wanglab/gogpt-training-data huggingface dataset:
Protein: Amyloid-beta A4 precursor protein-binding family A member 2 (Adapter protein X11beta) (Neuron-specific X11L protein) (Neuronal Munc18-1-interacting protein 2) (Mint-2) (P98084)
Organism: Mus musculus (Mouse)
Function: Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
Interaction partners:
- Amyloid-beta precursor protein
- Peripheral plasma membrane protein CASK
- Calsyntenin-1
- Syntaxin-binding protein 1
Sequence:
MAHRKRQSTASSMLDHRARPGPIPHDQEPESEDTELPLESYVPTGLELGTLRPESPTPEEQECHNHSPDGDSSSDYVNNTSEEEDYDEGLPEEEEGVTYYIRYCPEDDSYLEGMDCNGEEYIAHGAHPVDTDECQEAVEDWTDSVGPHTHSHGAENSQEYPDGHLPIPEDDPTVLEVHDQEEDGHYCSSKESYQDYYPPETNGNTGGASPYRMRRGDGDLEEQEEDIDQIVAEIKMSLSMTSITSASEASPEHMPELDPGDSTEACPPSDTGHGPGRQEARPKSLNLPPEVKHPGDLQRGLKTKTRTPEERPKWPQEQVCNGLEQPRKQQRSDLNGPTDNNNIPETKKVASFPSFVAVPGPCEAEDLIDGIIFAANYLGSTQLLSERNPSKNIRMMQAQEAVSRVKRMQKAAKIKKKANSEGDAQTLTEVDLFISTQRIKVLNADTQETMMDHALRTISYIADIGNIVVLMARRRMPRSASQDCIETTPGAQEGKKQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDIINTQEMYNDDLIHFSNSENCKELQLEKHKGEILGVVVVESGWGSILPTVILANMMNGGPAARSGKLSIGDQIMSINGTSLVGLPLATCQGIIKGLKNQTQVKLNIVSCPPVTTVLIKRPDLKYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATAHEKIVQALSNSVGEIHMKTMPAAMFRLLTGQETPLYI
Protein: Ring finger protein 123 (C9J266)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKWNVTTTNYGKAWAAGDIVSCLIDLDDGTLSFCLNGVSLGTAFENLSRGLGMAYFPAISLSFKESVAFNFGSRPLRYPVAGYRPLQDPPSADLVRAQRLLGCFRAVLSVELDPVEGRLLDKESSKWRLRGQPTVLLTLAHIFHHFAPLLRKVYLVEAVLMSFLLGIVEKGTPTQAQSVVHQVLDLLWLFMEDYEVQDCLKQLMMSLLRLYRFSPIVPDLGLQIHYLRLTIAILRHEKSRKFLLSNVLFDVLRSVVFFYIKSPLRVEEAGLQELIPTTWWPHCSSREGKESTEMKEETAEERLRRRAYERGCQRLRKRIEVVEELQVQILKLLLDNKDDNGGEASRYIFLTKFRKFLQENASGRGNMPMLCPPEYMVCFLHRLISALRYYWDEYKASNPHASFSEEAYIPPQVFYNGKVDYFDLQRLGGLLSHLRKTLKDDLASKANIVIDPLELQSTAMDDLDEDEEPAPAMAQRPMQALAVGGPLPLPRPGWLSSPTLGRANRFLSTAAVSLMTPRRPLSTSEKVKVRTLSVEQRTREDIEGSHWNEGLLLGRPPEEPEQPLTENSLLEVLDGAVMMYNLSVHQQLGKMVGVSDDVNEYAMALRDTEDKLRRCPKRRKDILAELTKSQKVFSEKLDHLSRRLAWVHATVYSQEKMLDIYWLLRVCLRTIEHGDRTGSLFAFMPEFYLSVAINSYSALKNYFGPVHSMEELPGDGTIQAEAEAEKGSLV
Protein: Growth-regulating factor 1 (OsGRF1) (Transcription activator GRF1) (A2XA73)
Organism: Oryza sativa subsp. indica (Rice)
Function: Transcription activator that plays a regulatory role in gibberellin-induced stem elongation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU01002, ECO:0000269|PubMed:10712532}.
Interaction partners:
- SS18 N-terminal domain-containing protein
Sequence:
MMMMSGRPSGGAGGGRYPFTASQWQELEHQALIYKYMASGTPIPSDLILPLRRSFLLDSALATSPSLAFPPQPSLGWGCFGMGFGRKAEDPEPGRCRRTDGKKWRCSKEAYPDSKYCEKHMHRGKNRSRKPVEMSLATPPPPSSSATSAASNSSAGVAPTTTTTSSPAPSYSRPAPHDAAPYQALYGGPYAAATARTPAAAAYHAQVSPFHLHIDTTHPHPPPSYYSMDHKEYAYGHATKEVHGEHAFFSDGTEREHHHAAAGHGQWQFKQLGMEPKQSTTPLFPGAGYGHTAASPYAIDLSKEDDDEKERRQQQQQQQQHCFLLGADLRLEKPAGHDHAAAAQKPLRHFFDEWPHEKNSKGSWMGLEGETQLSMSIPMAANDLPITTTSRYHNDE
Protein: NDUFC2-KCTD14 readthrough (A0A087WY27)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298}; Matrix side {ECO:0000256|ARBA:ARBA00004298}.
Interaction partners:
Sequence:
MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGGDIGLCCLSPGSLSDTPAVFAVGSSAATTH
Protein: Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4) (P49116)
Organism: Homo sapiens (Human)
Function: Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior (By similarity). Activates transcriptional activity of LHCG. Antagonist of PPARA-mediated transactivation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:15302918}.
Interaction partners:
- Juxtaposed with another zinc finger protein 1
- Nuclear receptor corepressor 1
- Nuclear receptor 2C2-associated protein
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Nuclear receptor subfamily 2 group C member 1
- DNA
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- Histone deacetylase 1
- Transcription intermediary factor 1-beta
- TNF receptor-associated factor 6
Sequence:
MTSPSPRIQIISTDSAVASPQRIQIVTDQQTGQKIQIVTAVDASGSPKQQFILTSPDGAGTGKVILASPETSSAKQLIFTTSDNLVPGRIQIVTDSASVERLLGKTDVQRPQVVEYCVVCGDKASGRHYGAVSCEGCKGFFKRSVRKNLTYSCRSNQDCIINKHHRNRCQFCRLKKCLEMGMKMESVQSERKPFDVQREKPSNCAASTEKIYIRKDLRSPLIATPTFVADKDGARQTGLLDPGMLVNIQQPLIREDGTVLLATDSKAETSQGALGTLANVVTSLANLSESLNNGDTSEIQPEDQSASEITRAFDTLAKALNTTDSSSSPSLADGIDTSGGGSIHVISRDQSTPIIEVEGPLLSDTHVTFKLTMPSPMPEYLNVHYICESASRLLFLSMHWARSIPAFQALGQDCNTSLVRACWNELFTLGLAQCAQVMSLSTILAAIVNHLQNSIQEDKLSGDRIKQVMEHIWKLQEFCNSMAKLDIDGYEYAYLKAIVLFSPDHPGLTSTSQIEKFQEKAQMELQDYVQKTYSEDTYRLARILVRLPALRLMSSNITEELFFTGLIGNVSIDSIIPYILKMETAEYNGQITGASL
Protein: Protein RESPONSE TO ABA AND SALT 1 (O04515)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of salt (NaCl) tolerance probably by enhancing abscisic acid (ABA) sensitivity.
Interaction partners:
- EXS
- Zinc finger protein ZAT18
- EXS
- Protein BEARSKIN1
- Protein EARLY-RESPONSIVE TO DEHYDRATION 7
- Late embryogenesis abundant protein 6
- Phosphate transporter PHO1 homolog 7
- Phosphate transporter PHO1 homolog 8
- Phosphate transporter PHO1 homolog 6
- Senescence/dehydration-associated protein At4g35985
Sequence:
MPNTSSSQSFTIFVDGWLIRHRYFVEQLMCASSLDETNRISLEEQQSLVAQFLSHCLQYYQEKFASVSLAGDNVFTFFCPPWFNSYAKLILWVGDFKPSLVFKLTEVSVADLTRHQKDRISSLKSETRRKEREVMRDFALVQQSVADPPVMLAARRVGAVGMVDGEETDLEEAMEVLKAGMAAAMNNADQLRCSTVGKVVEILTPPQAIKVLRTIGQLHLRLRDRDQERA
Protein: Splicing factor 3B subunit 2 (Q3UJB0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13435}. Nucleus speckle {ECO:0000250|UniProtKB:Q13435}.
Interaction partners:
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 5
- Splicing factor 3A subunit 3
- Splicing factor 3B subunit 4
- Splicing factor 3A subunit 1
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 3
- Splicing factor 3A subunit 2
- U5 small nuclear ribonucleoprotein 200 kDa helicase
Sequence:
MAAEHPEPPKGELQLPPPPPPGHYGAWAAQELQARLAEIGAPIQGSREELVERLQTYTRQTGIVLNRPVLRGEDGDKAAPPPMSAQLSGIPMPPPPMGLPPLQPPPPPPPPPPGLGLGFPMAHPPNLGPPPPLRVGEPVALSEEERLKLAQQQAALLMQQEERAKQAAVLMEQERQQEIAKMGTAVPRPPQDMGQLGVRTPLGPRVAAPVGPVVPTPTVLPMGAPVPRPRGPPPPPGDENREMDDPSVGPKIPQALEKILQLKESRQEEMNSQQEEEEMETDTRSSLGQSASETEEDTVSISKKEKNRKRRNRKKKKKPQRVRAASSESSGDREKDSGRSRGSDPPAADVEIEYVTEEPEIYEPNFIFFKRIFEAFKLTDDVKKEKEKEPEKLDKMESSAVPKKKGFEEEHKDSDDDSSDDEQEKKPEAPKLSKKKLRRMNRFTVAELKQLVARPDVVEMHDVTAQDPKLLVHLKATRNSVPVPRHWCFKRKYLQGKRGIEKPPFELPDFIKRTGIQEMREALQEKEEQKTMKSKMREKVRPKMGKIDIDYQKLHDAFFKWQTKPKLTIHGDLYYEGKEFETRLKEKKPGDLSDELRISLGMPVGPNAHKVPPPWLIAMQRYGPPPSYPNLKIPGLNSPIPESCSFGYHAGGWGKPPVDETGKPLYGDVFGTNAAEFQTKTEEEEIDRTPWGELEPSDEESSEEEEEEESDEDKPDETGFITPADSGLITPGGFSSVPAGMETPELIELRKKKIEEAMDGSETPQLFTVLPEKRTATVGGAMMGSTHIYDMSTVMSRKGPAPELQGVEVALAPEELELDPMAMTQKYEEHVREQQAQVEKEDFSDMVAEHAAKQKQKKRKAQPQDSRGGSKKYKEFKF
Protein: Wall associated kinase-like 7 (F4I2T5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSREKFSIYNLLSLLVLLIHGLIAASAQDLTVFSSCQSHCGGIAIPYPFGIGKDCYLNNNEWYEVICNRTSGNPLPVLKSINRELVNISLPDDSSDVFGLTRIKNPVTSLGCSNMEEISLALNVTGSPFFLTGRNTLVAVGCNNNASMTDDKLQIGGCESTCDVGFGQRGRNRSCNGYRCCQAKILSDRLQQIGIKIESLDDEAYSPLNITEPALFYDKGYGTVELGWFIDRLHNMSVVLGFAIQLPRVQAVGVTSEAIEAAGVTVATEAIHISRVDVQILMSVKKPKLKEATIVGKGMIVRISQETLGVNPTKTKD
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Brain cyclic nucleotide-gated channel 2) (BCNG-2) (Hyperpolarization-activated cation channel 1) (HAC-1) (O88703)
Organism: Mus musculus (Mouse)
Function: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:12928435, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- PEX5-related protein
Sequence:
MDARGGGGRPGDSPGTTPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRARLCSRDSACTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPSAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGVPAPSPAASARPASSSTPRLGPAPTARTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL
Protein: Acetyl-coenzyme A thioesterase (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Acyl-coenzyme A thioesterase 12) (Acyl-CoA thioesterase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (rACH) (rCACH-1) (Q99NB7)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes acetyl-CoA.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:11322891}.
Interaction partners:
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase
- Acetyl-CoA acetyltransferase, cytosolic
- Acetyl-CoA acetyltransferase, mitochondrial
- Acylphosphatase
- Acetyl-CoA carboxylase 1
- Aldehyde dehydrogenase family 3 member A2
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MEPTVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIVTIRAKVTRAFSTSMEISIKVRVQDKFTGIQKLLCVAFSTFVVKPLGKEKVHLKPVLLQTEQEQVEHRLASERRKVRLQHENTFSNIMKESNWLRDPVCNEEEGTATTMATSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFNAIVNNTFQNSVEVGVRVEAFDCREWAEGQGRHINSAFLIYNAVDDQEELITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLGTQWDISKKGSISNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKQVGSPARVAYHLLSDFTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSQRKPLKDDNTYIVALMSVVLPSVPPSPQYIRSQVICAGFLIQPVDSSSCTVAYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATHDGLKSVL
Protein: Lividin-2 (Q2UXR3)
Organism: Odorrana livida (Green mountain frog) (Polypedates lividus)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:16713657}.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTISLSLCQEERNADEEDGGEVTEEEVKRSFLDTLKNLAISAAKGAGQSVLSTLSCKLSKTC
Protein: UPF0400 protein C337.03 (O74814)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C4G9.04c
- Rpb7-binding protein seb1
- Decapping nuclease din1
- DNA-directed RNA polymerase II subunit rpb1
- 5'-3' exoribonuclease 2
- Cleavage and termination factor 1
- DNA-directed RNA polymerase II subunit RPB2
- Poly
- Polyadenylate-binding protein 2
- RNA binding exosome specificity factor Mmi1
Sequence:
MALTPDTVSSKLATLNETQESITGIAHWVMFHKRYADEIVQIWLEALYESSSNKKLLLLYLLNEVVQQSRVKKISEYIDAVSPYVVNSVADAYASVPASIKTKIKYVFDVWCQRGIFSKEILLSLQERFNNAENSGHSNYYPVGPPEWAPYTRLMTQTSLYAKSAHSTKTVVDALYKSYLEKQSDYSELLDNYKKQLNKASESCKGNYQACIESRSTLITSLESLIEEQKKLLSEEEESLKSVESIISNLENKESTTATSTLTDAGFGDKSSTAGKHNVETTSPPSSSPNSDDAYSPQVDSYSPSINSVPYTSNIVENPSEDNLSPLPPPASGPYSQEEEETSLFKSQRKEENEEESKELPEDSDIYGKDSSPSSDDSSAAGLYGDS
Protein: Uncharacterized protein, isoform C (E1JHG4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSSSSGKKHKKDKKNRHRSRSSERPRRVTEDEDVTLDLTDDSSSRHRHHKHKKHKEHRHKHHKQKERERANEVISLEESDSDSIPLLMQIVPTAWRCRYRRRCRRRPS
Protein: Transcriptional repressor NrdR (Q9HWX1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Interaction partners:
- Riboflavin biosynthesis protein RibD
- Ribonucleoside-diphosphate reductase
- Class III
- Transcription antitermination protein NusB
- Uncharacterized protein
- Chromosomal replication initiator protein DnaA
- Ribose operon repressor RbsR
- HTH-type transcriptional regulator ArgP
Sequence:
MHCPFCGAHDTKVIDSRLVAEGDQVRRRRECLACGERFTTFETAELVMPRLIKQDGSRQPFDEDKLRAGMQRALEKRPVSVERLEAAIGHIKHQLRATGEREIKSRVLGELVMAELQKLDEVAYIRFASVYRRFQDLNEFREEIERLAREPAKE
Protein: DNA-directed RNA polymerase II subunit RPB9 (RNA polymerase II subunit B9) (B12.6) (DNA-directed RNA polymerase II 14.2 kDa polypeptide) (DNA-directed RNA polymerase II subunit 9) (P27999)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template. Involved in the regulation of transcription elongation. Involved in DNA repair of damage in the transcribed strand. Mediates a transcription-coupled repair (TCR) subpathway of nucleotide excision repair (NER).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB11
- Transcription initiation factor IIF subunit alpha
- DNA-directed RNA polymerase II subunit RPB1
- DNA repair and recombination protein RAD26
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- Transcription elongation factor SPT4
- Transcription elongation factor S-II
Sequence:
MTTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSPLVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQFS
Protein: Cytochrome c oxidase subunit 5B, mitochondrial (Cytochrome c oxidase polypeptide Vb) (P00425)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:2986105}; Single-pass membrane protein {ECO:0000250|UniProtKB:P00424}.
Interaction partners:
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MLRTSLTKGARLTGTRFVQTKALSKATLTDLPERWENMPNLEQKEIADNLTERQKLPWKTLNNEEIKAAWYISYGEWGPRRPVHGKGDVAFITKGVFLGLGISFGLFGLVRLLANPETPKTMNREWQLKSDEYLKSKNANPWGGYSQVQSK
Protein: DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.38) (Deoxycytidine deaminase) (Q7YR23)
Organism: Macaca mulatta (Rhesus macaque)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. May inhibit the mobility of LTR retrotransposons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21835787}. Nucleus {ECO:0000250|UniProtKB:Q9HC16}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9HC16}. Note=Mainly cytoplasmic, small amount are found in the nucleus. {ECO:0000250|UniProtKB:Q9HC16}.
Interaction partners:
- Acetyl-CoA acetyltransferase, mitochondrial
- Elongin-B
- Core-binding factor subunit beta
- Uncharacterized protein
- RING-box protein 2
- DNA dC->dU-editing enzyme APOBEC-3G
- Tripartite motif-containing protein 5
- DNA dC->dU-editing enzyme APOBEC-3G
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- Cytochrome c oxidase subunit 5A, mitochondrial
Sequence:
MKPHFRNTVEPMDPRTFVSNFNNRPILSGLNTVWLCCEVKTKDPSGPPLDAKIFQGKVYSKAKYHPEMRFLRWFHKWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPKVTLTIFVARLYYFWKPDYQQALRILCQKRGGPHATMKIMNYNEFQDCWNKFVDGRGKPFKPRNNLPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQHRGFLRNQAPNIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHVSLCIFAARIYDDQGRYQEGLRALHRDGAKIAMMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAILQNQEN
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC 2.4.1.15) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (O59921)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
Interaction partners:
- Trehalose-6-phosphate phosphatase
- Large subunit of trehalose 6-phosphate synthase
- Glycogen [starch] synthase
- Cytosolic neutral trehalase
- glycogenin glucosyltransferase
- 1,3-beta-glucan synthase
- Synthase subunit of trehalose-6-phosphate synthase/phosphatase complex
- Spore development regulator vosA
- Acid trehalase
- Velvet complex subunit B
Sequence:
MPGVEKSSQNESRLLLVSNRLPITIKRSEDGKYDFSMSSGGLVSGLSGLSKTTTFQWYGWPGLEVPEEEIPTLKNRLKEEYNAIPVFIDDELADRHYNGFSNSILWPLFHYHPGEITFDESAWEAYKEANRLFAQAVASQVQDGDLIWVHDYHLMLLPEMLREEIGNTKKNIKIGFFLHTPFPSSEIYRILPVRNELLLGLLHCDLIGFHTYDYTRHFLSACSRLLGLPTTPNGIEFQGKIIACGAFPIGIDPEKFKEGLKKEKVQKRIATLEQKFQGVKLMVGVDRLDYIKGVPQKLHALEVFLSDHPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGKFGTVEFMPIHFLHKSVNFDELIALYAVSDACVVSSTRDGMNLVSYEYIATQEKRHGSLVLSEFAGAAQSLNGSIIVNPWNTEELAAAYHEAVTMSDEQRALNFSKLDKYVNKYTSAFWGQSFVTELTRISEQAAGKLPTKETPVNGETSKLETSSQ
Protein: Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) (Q8PDA8)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Interaction partners:
- Kynureninase
- Tryptophan 2,3-dioxygenase-like protein
- Group 1 truncated hemoglobin
- Thiopurine S-methyltransferase
- site-specific DNA-methyltransferase
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- Hemolysin III
- Hemolysin III
- Tryptophan-rich sensory protein
Sequence:
MPVDKNLRDLEPGIHTDLEGRLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLAHELRAAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVLGPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLYEEFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWREYSLCEDLVDVETQFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLQQALALTFFPELFDVRTSVGVDNRPPQGSADAGKR
Protein: Zinc finger protein 277 (G5E9M4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASKTQGAVARMQEDRDGSCSTVGGVGYGDSKDCILEPLSLPESPGGTTTLEGSPSVPCIFCEEHFPVAEQDKLLKHMIIEHKIVIADVKLVADFQRYILYWRKRFTEQPITDFCSVIRINSTAPFEEQENYFLLCDVLPEDRILREELQKQRLREILEQQQQERNDTNFHGVCMFCNEEFLGNRSVILNHMAREHAFNIGLPDNIVNCNEFLCTLQKKLDNLQCLYCEKTFRDKNTLKDHMRKKQHRKINPKNREYDRFYVINYLVRLSFHNLKFDCSTANKIFLRTN
Protein: Large ribosomal subunit protein uL29B (60S ribosomal protein L35-B) (P0CX85)
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:
Sequence:
MAGVKAYELRTKSKEQLASQLVDLKKELAELKVQKLSRPSLPKIKTVRKSIACVLTVINEQQREAVRQLYKGKKYQPKDLRAKKTRALRRALTKFEASQVTEKQRKKQIAFPQRKYAIKA