIIFNTFVMMQLFNEINARKIHGERNVFDGIFSNPIFCTIVLGTFGIQIVIVQFGGKPFSCSPLSTEQWLWCLFVGVGELVWGQVIATIPTSQLKCLKEAGHGPGKDEMTDEELAEGEEEIDHAERELRRGQILWFRGLNRIQTQMEVVSTFKRSGSFQGAVRRRSSVLSQLHDVTNLSTPTHIRVVKAFRSSLYEGLEKPESKSCIHNFMATPEFLINDYTHNIPLIDDTDVDENEERLRAPPPPPPNQNNNAIDSGIYLTTHATKSATSSAFSSRPGSPLHSMETSL
Protein: Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein) (W5ULY8)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Lysophosphatidic acid receptor 1
- Dopamine receptor D2a
- D
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Beta-2 adrenergic receptor
- Endothelin receptor type B isoform X2
- Endothelin receptor type B
- Phosphoinositide 3-kinase regulatory subunit 5
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Sequence:
MGCTLSTEDKAAVERSRRIDRNLRDDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDTARADDARQLFVLAGSAEEGFMTAELAGVIKRLWKDGGVQACFSRSREYQLNDSAAYYLNDLDRISQATYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Protein: Transcription factor Ovo-like 2 (mOvo2) (Zinc finger OVO2) (Zinc finger protein 339) (Zinc finger protein mOVO) (Q8CIV7)
Organism: Mus musculus (Mouse)
Function: Zinc-finger transcription repressor factor. Plays a critical role in maintaining the identity of epithelial lineages by suppressing epithelial-to mesenchymal transition (EMT) mainly through the repression of ZEB1, an EMT inducer. Positively regulates neuronal differentiation. Suppresses cell cycling and terminal differentiation of keratinocytes by directly repressing MYC and NOTCH1 (By similarity). Important for the correct development of primordial germ cells in embryos. Plays dual functions in thermogenesis and adipogenesis to maintain energy balance. Essential for brown/beige adipose tissue-mediated thermogenesis, is necessary for the development of brown adipocytes. In white adipose tissues, limits adipogenesis by blocking CEBPA binding to its transcriptional targets and inhibiting its transcription factor activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:36228616, ECO:0000269|PubMed:9468311}.
Interaction partners:
- Grainyhead-like protein 2 homolog
Sequence:
MPKVFLVKRRSPGVSVRSWDELPDDKRADTYIPVSLGCLLRDPPEDCRSDGGSSSGCSSSAGEPGGAESSSSPRAPEPETPELHDAQGTDGHLAAMQRPVARSKIKFTTGTCDNSVIHNCDLCGKSFRLQRMLNRHLKCHNQVKRHLCTFCGKGFNDTFDLKRHVRTHTGIRPYKCEVCNKAFTQRCSLESHLKKIHGVQQQYAYKQRRDKLYVCEDCGYTGPTQEDLYLHVNSDHPGSTFLKKTSKKLAALMQNKLTSPLQENSTLSEEEEKK
Protein: Myotrophin (Protein V-1) (P58546)
Organism: Homo sapiens (Human)
Function: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
Interaction partners:
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit beta
- Leucine zipper protein 6
- F-actin-capping protein subunit alpha-2
- Alpha-adducin
- Macrophage-capping protein
- F-actin-capping protein subunit alpha-3
- Beta-adducin
- Tropomodulin-4
Sequence:
MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ