wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein phosphatase non-receptor type 9 (EC 3.1.3.48) (Q641Z2)
Organism: Rattus norvegicus (Rat)
Function: Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MEPATAPRPDMAPELTPEEEQATKQFLEEINKWTVQYNVSPLSWNVAVKFLMARKFDVLRAVELFHCYRETRRKEGIVKLKPHEEPLRSEILSGKFTILNVRDPTGASIALFTARLHHPHKSVQHVVLQALFYLLDRAVDSFETQRNGLVFIYDMCGSNYANFELDLGKKVLNLLKGAFPARLKKVLIVGAPIWFRVPYSIISLLLKDKVRERIQILKTSEVTQHLPRECLPENLGGYIKIDLATWNFQFLPQVNGHPDPFDEIILFSLPPALDWDSVHVPGPHAMTIQELVDYVNTRQKQGIYEEYEDIRRENPVGTFHCSMSPGNLEKNRYGDVPCLDQTRVKLTKRSGHTQTDYINASFMDGYKQKNAYIGTQGPLENTYRDFWLMVWEQKVLVIVMTTRFEEGGRRKCGQYWPLEKDSRIQFGFLTVTNLGVENMNHYKKTTLEIHNTEERQKRQVTHFQFLSWPDYGVPSSAASLIDFLRVVRSQQSMAVGSLGARSKGQCPEPPIVVHCSAGIGRTGTFCSLDICLAQLEELGTLNVFQTVSRMRTQRAFSIQTPEQYYFCYKAILEFAEREGMVPSGHSLLAMDGQ
Protein: Gamma-crystallin C (Gamma-C-crystallin) (Q61597)
Organism: Mus musculus (Mouse)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Gamma-crystallin D
- Gamma-crystallin E
- Gap junction alpha-8 protein
- Lens fiber major intrinsic protein
- Gamma-crystallin B
- Phakinin
- Heat shock factor protein 4
- Gap junction alpha-3 protein
Sequence:
MGKITFFEDRSFQGRCYECSSDCPNLQTYFSRCNSVRVDSGCWMLYERPNYQGHQYFLRRGEYPDYQQWMGFSDSIRSCRLIPHAGSHRMRLYEKEDHKGVMMELSEDCSCIQDRFHLSEVRSLQVLEGCWVLYEMPNYRGRQYLLRPQEYRRFQDWGSVDAKAGSLRRVVDLY
Protein: Conserved protein (P72040)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible enoyl-CoA hydratase EchA21
- Uncharacterized protein Rv0048c
- Anti-sigma-L factor RslA
- Probable conserved transmembrane protein alanine and leucine rich
Sequence:
MPPESRPGPDSPPTDELACAEAALQVLQQVLHTIGRQDKAKQTPCPGYDVKKLTEHLLNSIMVLGGMVGAEFSLRADIDSVERLVSGAARSALDAWHRHGLEGDVSLGPGSMSAKVAVSVFSVEFLVHAWDYAVAVGSELKAADSLAEYVLELARKLIKPEERSVAGFNEPVDVPEDGGALERLIAFTGRNPAR
Protein: Deadenylation-dependent mRNA-decapping factor pdc2 (DNA topoisomerase 2-associated protein PAT1 homolog pdc2) (Partner of decapping enzyme protein 2) (Protein PAT1 homolog pdc2) (O42958)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. Stabilizes the 3' terminus of mRNAs and modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Necessary for accurate chromosome transmission during cell division (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:28031482}. Nucleus {ECO:0000269|PubMed:28031482}. Cytoplasm, P-body {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:28031482}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:28031482}.
Interaction partners:
- LSM1-LSM7 complex subunit lsm1
- LSM complex subunit lsm4
- LSM complex subunit lsm7
- LSM complex subunit lsm2
- LSM complex subunit lsm3
- LSM complex subunit lsm5
- LSM complex subunit lsm6
- Putative ATP-dependent RNA helicase ste13
- mRNA decapping complex subunit 2
- 5'-3' exoribonuclease 1
Sequence:
MSFFGFNTTLPKENMFPNEGQLEEDGIDFEETYDDLGNQLNEAGDELNDETFGVSAGSIGRDFDFSGTTAQASAQLEDEQYQINQQNIFAKPVKPASSELPQVSRLNGASQFPSREPASTAINKLSDLQPMASIWENIVPEKPAIIPPEVASLQDRLGAQPSEKVFSLQELEEQLLNSMTAPKPPSQPAIPIVPSEMAAQVTRENISSLDPAISAASIGNVTFGQPNIPSTTTDFAGLAAPNMVHPSQAIPNPVMQPSLVPQMPYPQNGMYNPSVAPPASLVNLFQQEQLIQNQNLDEKRQKLERDHMLMAQCAGLMTRSDKSFIARIQISQLMSEDPESDDFYYRVYSIIRGRKPSEEEASHFIQTYLGPSNNRRRGRRSENPMQKLQQQLQRLVSSAKERPKATQLSLEGALGKIAVNTVRTPRQLLNVKRPTEPASSNSSLNNFSGFSTKKDVLHAIEKVYDLLLDFEQALRKASTLETTDQEQIDTWKTTLSEKLESIWKALYINESLEASSKTRPPFISIISHPKGMRLLPRLFPHLSKEQQISILKVVVYNFDSLDIVLRGTFDVNGELPLDVVSEMSSFTQFIIPPLLTIVNELDLETINNLFSQLLNRTNAVYLIQTKIGLSFLTLFISRAEILKQSGTVNQNEKEEWENTFNVMFNRVKGHFSTVFPPPNARAYADESYPWEFLAACATAASSEQHFTLVSETRDRVLDNIITSKRAPSEIAVVRISNVNLFLNAMGLDARQLSA
Protein: Secretion protein XqhA (Q9I2M7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442, ECO:0000256|RuleBase:RU004004}.
Interaction partners:
- XphA
- Type II secretion system protein N
- Type II secretion system protein K
- Type II secretion system protein E
- Type II secretion system protein J
- Type II secretion system protein F
- Type II secretion system core protein G
- Type II secretion system core protein G
- Type II secretion system core protein G
- Type II secretion system protein I
Sequence:
MPRCSTRSAQRLSPLFLVLSLAVLGLAPPVHPAPAETAAAQEEEQWTINMKDAEIGDFIEQVSSISGQTFVVDPRVKGRVTVVSQARLSLAEVYQLFLSVLATHGYAVLPQGDQARIVPNMEARQDAAQKTVRDGPGSLETRVVQAQQTSVAELIPMIRPLVPAHGHLAAVPSANALIVSDRRSNIERIEAIVRSLDRAGEHDYSIYDMRHAWVAEIAEVLDRSVTPAAGKSAATVQVLADSRSNRLVLLGPPQARARLLRLAQSLDVPSSRSANSRVIRLRHGDAKTLAATLGEIGESLHGERGQDGRGSGKRGLLVRADESLNALVILADPEDVGLLEDIVRQLDVPRAQLLVEAAIVELSGEIGDALGVQWALRSGHVAGGAGFADSGLSIGTLLGALQAGKPPAELPDGAIVGLGSRDFGALVTALSRNSRSNLLSTPSLLTLDNQKAEILVGQNVPFQTGSYTTSASGSSNPFTTVERKDIGVTLKVTPHIGEDRMLRLEIEQEISSIAPTATLAAKAVDLVTNKRSIKSTVLADDGQVIVLGGLIQDDLQRSDSRVPLLGDIPGVGRLFRSSRETRVKRNLMVFLRPSIVRDAAGLERISHGRYRSIQLLRGAAGEPARPLFEDAGAIDLRPAAQVAPAPIGSPRSYPAPAPVLMEKPRLADPASLGDGRGGEVLEVRQGTHAPQPPSPQRYAVRLVEGSSEAFMRALIERHPGLSLRLRRELRDGQELFAVERGDYLDPEQARRALAELPESLPRGKARVIAHTPGSAL
Protein: Engulfment and cell motility 2 (Q5JVZ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPPPSDIVKVAIEWPGANAQLLEIDQKRPLASIIKEVCDGWSLPNPEYYTLRYADGPQLYITEQTRSDIKNGTILQLAISPSRAARQLMERTQSSNMETRLDAMKELAKLSADVTFATEFINMDGIIVLTRLVESGTKLLSHYSEMLAFTLTAFLELMDHGIVSWDMVSITFIKQIAGYVSQPMVDVSILQRSLAILESMVLNSQSLYQKIAEEITVGQLISHLQVSNQEIQTYAIALINALFLKAPEDKRQDMANAFAQKHLRSIILNHVIRGNRPIKTEMAHQLYVLQVLTFNLLEERMMTKMDPNDQAQRDIIFELRRIAFDAESDPSNAPGSGT
Protein: Macrophage colony-stimulating factor 1 (CSF-1) (MCSF) (Proteoglycan macrophage colony-stimulating factor) (PG-M-CSF) [Cleaved into: Processed macrophage colony-stimulating factor 1; Macrophage colony-stimulating factor 1 43 kDa subunit] (P07141)
Organism: Mus musculus (Mouse)
Function: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed macrophage colony-stimulating factor 1]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Macrophage colony-stimulating factor 1 receptor
- Interleukin-34
- Pro-epidermal growth factor
- Mast/stem cell growth factor receptor Kit
- Granulocyte-macrophage colony-stimulating factor
- Proto-oncogene tyrosine-protein kinase Src
- Receptor-type tyrosine-protein kinase FLT3
- Epidermal growth factor receptor
- Vascular endothelial growth factor receptor 2
- Tumor necrosis factor ligand superfamily member 11
Sequence:
MTARGAAGRCPSSTWLGSRLLLVCLLMSRSIAKEVSEHCSHMIGNGHLKVLQQLIDSQMETSCQIAFEFVDQEQLDDPVCYLKKAFFLVQDIIDETMRFKDNTPNANATERLQELSNNLNSCFTKDYEEQNKACVRTFHETPLQLLEKIKNFFNETKNLLEKDWNIFTKNCNNSFAKCSSRDVVTKPDCNCLYPKATPSSDPASASPHQPPAPSMAPLAGLAWDDSQRTEGSSLLPSELPLRIEDPGSAKQRPPRSTCQTLESTEQPNHGDRLTEDSQPHPSAGGPVPGVEDILESSLGTNWVLEEASGEASEGFLTQEAKFSPSTPVGGSIQAETDRPRALSASPFPKSTEDQKPVDITDRPLTEVNPMRPIGQTQNNTPEKTDGTSTLREDHQEPGSPHIATPNPQRVSNSATPVAQLLLPKSHSWGIVLPLGELEGKRSTRDRRSPAELEGGSASEGAARPVARFNSIPLTDTGHVEQHEGSSDPQIPESVFHLLVPGIILVLLTVGGLLFYKWKWRSHRDPQTLDSSVGRPEDSSLTQDEDRQVELPV
Protein: Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F) (P30405)
Organism: Homo sapiens (Human)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:10406942}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC1
- ADP/ATP translocase 1
- Cellular tumor antigen p53
- Mitochondrial inner membrane m-AAA protease component paraplegin
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- Cytochrome c
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- ADP/ATP translocase 3
Sequence:
MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS
Protein: Solute carrier family 2, facilitated glucose transporter member 6 (Glucose transporter type 6) (GLUT-6) (Q3UDF0)
Organism: Mus musculus (Mouse)
Function: Probable sugar transporter that acts as a regulator of glycolysis in macrophages. Does not transport glucose (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9UGQ3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MQEPLLRTEGLDYDTFPEVPATPGERERAGALKNRRVFLATFAAVLGNFSFGYALVYTSPVIPELKLSSDPALHLDKIQASWFGSVFTLGAAAGGLSAMLLNDLLGRKLSIMFSAVPSAIGYAIMAGARGLWMLLLGRMLTGFAGGLTAACIPVYVSEIAPPDVRGALGATPQLMAVFGSLSLYALGLLLPWRWLAVAGEGPVLIMILLLSFMPNSPRFLLSKSRDEEALQALTWLRADSEVHWEFEQIQDNVRRQSSRVSWAEAREPRVYRPVLIAVLMRFLQQLTGITPILVYLQTIFDNTSVVLPSQQDAAIVGAVRLLSVLIAAVTMDLAGRKVLLYVSASVMFAANLTLGLYVQFVPRPLTPNSTVEIVTLGDTAFNYLTLIPLLATMLFIMGYAMGWGPITWLLMSEVLPLRARGVASGLCVLVSWLTAFVLTNYFLLAVNAFGLQVPFFFFSAICLLSLLFTGCCVPETRGRSLEQIEAFFHTRRMSFRP
Protein: Dihydromethanopterin reductase (acceptor) (H(2)MPT reductase) (EC 1.5.99.15) (Q57661)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Involved in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. Catalyzes the reduction of dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin (H(4)MPT). Ferredoxin may serve as an electron donor.
Interaction partners:
- Tetrahydromethanopterin:alpha-L-glutamate ligase
- 4-phosphopantoate--beta-alanine ligase
Sequence:
MNYRFGINMKIVWCITGAGHLLRESFQVMKRLKEEIEDLKVTTLVSRAGEEVVKMYGLFGELYNISNGNYYEELILEREHPYSSPITGRLSLGKYDYLICSPATGNTVAKVVNGIADSLVTNAIAQAGKGFVKSLIVPVDYKAGIVTTKLPYAIDKKKCKLCLKCINVCPNGAIVKRDNFVEILLSKCLGCGNCKKVCPYNAIIEGKEIKMRVRKIDAENTRKLMELEDVIVLKHPYEILEFFNIR
Protein: Profilin-4 (AtPROF3) (AthPRF4) (Q38904)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:17933902}.
Interaction partners:
- Actin-depolymerizing factor 7
- Actin-depolymerizing factor 1
- Actin-depolymerizing factor 12
- Actin-depolymerizing factor 4
- Formin-like protein 2
- Actin-depolymerizing factor 2
- Actin-depolymerizing factor 9
- Actin-depolymerizing factor 5
- Actin-depolymerizing factor 8
- Putative actin-depolymerizing factor 11
Sequence:
MSWQTYVDEHLMCDVGDGQGHHLTAAAIVGHDGSVWAQSANFPQFKGQEFSDIMKDFDEPGHLAPTGLFMAGAKYMVIQGEPGAVIRGKKGAGGITIKKTGQSCVFGIYEEPVTPGQCNMVVERLGDYLLEQGL
Protein: 2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase) (EC 2.3.3.16) (P31660)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA to yield citrate but with a lower specificity.
Interaction partners:
- 2-methylcitrate dehydratase
- 2-methylisocitrate lyase
- Propionate--CoA ligase
- Phosphate acetyltransferase
- Acetyl-coenzyme A synthetase
- Isocitrate dehydrogenase
- Propanoyl-CoA:succinate CoA transferase
- Formate acetyltransferase 1
- PFL-like enzyme TdcE
- Methylmalonyl-CoA decarboxylase
Sequence:
MSDTTILQNSTHVIKPKKSVALSGVPAGNTALCTVGKSGNDLHYRGYDILDLAKHCEFEEVAHLLIHGKLPTRDELAAYKTKLKALRGLPANVRTVLEALPAASHPMDVMRTGVSALGCTLPEKEGHTVSGARDIADKLLASLSSILLYWYHYSHNGERIQPETDDDSIGGHFLHLLHGEKPSQSWEKAMHISLVLYAEHEFNASTFTSRVIAGTGSDMYSAIIGAIGALRGPKHGGANEVSLEIQQRYETPDEAEADIRKRVENKEVVIGFGHPVYTIADPRHQVIKRVAKQLSQEGGSLKMYNIADRLETVMWESKKMFPNLDWFSAVSYNMMGVPTEMFTPLFVIARVTGWAAHIIEQRQDNKIIRPSANYVGPEDRPFVALDKRQ
Protein: Developmentally-regulated G-protein 1 (AtDRG1) (Developmentally-regulated G-protein 2A) (AtDRG2a) (Q9LQK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds GDP and GTP, and has low GTPase activity. May interact with phosphatidic acid (PA).
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:10380799}. Cytoplasm {ECO:0000269|PubMed:10380799}.
Interaction partners:
- UPF0235 protein At5g63440
- Ubiquitin-conjugating enzyme family protein
- Zinc finger CCCH domain-containing protein 21
- Probable cysteine protease RD21B
- Cysteine proteinase RD21A
- At1g09850
- Probable cysteine protease RD21C
- DEAD-box ATP-dependent RNA helicase 16
- Protein ILITYHIA
- Probable glycine-rich RNA-binding protein 1
Sequence:
MGIIERIKEIEAEMARTQKNKATEYHLGQLKAKIAKLRTQLLEPPKGASGGGEGFEVTKYGHGRVALIGFPSVGKSTLLTMLTGTHSEAASYEFTTLTCIPGVIHYNDTKIQLLDLPGIIEGASEGKGRGRQVIAVAKSSDLVLMVLDASKSEGHRQILTKELEAVGLRLNKTPPQIYFKKKKTGGISFNTTAPLTHIDEKLCYQILHEYKIHNAEVLFRENATVDDFIDVIEGNRKYIKCVYVYNKIDVVGIDDVDRLSRQPNSIVISCNLKLNLDRLLARMWDEMGLVRVYSKPQGQQPDFDEPFVLSSDRGGCTVEDFCNHVHRTLVKDMKYALVWGTSTRHNPQNCGLSQHLEDEDVVQIVKKKERDEGGRGRFKSHSNAPARIADREKKAPLKQ
Protein: Leucine-rich repeat transmembrane neuronal 2 (Leucine-rich repeat transmembrane neuronal protein 2 precursor) (F1R4D3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Neurexin-3a.
- Neurexin-1a-beta
- Neurexin 2a
- Neuroligin 1
- Disks large homolog 4
- SH3 and multiple ankyrin repeat domains 2a.
- Peripheral plasma membrane protein CASK
Sequence:
MGFHSRWPLVGQAPAALCVISMLLCLPPVSCTTCPQKCRCEDLQFYCDTQGLLAPPDGVDKGALGLSLRHNSISELSSDQFFGFTQLTWLHLDHNQITTVHEDAFQGLYKLKDLNLSSNRITKLPNTTFIHLINLQILDLSFNQMTALEPELFHGLRKLQILHLRSNSLRTTPVRAFWDCRSLEYLGLSNNRLRSLARNGFAGLIKLRELHLEHNHLTKINLAHFPRLVALQFLYLQWNKINNLTSTMEWKWTTLEKLDLTGNEIRVLIPEVFETLPSLKILLLDNNKLSNLDSQTMDMWKSLNVIGLSSNLWECTKRICNLATWLSTFKGRWEHSILCYSPEYAQGEEILDAVYGFQLCQNFSAPVVLTSTSTEAMLPDITSSLFGNMQTPTQDFYAEDFGSFTIVTTTTTTTQPPRTALATTMTVEGADVTEDYSAMDNTLLTQRVIIGTMALLFSFFLIIFVVYISRKCCPPTLRRIRHCSAIQNRRQMRTQQRQPMADLATQVPYNEYETSHEEGALVIINGYGQCKCQQLPYKECEV
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 (Q9SKC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
Interaction partners:
- Transmembrane protein
- NADH dehydrogenase 1 beta subcomplex subunit 10-B
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase iron-sulfur protein 8-B, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase iron-sulfur protein 6
- Cytochrome b-c1 complex subunit 9, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
Sequence:
MEVPGSSKKMIATQEEMSAAKIALGSRDMCAHLLIPLNKCRQAEFYLPWKCEDERHVYEKCEYELVMERMLAMKKIREEEALAKQNKLQGNAAVPLIPKTANA
Protein: Cytoplasmic polyadenylation element-binding protein 1-A (CPE-BP1-A) (CPE-binding protein 1-A) (CPEB-1-A) (58 kDa CPE-binding protein) (Q91572)
Organism: Xenopus laevis (African clawed frog)
Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation and early development. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In the absence of phosphorylation and in association with tacc3/maskin, also acts as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation. Requires zinc for RNA binding. Involved in the cell cycle progression from S phase into M phase.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Membrane. Note=During mitosis localizes with tacc3/maskin and CPE-containing mRNAs to both spindle poles. Membrane-associated. Colocalizes with members of the polyadenylation and translation complex factors (cpsf, aplp1, tacc3/maskin, aurka, etc.), including CPE-containing RNAs.
Interaction partners:
Sequence:
MAFPLKDDLGRAKDCWGCPSDTPALSTCSNADIFRRINAMLDNSLDFTGVCTTPNTKGKCEHLQDYQDTEGPAASRMLFSTSHEPLPRGLPDTNDLCLGLQSLSLTGWDRPWSTQDSEAGGHSSTPTAAQSVFSMLNSPMGKPSPLGFLTFDPIGSDLMEKYPTPLLRSSRLDSRSILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLPLGGGVSRDPLKLGIGSRLDQDHAALAAATVSPLGITKGWPSTSVWPSWDLLDSAEDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPVYSCKVFLGGVPWDITETGLINTFRVFGALSVEWPGKDGKHPRCPPKGNMPKGYVYLVFESEKSVRALLQACSQDLLSQDGLSEHYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLDPSKTVFVGALHGMLNAEALASIMNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTAKFTKKVQIDPYLEDSVCQVCNAQPGPFFCRDQVCFKYFCRSCWHWQHSMEILRHHRPLMRNQKSRDSS
Protein: N-alpha-acetyltransferase 40 (EC 2.3.1.257) (N-acetyltransferase 11) (N-alpha-acetyltransferase D) (NatD) (hNatD) (Protein acetyltransferase 1) (Q86UY6)
Organism: Homo sapiens (Human)
Function: N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A. In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence'. Acts as a negative regulator of apoptosis. May play a role in hepatic lipid metabolism (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25732826}. Nucleus {ECO:0000269|PubMed:25732826}.
Interaction partners:
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 60
- N-alpha-acetyltransferase 20
- WD repeat-containing protein 11
- Histone H4
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 80
- Exportin-T
Sequence:
MGRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRLGDPLEAFPVFKKYDRNGLNVSIECKRVSGLEPATVDWAFDLTKTNMQTMYEQSEWGWKDREKREEMTDDRAWYLIAWENSSVPVAFSHFRFDVECGDEVLYCYEVQLESKVRRKGLGKFLIQILQLMANSTQMKKVMLTVFKHNHGAYQFFREALQFEIDDSSPSMSGCCGEDCSYEILSRRTKFGDSHHSHAGGHCGGCCH
Protein: Putative ammonium transporter 1 member 5 (AtAMT1;5) (Q9LK16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ammonium transport.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nitrogen regulatory protein P-II homolog
- Urea-proton symporter DUR3
Sequence:
MSGAITCSAADLSALLGPNATAAADYICGQLGSVNNKFTDAAYAIDNTYLLFSAYLVFAMQLGFAMLCAGSVRAKNTMNIMLTNVLDAAAGGLFYYLFGYAFAFGESSDGFIGRHNFGLQNFPTLTSDYSFFLYQWAFAIAAAGITSGSIAERTKFVAYLIYSSFLTGFVYPVVSHWFWSPDGWASPFRSEDRLFGTGAIDFAGSGVVHMVGGIAGLWGALIEGPRIGRFPDGGHAIALRGHSASLVVLGTFLLWFGWYGFNPGSFTKILIPYNSGSNYGQWSGIGRTAVTTTLSGCTAALTTLFGKRLLSGHWNVTDVCNGLLGGFAAITAGCSVVDPWAAIVCGFVASLVLIGCNKLAELLKYDDPLEAAQLHGGCGAWGLIFVGLFAKEKYINEVYGASPGRHYGLFMGGGGKLLGAQLVQIIVIVGWVSATMGTLFFILKKLNLLRISEQHEMRGMDLAGHGGFAYIYHDNDDDSIGVPGSPVPRAPNPPAV
Protein: Protein TIC 20-IV, chloroplastic (Translocon at the inner envelope membrane of chloroplasts 20-IV) (AtTIC20-IV) (Q9ZQZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein precursor import into chloroplasts. Partially redundant with TIC20-I, but not with TIC20-II or TIC20-V.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:21395885}; Multi-pass membrane protein {ECO:0000269|PubMed:21395885}.
Interaction partners:
- Protein TIC 20-v, chloroplastic
- Protein TIC 20-II, chloroplastic
- Protein TOC75-4, chloroplastic
- Probable inactive shikimate kinase like 1, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic
Sequence:
MQGLAATTTNRGSLTFLAPRNHSPISKKFVNPRVFFPNVDSSAKLRLSASSISRRCPREIAPLSATASVDFAAAATSSNQLFANGLPPLAPGLRRHRRPIEPARVAKDDFFKIKLPKIAERPEWWWRTLACVPYLISLQISDVGFYVQPFLEKHDAIGDMIYFIPGAINRWPTWFFMVYCYLGYMWVVKNKELPHYLRFHMMMGMLLETALQVIWCTSNFFPLIHFKGRFGMYYWMAIGFTYICLLLECIRCALAGVYAQIPFMTDAASIHTLFNLGGFQRPLR
Protein: Non-structural protein ORF4a (ORF4a) (K9N4V0)
Organism: Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1)
Function: DsRNA-binding protein that plays a role in the inhibition of host innate response. Suppresses host PACT-induced activation of RIGI and MDA5 and thereby circumvents the production of type I inteferons. Prevents also the activation of host NF-kappaB.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:24318862}.
Interaction partners:
Sequence:
MDYVSLLNQIWQKYLNSPYTTCLYIPKPTAKYTPLVGTSLHPVLWNCQLSFAGYTESAVNSTKALAKQDAAQRIAWLLHKDGGIPDGCSLYLRHSSLFAQSEEEESFSN