wanglab/gogpt-training-data huggingface dataset:
Protein: Elongation factor G, mitochondrial (EF-Gmt) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) (P25039)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS5m
- Ribosome-recycling factor, mitochondrial
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein bS16m
Sequence:
MSVQKMMWVPRKMVGGRIPFFTCSKVFSGFSRRSFHESPLARSTYEEEKVLVDEIKQKLTPDDIGRCNKLRNIGISAHIDSGKTTFTERVLYYTKRIKAIHEVRGRDNVGAKMDSMDLEREKGITIQSAATYCSWDKEGKNYHFNLIDTPGHIDFTIEVERALRVLDGAVLVVCAVSGVQSQTVTVDRQMRRYNVPRVTFINKMDRMGSDPFRAIEQLNSKLKIPAAAVQIPIGSESSLSGVVDLINRVAIYNKGDNGEIIEKGPVPENLKPLMEEKRQLLIETLADVDDEMAEMFLEEKEPTTQQIKDAIRRSTIARSFTPVLMGSALANTGIQPVLDAIVDYLPNPSEVLNTALDVSNNEAKVNLVPAVQQPFVGLAFKLEEGKYGQLTYVRVYQGRLRKGNYITNVKTGKKVKVARLVRMHSSEMEDVDEVGSGEICATFGIDCASGDTFTDGSVQYSMSSMYVPDAVVSLSITPNSKDASNFSKALNRFQKEDPTFRVKFDPESKETIISGMGELHLEIYVERMRREYNVDCVTGKPQVSYRESITIPADFDYTHKKQSGGAGQYGRVIGTLSPVDDITKGNIFETAIVGGRIPDKYLAACGKGFEEVCEKGPLIGHRVLDVKMLINDGAIHAVDSNELSFKTATMSAFRDAFLRAQPVIMEPIMNVSVTSPNEFQGNVIGLLNKLQAVIQDTENGHDEFTLKAECALSTMFGFATSLRASTQGKGEFSLEFSHYAPTAPHVQKELISEFQKKQAKK
Protein: Neutral ceramidase (N-CDase) (NCDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylsphingosine amidohydrolase) (Q9I596)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid at an optimal pH of 8-9. Also catalyzes the synthesis of Cers from Sph and fatty acid.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Alanine racemase N-terminal domain-containing protein
- Probable transcriptional regulator
- Lipoprotein
- Probable cytochrome c
- Probable N-acetylglucosamine-6-phosphate deacetylase
- Probable acyl-CoA dehydrogenase
- Hemolytic phospholipase C
- DUF934 domain-containing protein
Sequence:
MSRSAFTALLLSCVLLALSMPARADDLPYRFGLGKADITGEAAEVGMMGYSSLEQKTAGIHMRQWARAFVIEEAASGRRLVYVNTDLGMIFQAVHLKVLARLKAKYPGVYDENNVMLAATHTHSGPGGFSHYAMYNLSVLGFQEKTFNAIVDGIVRSIERAQARLQPGRLFYGSGELRNANRNRSLLSHLKNPDIVGYEDGIDPQMSVLSFVDANGELAGAISWFPVHSTSMTNANHLISPDNKGYASYHWEHDVSRKSGFVAAFAQTNAGNLSPNLNLKPGSGPFDNEFDNTREIGLRQFAKAYEIAGQAQEEVLGELDSRFRFVDFTRLPIRPEFTDGQPRQLCTAAIGTSLAAGSTEDGPGPLGLEEGNNPFLSALGGLLTGVPPQELVQCQAEKTILADTGNKKPYPWTPTVLPIQMFRIGQLELLGAPAEFTVMAGVRIRRAVQAASEAAGIRHVVFNGYANAYASYVTTREEYAAQEYEGGSTLYGPWTQAAYQQLFVDMAVALRERLPVETSAIAPDLSCCQMNFQTGVVADDPYIGKSFGDVLQQPRESYRIGDKVTVAFVTGHPKNDLRTEKTFLEVVNIGKDGKQTPETVATDNDWDTQYRWERVGISASKATISWSIPPGTEPGHYYIRHYGNAKNFWTQKISEIGGSTRSFEVLGTTP
Protein: (-)-isopiperitenone reductase (EC 1.3.1.82) (Q6WAU1)
Organism: Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata)
Function: Monoterpene synthase that catalyzes the specific reduction of the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-isopulegone. Does not catalyze the reverse reaction. Unable to reduce (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond of (-)-carvone. Able to utilize NADH with 20% the efficiency of NADPH.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MAEVQRYALVTGANKGIGFEICRQLAEKGIIVILTSRNEKRGLEARQKLLKELNVSENRLVFHQLDVTDLASVAAVAVFIKSKFGKLDILVNNAGVSGVEMVGDVSVFNEYIEADFKALQALEAGAKEEPPFKPKANGEMIEKFEGAKDCVVTNYYGPKRLTQALIPLLQLSPSPRIVNVSSSFGSLLLLWNEWAKGVLGDEDRLTEERVDEVVEVFLKDIKEGKLEESQWPPHFAAERVSKAALNAYTKIAAKKYPSFRINAICPGYAKTDITFHAGPLSVAEAAQVPVKLALLPDGGPSGCFFPRDKALALY
Protein: Probable galacturonosyltransferase-like 10 (EC 2.4.1.-) (Galactinol synthase 8) (AtGolS8) (GolS-8) (Q9LHD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pectin and/or xylans biosynthesis in cell walls.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Pathogen-associated molecular patterns-induced protein A70
- Galactinol synthase 10
- Galactinol synthase 2
Sequence:
MMSGSRLASRLIIIFSIISTSFFTVESIRLFPDSFDDASSDLMEAPAYQNGLDCSVLAKNRLLLACDPSAVHIAMTLDPAYLRGTVSAVHSILKHTSCPENIFFHFIASGTSQGSLAKTLSSVFPSLSFKVYTFEETTVKNLISSSIRQALDSPLNYARSYLSEILSSCVSRVIYLDSDVIVVDDIQKLWKISLSGSRTIGAPEYCHANFTKYFTDSFWSDQKLSSVFDSKTPCYFNTGVMVIDLERWREGDYTRKIENWMKIQKEDKRIYELGSLPPFLLVFGGDIEAIDHQWNQHGLGGDNIVSSCRSLHPGPVSLIHWSGKGKPWVRLDDGKPCPIDYLWAPYDLHKSQRQYLQYNQELEIL
Protein: Serine protease 44 (EC 3.4.21.-) (Testis serine protease 4) (TESSP-4) (Testis-specific serine protease 4) (Q402U7)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:23536369}.
Interaction partners:
- Testis-specific expressed protein 55
- Protein SPMIP9
- Disintegrin and metalloproteinase domain-containing protein 24
- Probable inactive serine protease 37
Sequence:
MAFQGCDCFGLLVWLLLLQTRLGKARMVPGTPSLSPLPSENGLDDSGVNPQERPLTGMPETSLPRKPGDSTRPLDSMAFTPGQSFSTMSLSRQPFPTWVPPTSACGHRTARIVGGRPAPARKWPWQVSLQVHKQHICGGSLISKWWVITAAHCVYGHLDYAVFMGDADLWSKRPVRIPVQDIIVHQDFSMMRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIELNIIRHEKCNQILKDIMGNIFTLVQEGGVCGYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWIIKELSRASCWKLSGFLVLSVCLVLHLAIVVAL
Protein: Dihydromonacolin L monooxygenase LovA (EC 1.14.14.124) (EC 1.14.14.125) (Dihydromonacolin L hydroxylase) (Lovastatin biosynthesis cluster protein A) (Monacolin L hydroxylase) (Q0C8M4)
Organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Function: Dihydromonacolin L monooxygenase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Subcellular location: Membrane {ECO:0000305|PubMed:21495633}; Single-pass membrane protein {ECO:0000305|PubMed:21495633}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:21495633}; Single-pass type II membrane protein {ECO:0000305|PubMed:21495633}.
Interaction partners:
Sequence:
MTVDALTQPHHLLSLAWNDTQQHGSWFAPLVTTSAGLLCLLLYLCSSGRRSELPVFNPKTWWELTTMRAKRDFDANAPSWIESWFSQNDKPIRFIVDSGYCTILPSSMADEFRKMKELCMYKFLGTDFHSHLPGFDGFKEVTRDAHLITKVVMNQFQTQAPKYVKPLANEASGIITDIFGDSNEWHTVPVYNQCLDLVTRTVTFIMVGSKLAHNEEWLDIAKHHAVTMAIQARQLRLWPVILRPLVHWLEPQGAKLRAQVRRARQLLDPIIQERRAERDSCLAKGIEPPRYVDSIQWFEDTAKGKWYDAAGAQLAMDFAGIYGTSDLLIGGLVDIVRHPHLLEPLRDEIRTVIGQGGWTPASLYKLKLLDSCLKESQRVKPVECATMRSYALQDVTFSNGTFIPKGELVAVAADRMSNPEVWPEPAKYDPYRYMRLREDPAKAFSAQLENTNGDHIGFGWHPRACPGRFFASKEIKMMLAYLLIRYDWKVVPNEPLQYYRHSFSVRIHPTTKLMMRRRDEDIRLPGSL
Protein: Reticulocyte binding protein 5 (B2L3N7)
Organism: Plasmodium falciparum (malaria parasite P. falciparum)
Interaction partners:
Sequence:
MIRIKKKLILTIIYIHLFILNRLSFENAIKKTKNQENNLTLLPIKSTEEEKDDIKNGKDIKKEIDNDKENIKTNNAKDHSTYIKSYLNTNVNDGLKYLFIPSHNSFIKKYSVFNQINDGMLLNEKNDVKNNEDYKNVDYKNVNFLQYHFKELSNYNIANSIDILQEKEGHLDFVIIPHYTFLDYYKHLSYNSIYHKSSTYGKYIAVDAFIKKINETYDKVKSKCNDIKNDLIATIKKLEHPYDINNKNDDSYRYDISEEIDDKSEETDDETEEVEDSIQDTDSNHTPSNKKKNDLMNRTFKKMMDEYNTKKKKLIKCIKNHENDFNKICMDMKNYGTNLFEQLSCYNNNFCNTNGIRYHYDEYIHKLILSVKSKNLNKDLSDMTNILQQSELLLTNLNKKMGSYIYIDTIKFIHKEMKHIFNRIEYHTKIINDKTKIIQDKIKLNIWRTFQKDELLKRILDMSNEYSLFITSDHLRQMLYNTFYSKEKHLNNIFHHLIYVLQMKFNDVPIKMEYFQTYKKNKPLTQ
Protein: Chaperone protein dnaJ-like protein (Q9SH87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Thylakoid lumenal P17.1 protein
- DnaJ/Hsp40 cysteine-rich domain superfamily protein
- At2g24860/F27C12.22
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
- Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic
- Protein disulfide-isomerase LQY1, chloroplastic
Sequence:
MDKPLLSGSEKTNESERLDSYQYLQRNSSSARNPSFAGAGVVTVEEIRTASAVSSDPPSLYPPVIKTPVSLPIPQAIGYPSASGAGHELQQRQFLDEIEIRELLIDHIGHRCCWGSRPARTWKIHAVEDCNVYVGTLDTFIEEREALTQTVPFTGGEFNGKKHGSEPGLWELDLRPQFPTLFVPYKETQVLVPNSETVEKCTGCTGRGDVVCPTCNADGEPGFYKENQMMKCSTCYGRGLVAHKDGSDTICTNCNGKGKLPCPTCQSRGLIKCQTCDSTGSLLTSSIAVVKWKTLSKRKVSATRGAGSVPEEVFDRAEGVQLCNTQAYQCTPAYFADSYFLNRFSSEVISLRAEVPPTANVVCERHTISVVPVTRVTMEDRGKAFSFYIIGFGKEIYLKDYYPARFCWGLCPCLEWLKV
Protein: Uncharacterized transporter YeaV (P0ABD1)
Organism: Escherichia coli (strain K12)
Function: Probable transporter whose substrate is unknown. Is not involved in aerobic D-malate transport.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Carnitine monooxygenase oxygenase subunit
- Glycine betaine uptake system ATP-binding protein YehX
- 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM
- Inner membrane metabolite transport protein YhjE
Sequence:
MVLLAMGLVIYLATSKYGNIRLGEGKPEYSTLSWLFMFICAGLGSSTLYWGVAEWAYYYQTPGLNIAPRSQQALEFSVPYSFFHWGISAWATYTLASLIMAYHFHVRKNKGLSLSGIIAAITGVRPQGPWGKLVDLMFLIATVGALTISLVVTAATFTRGLSALTGLPDNFTVQAFVILLSGGIFCLSSWIGINNGLQRLSKMVGWGAFLLPLLVLIVGPTEFITNSIINAIGLTTQNFLQMSLFTDPLGDGSFTRNWTVFYWLWWISYTPGVAMFVTRVSRGRKIKEVIWGLILGSTVGCWFFFGVMESYAIHQFINGVINVPQVLETLGGETAVQQVLMSLPAGKLFLAAYLGVMIIFLASHMDAVAYTMAATSTRNLQEGDDPDRGLRLFWCVVITLIPLSILFTGASLETMKTTVVLTALPFLVILLVKVGGFIRWLKQDYADIPAHQVEHYLPQTPVEALEKTPVLPAGTVFKGDN
Protein: Transcription factor cbf11 (C-promoter element-binding factor-like protein 11) (O74954)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcription factor that behaves as a negative regulator of adhesion. Recognizes specifically the canonical CSL response element GTGA/GGAA. May also play a cbf12-antagonistic role in the regulation of a number of other important processes such as extracellular material production, colony morphogenesis, ploidy maintenance, or meiosis.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Transcription factor cbf12
- Sphingosine N-acyltransferase lag1
- Triacylglycerol lipase ptl1
- Acetyl-CoA carboxylase
- Uncharacterized transcriptional regulatory protein C15D4.02
Sequence:
MGDYFAWDFANISGSNTSGSLNLNQLNLDNINNGLHNQEDGAGGRNENSERVGSGSPGSVSMQVLSLFSAVNSALATLEKSEEFPSVVKDEQSIFPAVAKASNSLDELAQNIIPAPSPPGFNRKRKTFDEDSSVEMIRRAISDHLDLLNNCCIGIANLNEDSVHKISLTRSGKPSQLVTVSCRHSSVIQKSYGSEKRYLCPPPMVYINGNYSSIFNQSFRTEISIMNDFGQCSQPISEEYTGQGCMIFRSLHISSLVAAKSKNLRLSLDMFSNVNNQLLSHLVTSSISIVSKPSKKGSKLKISNITLRSGSVVSLYNRINSQTVRTKYTSIEAGQFCLRGDRWVPLRINLLLPDENGKLKVCDDVDNPEPIKYGSIVELVDEATGTTSDPLIIRRVEKDHIAEEDGYVNQMHRIVLESAYPISNVRHLKIAEHSSLAYSNNISVRWFLGATSAQNRNASSEAILPIEWEAVGNLSSNEMTRVGDSVCWTIVGISHFDCTMMLPFNQNPVPTVTDYPYIEEPPEYLESSRSLQFKIGGYSVGLQIWLGVHGPLSYSFTAAADTSTMGTVTLGLSQISYDPSCAEQKYPLLFVIPGGIVIIGKCEILLTSSAFGN
Protein: Protein GrpE (HSP-70 cofactor) (C4ZYN1)
Organism: Escherichia coli (strain K12 / MC4100 / BW2952)
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
Interaction partners:
Sequence:
MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKVANLEAQLAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIELTLKSMLDVVRKFGVEVIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA
Protein: Casein kinase I isoform alpha (CKI-alpha) (EC 2.7.11.1) (CK1) (P48729)
Organism: Homo sapiens (Human)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2 (By similarity). May play a role in segregating chromosomes during mitosis. May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration. Acts as an inhibitor of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1409656}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:1409656}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:1409656}. Nucleus speckle {ECO:0000303|PubMed:18305108}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BK63}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8BK63}. Note=Localizes to the centrosome in interphase cells, and to kinetochore fibers during mitosis. Also recruited to the keratin cytoskeleton (PubMed:23902688). {ECO:0000269|PubMed:1409656, ECO:0000269|PubMed:23902688}.
Interaction partners:
- Axin-1
- Adenomatous polyposis coli protein
- Glycogen synthase kinase-3 beta
- Catenin beta-1
- Protein cereblon
- Axin-2
- Glycogen synthase kinase-3 alpha
- Protein Mdm4
- E3 ubiquitin-protein ligase Mdm2
- APC membrane recruitment protein 1
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF
Protein: Cysteine-rich secretory protein LCCL domain containing 2 (A0A0G2JYX8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLHNKLRGQVYPPASNMEYMTWDEELERSAAAWAQRCLWEHGPASLLVSIGQNLAVHWGRYRSPGFHVQSWYDEVKDYTYPYPHECNPWCPERCSGAMCTHYTQMVWATTNKIGCAVHTCRSMSVWGDIWENAVYLVCNYSPKGNWIGEAPYKHGRPCSECPSSYGGGCRNNLCYRGR
Protein: Oxygen-evolving enhancer protein 3-2, chloroplastic (OEE3) (16 kDa subunit of oxygen evolving system of photosystem II) (OEC 16 kDa subunit) (Q41932)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for photosystem II assembly/stability and photoautotrophic growth under low light conditions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}; Peripheral membrane protein {ECO:0000269|PubMed:11719511}; Lumenal side {ECO:0000269|PubMed:11719511}. Note=Associated with the photosystem II complex.
Interaction partners:
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Oxygen-evolving enhancer protein 1-2, chloroplastic
- Putative oxygen-evolving enhancer protein 2-2
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Chlorophyll a-b binding protein CP26, chloroplastic
- Photosystem I reaction center subunit IV A, chloroplastic
- Photosystem II CP43 reaction center protein
- Cytochrome b559 subunit alpha
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem II CP47 reaction center protein
Sequence:
MAQAVTSMAGLRGASQAVLEGSLQINGSNRLNISRVSVGSQRTGLVIRAQQNVSVPESSRRSVIGLVAAGLAGGSFVKAVFAEAIPIKVGGPPLPSGGLPGTDNSDQARDFSLALKDRFYIQPLSPTEAAARAKDSAKEIINVKSFIDKKAWPYVQNDLRLRASYLRYDLNTVISAKPKEEKQSLKDLTAKLFQTIDNLDYAARSKSSPDAEKYYSETVSSLNNVLAKLG
Protein: Calmodulin regulator protein PCP4 (Brain-specific polypeptide PEP-19) (Purkinje cell protein 4) (P48539)
Organism: Homo sapiens (Human)
Function: Functions as a modulator of calcium-binding by calmodulin. Thereby, regulates calmodulin activity and the different processes it controls. For instance, may play a role in neuronal differentiation through activation of calmodulin-dependent kinase signaling pathways.
Interaction partners:
- Calmodulin-like protein 6
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Calmodulin-1
Sequence:
MSERQGAGATNGKDKTSGENDGQKKVQEEFDIDMDAPETERAAVAIQSQFRKFQKKKAGSQS
Protein: A-kinase anchor protein 17A (AKAP-17A) (721P) (B-lymphocyte antigen) (Protein XE7) (Protein kinase A-anchoring protein 17A) (PRKA17A) (Splicing factor, arginine/serine-rich 17A) (Q02040)
Organism: Homo sapiens (Human)
Function: Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre-mRNA splicing in a PKA-dependent manner.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:16982639, ECO:0000269|PubMed:19840947}.
Interaction partners:
- Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein
- Acetylserotonin O-methyltransferase
- ADP/ATP translocase 3
- Putative GTP-binding protein 6
- Caspase activity and apoptosis inhibitor 1
Sequence:
MAAATIVHDTSEAVELCPAYGLYLKPITKMTISVALPQLKQPGKSISNWEVMERLKGMVQNHQFSTLRISKSTMDFIRFEGEVENKSLVKSFLACLDGKTIKLSGFSDILKVRAAEFKIDFPTRHDWDSFFRDAKDMNETLPGERPDTIHLEGLPCKWFALKESGSEKPSEDVLVKVFEKFGEIRNVDIPMLDPYREEMTGRNFHTFSFGGHLNFEAYVQYREYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKHLSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRERLLSILLSKKPDDSHTHDELGVAHADLLQPVLDILQTVSSGCVSATTLHPLGGQPPAGAPKESPAHPEADGAPKSVNGSVAEEAPCKEVQSSCRVVPEDGSPEKRCPGGVLSCIPDNNQQPKGIPACEQNVSRKDTRSEQDKCNREPSKGRGRATGDGLADRHKRERSRARRASSREDGRPRKERRPHKKHAYKDDSPRRRSTSPDHTRSRRSHSKDRHRRERSRERRGSASRKHSRHRRRSERSRSRSPSRHRSTWNR
Protein: Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit) (P18946)
Organism: Gallus gallus (Chicken)
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein {ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 6
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 6
- NADH-ubiquinone oxidoreductase chain 3
- Cytochrome c oxidase subunit 3
- NADH-ubiquinone oxidoreductase chain 4L
- Complex III subunit 9
- Ubiquinol-cytochrome c reductase core protein 2.
- ATP synthase F
Sequence:
MAPNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVCLMTQILTGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTLVEWAWGGFSVDNPTLTRFFALHFLLPFAIAGITIIHLTFLHESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPFLTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPLSQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFTILLILFPTIGTLENKMLNY
Protein: Innate immunity activator protein (Q7TN12)
Organism: Mus musculus (Mouse)
Function: Expressed in peripheral macrophages and intestinal myeloid-derived cells, is required for optimal PRR (pattern recognition receptor)-induced signaling, cytokine secretion, and bacterial clearance. Upon stimulation of a broad range of PRRs (pattern recognition receptor) such as NOD2 or TLR2, TLR3, TLR4, TLR5, TLR7 and TLR9, associates with YWHAQ/14-3-3T, which in turn leads to the recruitment and activation of MAP kinases and NF-kappa-B signaling complexes that amplifies PRR-induced downstream signals and cytokine secretion (By similarity). In the intestine, regulates adherens junction stability by regulating the degradation of CYTH1 and CYTH2, probably acting as substrate cofactor for SCF E3 ubiquitin-protein ligase complexes. Stabilizes adherens junctions by limiting CYTH1-dependent ARF6 activation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q3KP66}. Cytoplasm {ECO:0000250|UniProtKB:Q3KP66}. Note=Translocates to the nucleus upon NOD2 stimulation. {ECO:0000250|UniProtKB:Q3KP66}.
Interaction partners:
Sequence:
MLQMPKLNEIPPGRGGPGEPWGEGRWAGPTGPEAARPARGARGQARGARARWDSWEHSRLPTHPGPGWDQCSPSFLCAPSSQKLIMESKDEVSDSDSGIILQSGPDSPVSPMKELTNAVRKQQRALEARLEACLEELRRLCLREAELTGTLPAEYPLKPGEKAPKVRRRIGAAYKLDEWALHREDPLSSLERQLALQLQITEAARRLCAEENLSRQARRQRKHAALQEEKKLRDLQRCLGDRRRNSEPPPTTVPSLGRELSASDDSSLSDGLLLEEEDSQAPKPPPESPAPPSRPLPPQSLEGLQPTGPESGGQERAPIQNSPWKETSLDHPYEKPRKSSELSSESSSPATTPQDQPNPSSLWVLDAASYHVVPIRNVPGQRQGRTSAPATPEMQGRRGQSQSLRVDSFRAGAEGRGRSAFPRRRPTHYTVTVPDSCFTPGKPPLPHPACHSCSEDSGSDVSSISHPTSPGSSSPDISFLRPLCLPEPPRHRGAWGPACGRELAPHYSKLLLPAGYFPTGRYVMVAEGHLPPGEWELCRAAVGAAYDEEGAPLRYQRLVPSHSRIVRTPSLKDSPAGRGLSKAAVSEELKWWHERARLRSSRPHSLDRQGAFRVRSLPPGRESFGRASGPRTQVPPVYVLRRSTDGAPVQVFVPENGEIISQV