wanglab/gogpt-training-data huggingface dataset:
Protein: PCI domain-containing protein 2 (CSN12-like protein) (Q8BFV2)
Organism: Mus musculus (Mouse)
Function: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (By similarity). Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability (By similarity). Blocks the activity of the SRCAP chromatin remodeling complex by interacting with SRCAP complex member ZNHIT1 and inhibiting its interaction with the complex. This prevents the deposition of histone variant H2AZ1/H2A.Z at the nucleosomes of key lymphoid fate regulator genes which suppresses their expression and restricts lymphoid lineage commitment.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5JVF3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q5JVF3}.
Interaction partners:
- Germinal-center associated nuclear protein
- Transcription and mRNA export factor ENY2
- Centrin-2
- 26S proteasome complex subunit SEM1
- Centrin-3
- Leukocyte receptor cluster member 8 homolog
- SAC3 domain-containing protein 1
- Nuclear pore complex protein Nup153
- Mitotic spindle assembly checkpoint protein MAD1
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MAHITINQYLQQVYEAIDTRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRIFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRITYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRSSQKNKRMILIYLLPVKMLLGHMPTIELLRKYHLMQFSEVTKAVSEGNLLLLNEALAKHETFFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMHVEDVDIDEVQCILANLIYMGHIKGYISHQHQKLVVSKQNPFPPLSTVC
Protein: Probable acyl-CoA dehydrogenase FadE24 (P95187)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable acyl-CoA dehydrogenase FadE23
- Probable fatty oxidation protein FadB
- Electron transfer flavoprotein subunit beta
- Probable pyruvate formate lyase activating protein PflA
- Electron transfer flavoprotein subunit alpha
- Probable NADPH quinone oxidoreductase FadB4
- Possible acyl-CoA dehydrogenase FadE16
- Probable acetyl-CoA acyltransferase FadA2
Sequence:
MTNTTSAANAAKPSGARTDRRGRTTGVGLAPHKRTGIDVALALLTPIVGQEFLDKYRLRDPLNRSLRYGVKTMFATAGAATRQFQRVQGLRGGPTRLKSSGRDYFDLTPDDDQKLIIETVDEFAEEVLRPAAHDADDAATYPSDLTAKAAELGITAINIPEDFDGIAEHRSSVTNVLVAEALAYGDMGLALPILAPGGVASALTHWGSADQQATYLKEFAGENVPQACVAITEPQPLFDPTRLKTTAVRTPSGYRLDGVKSLIPAAADAELFIVGAQLGGKPALFIVESAASGLTVKADPSMGIRGAALGQVELCGVSVPLNARLGEDEASDNDYSEALALARLGWAALAVGTSHAVLDYVVPYVKQRQAFGEPIAHRQAVAFMCANIAIELDGLRLITWRGASRAEQGLPFAREAALAKRLGSDKGMQIGLDGVQLLGGHGYTKEHPVERWYRDLRAIGVAEGVVVI
Protein: Cadm4 protein (Cell adhesion molecule 4) (Q5U3R8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAFSSVWKYWAPLPLLLLLYSHTARGQAVQAENVTVLEGGTAQISCRLQNYDGSIVVIQNPRRQTLFFNGTRALKDDRFQMVLFTPKLVRITLTNVSVSDEGGYFCQLYTDDTHHQVATLSVVVPPEVPSVEVKTEAVEGGEVELTCLSLRSKLPATLRWVRDRREIPGVISQQENGKTVSVSNTIRIPVERKDNGAALSCEASHPALVSQKRVRHYSLDVHFAPTVKIVPPQGILREGDSLSLTCSVTGNPLPRDIQWSRVNDTLPERAEKTGNILHMSRLSQSHNGTYLCQAHNNYGRAADHYTLLVYDPGAVVETHSAVPFAVIGGILALLVFTVICVLIVTIWCSVRQKGSYLTHEASGLDEHGEVQEAFLNGNDASQGKKEYLL
Protein: Probable LRR receptor-like serine/threonine-protein kinase At5g45780 (EC 2.7.11.1) (C0LGU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Receptor-like kinase
Sequence:
MEISLMKFLFLGIWVYYYSVLDSVSAMDSLLSPKGVNYEVAALMSVKNKMKDEKEVLSGWDINSVDPCTWNMVGCSSEGFVVSLEMASKGLSGILSTSIGELTHLHTLLLQNNQLTGPIPSELGQLSELETLDLSGNRFSGEIPASLGFLTHLNYLRLSRNLLSGQVPHLVAGLSGLSFLDLSFNNLSGPTPNISAKDYRIVGNAFLCGPASQELCSDATPVRNATGLSEKDNSKHHSLVLSFAFGIVVAFIISLMFLFFWVLWHRSRLSRSHVQQDYEFEIGHLKRFSFREIQTATSNFSPKNILGQGGFGMVYKGYLPNGTVVAVKRLKDPIYTGEVQFQTEVEMIGLAVHRNLLRLFGFCMTPEERMLVYPYMPNGSVADRLRDNYGEKPSLDWNRRISIALGAARGLVYLHEQCNPKIIHRDVKAANILLDESFEAIVGDFGLAKLLDQRDSHVTTAVRGTIGHIAPEYLSTGQSSEKTDVFGFGVLILELITGHKMIDQGNGQVRKGMILSWVRTLKAEKRFAEMVDRDLKGEFDDLVLEEVVELALLCTQPHPNLRPRMSQVLKVLEGLVEQCEGGYEARAPSVSRNYSNGHEEQSFIIEAIELSGPR
Protein: ATP synthase subunit beta, mitochondrial (EC 7.1.2.2) (Q01859)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit d
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit a, chloroplastic
- ATP synthase subunit a
- F-ATPase gamma subunit
- F-ATPase protein 6
- ATP synthase epsilon chain, chloroplastic
- Os02g0750100 protein
Sequence:
MATRRALSSLVRAASRLRGASPAPRPRGPLHRPSPSGYLFNRAAAYATAAAAKEAAPPAPATGKATGGGKITDEFTGAGAVGQVCQVIGAVVDVRFDEGLPPILTALEVLDHNIRLVLEVAQHLGENMVRTIAMDGTEGLVRGQRVLNTGSPITVPVGRATLGRIMNVIGEPIDEKGDITTNHFLPIHREAPAFVEQATEQQILVTGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGDKQSESKCALVYGQMNEPPGARARVGLTGLTVAEHFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHVLGEDHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEVFTGAPGKYVELKESVNSFQGVLDGKYDDLPEQSFYMVGGIEEVIAKAEKIAKESAS
Protein: Bacterial microcompartment shell protein EutK (Ethanolamine utilization protein EutK) (Q9ZFU8)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC. Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:27063436}.
Interaction partners:
- Bacterial microcompartment shell vertex protein EutN
- Bacterial microcompartment shell protein EutL
- Bacterial microcompartment shell protein EutS
- Ethanolamine ammonia-lyase reactivase EutA
- Acetaldehyde dehydrogenase
- Ethanolamine utilization protein EutJ
- Ethanolamine ammonia-lyase small subunit
- Probable ethanolamine permease EutH
- HTH-type DNA-binding transcriptional activator EutR
- Acetate kinase EutQ
Sequence:
MINALGLLEVDGMVAAVDAADAMLKAANVRLLSHQVLDPGRLTLVVEGDLAACRAALDAGSAAAQRTGRVISRKEIGRPEEDTQWLIGGFARATTPTEKAPQVPATPEFAEALLALLASVRQGMTAGEVAAHFGWPLEQARNVLEQLFSDGALRKRSSRYRIKN
Protein: N-acetylmuramate alpha-1-phosphate uridylyltransferase (MurNAc-1P uridylyltransferase) (MurNAc-alpha-1P uridylyltransferase) (EC 2.7.7.99) (Q88QT2)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P. Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc. Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc. Is not able to use GlcNAc-alpha-1P and GalNAc-alpha-1P as substrates. Cannot accept other nucleotide triphosphates (ATP, CTP, TTP, or GTP) than UTP.
Interaction partners:
- N-acetylmuramate/N-acetylglucosamine kinase
- UDP-N-acetylenolpyruvoylglucosamine reductase
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Selenocysteyl-tRNA-specific translation elongation factor
- Histidinol-phosphatase
- N-acetylmuramic acid 6-phosphate phosphatase
- Hydrolase, haloacid dehalogenase-like family
- dTDP-glucose 4,6-dehydratase
- DnaJ-like protein DjlA
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Sequence:
MKAMILAAGKGERMRPLTLHTPKPLVPVAGQPLIEYHLRALAAAGVTEVVINHAWLGQQIEDHLGDGSRFGLSIRYSPEGEPLETGGGIFKALPLLGDAPFLLVNGDVWTDYDFARLQAPLQGLAHLVLVDNPGHHGRGDFRLVGEQVVDGDDAPGTLTFSGISVLHPALFEGCQAGAFKLAPLLRQAMAAGKVSGEHYRGHWVDVGTLERLAEAESLIGERA
Protein: Nuclear factor 1 C-type (NF1-C) (Nuclear factor 1/C) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/C) (NF-I/C) (NFI-C) (TGGCA-binding protein) (P70255)
Organism: Mus musculus (Mouse)
Function: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
Subcellular location: Nucleus.
Interaction partners:
- Neurofibromin
Sequence:
MYSSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKAEVKQKWASRLLAKLRKDIRPECREDFVLAVTGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAACAHPVLCVQPHHIGVAVKELDLYLAYFVRERDAEQSSSPRTGVGSDQEDSKPITLDTTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPASAGMRRTLPSTSSSGSKRHKSGSMEEDVDTSPGGDYYTSPNSPTSSSRNWTEDIEGGISSPVKKTEMDKSPFNSPSPQDSPRLSSFTQHHRPVIAVHSGIARSPHPTSALHFPATPILPQTASTYFPHTAIRYPPHLNPQDPLKDLVSLACDPATQQPGPPALRPTRPLQTVPLWD
Protein: Heme-binding protein 1 (p22HBP) (Q9R257)
Organism: Mus musculus (Mouse)
Function: May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12413491, ECO:0000269|PubMed:9813049}.
Interaction partners:
- Formyl peptide receptor-related sequence 1
- Formyl peptide receptor-related sequence 7
- Formyl peptide receptor 2
- Formyl peptide receptor-related sequence 6
- Formyl peptide receptor-related sequence 4
- Formyl peptide receptor-related sequence 3
Sequence:
MLGMIRNSLFGSVETWPWQVLSTGGKEDVSYEERACEGGKFATVEVTDKPVDEALREAMPKIMKYVGGTNDKGVGMGMTVPVSFALFPNEDGSLQKKLKVWFRIPNQFQGSPPAPSDESVKIEEREGITVYSTQFGGYAKEADYVAHATQLRTTLEGTPATYQGDVYYCAGYDPPMKPYGRRNEVWLVKA
Protein: Protein btn1 (Q9US09)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in vacuolar transport and vacuole pH homeostasis. Also required for cytokinesis.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Interaction partners:
- Nucleoporin nup124
Sequence:
MIKLRLTKDAKVGCCFLIFGLLNNLLYVIILSAALDLVGANVSKGVVLLSNIVPSLACKLSASILHVHKFKFAKRIGFCVFMSILGMQWIAWSSSVPSKMLGVSLAAISSSFGEISFLHLSSRYHSVSLPCWSSGTGLAGLFGASSYLVMTTWFNFSVRSTLIISSFLPLFLLIMYFFVLPESESTSPSINNNYTPIESIDLRAGHVSFNFVNSLKQTFIFMQPYLLSHMFPQFLVYFSEYTINIGVAPTLLFPPEKAGFSSFRDFYPTYQTVYQIGVFLSRSSISFFTVPYLRTLAITQFIILLFTILQSALYLTSSYHFVLFLIFVEGLIGGTVYVNVYHSLQTTESSQRELAISTVGSSDSSGIFLASLVSLFLEPSLCHFQADRGRDWCALT
Protein: Synaptotagmin-4 (Synaptotagmin IV) (SytIV) (P50232)
Organism: Rattus norvegicus (Rat)
Function: Synaptotagmin family member which does not bind Ca(2+). Involved in neuronal dense core vesicles (DCVs) mobility through its interaction with KIF1A. Upon increased neuronal activity, phosphorylation by MAPK8/JNK1 destabilizes the interaction with KIF1A and captures DCVs to synapses. Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000269|PubMed:29166604, ECO:0000305|PubMed:30021165}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Otoferlin
- Synaptotagmin-1
- Multifunctional fusion protein
- Vesicle-associated membrane protein 2
- Syntaxin-6
Sequence:
MAPITTSRVEFDEIPTVVGIFSAFGLVFTVSLFAWICCQRRSAKSNKTPPYKFVHVLKGVDIYPENLSSKKKFGGDDKSEAKRKAALPNLSLHLDLEKRDLNGNFPKTNPKAGSSSDLENVTPKLFPETEKEAVSPESLKSSTSLTSEEKQEKLGTLFLSLEYNFEKKAFVVNIKEAQGLPAMDEQSMTSDPYIKMTILPEKKHKVKTRVLRKTLDPVFDETFTFYGVPYPHIQELSLHFTVLSFDRFSRDDVIGEVLVPLSGIELSDGKMLMTREIIKRNAKKSSGRGELLVSLCYQSTTNTLTVVVLKARHLPKSDVSGLSDPYVKVNLYHAKKRISKKKTHVKKCTPNAVFNELFVFDIPCESLEEISVEFLVLDSERGSRNEVIGRLVLGATAEGSGGGHWKEICDFPRRQIAKWHMLCDG
Protein: Defective proventriculus, isoform A (IP14647p) (Q9W268)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- AT-rich binding protein
- Ubiquitin-like protein 5
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MDFQSAMETFAEAWVAANAGQQSQALALTRAVNAAAVVASANAKSPNASSSASASLADLAVKKEHSISPPHSVVSVGVGVAGEDQHRRSSLQGVQEKLTQLQMQQQHHQQQQQQQQQQQQQHQQQQQHHHHQQQAQQAGAGVGSGELAGRRSSEGTPPTAHPPTNSEGQALSSSTASSSQNATPKSDRERERERERDREERVERGSISCLPPAALGMAVGVQQAQHQEKLLSHPALDSRREFDVSKVNPKSLPLHCVVESVHSLHASLTIDTRQPWKRRPNIETDSYVIIAAATPWSEIVQTALQRLGYSQEVANTARGSLIIKHWKPIPLEQISDNPAVPVSDIVGELTSVITLRIVILRPKTSPFGEIKDKLLKLLVLQSHAVLRSTGCPLDEVTLSQICRSSHQNTYALPGGEISDELRRKFDQWWSNQLSPQATAMTPKMLPFMTGPSAVPVPVAVPGEMDFPVGTAMAAAAAAAAHAAAAGGAAGGNPLGSMGSRESLLLANEAAHHAGAGQAPGPGHHGSMLVHPMHASMHHHHHHGGGGGHGPPYPNQKTRMRTSFDPEMELPKLQKWFADNPHPSRQQIQTYVVQLNALESRRGRKPLDVNNVVYWFKNARAAQKRAEMRGGSLGSAISALGHAAMNGYLSQHAPLGQNSSSSAGSQPMSMGNLSMSHDYLKSPLSLKSEDIDTMSQHSDDMDEEQSRPNTPQLPLSLTTHERHRSSPLMDEDEDEAGEQQQPQEAKSDGMNGSVKDEERQEKSRDELQDNEKENSNGEDRHLDADAQMEASSNLNNNHNNSSLHIEQEVGSTPKRSTPKEEDDDLDMDEDEEDNENDASHLDEFRSPSPDLAGGVVPHKDQLPFPMVPNSMFSQSFMYMSHYIPAFGQAAAGHPHHHAAAAAAAAGIQPNALMGGGGLNLSSISNEERRKRNRTFIDPVTEVPKLEQWFAMNTHPSHNLILKYTEDLNTMPYRQKFPRLESKNVQFWFKNRRAKCKRLKMSLYDSNQCAQLGGLGSFVPKYEERD
Protein: Serine/threonine-protein kinase H1 (EC 2.7.11.1) (Protein serine kinase H1) (PSK-H1) (P11801)
Organism: Homo sapiens (Human)
Function: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:11087665, ECO:0000269|PubMed:14644153}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11087665}. Nucleus speckle {ECO:0000269|PubMed:11087665}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14644153}; Lipid-anchor. Cell membrane {ECO:0000269|PubMed:14644153}; Lipid-anchor {ECO:0000269|PubMed:14644153}. Cytoplasm {ECO:0000269|PubMed:11087665, ECO:0000269|PubMed:14644153}. Note=Localized in the brefeldin A-sensitive Golgi compartment, at centrosomes, in the nucleus with a somewhat speckle-like presence, membrane-associated to the endoplasmic reticulum (ER) and the plasma membrane (PM), and more diffusely in the cytoplasm (PubMed:11087665, PubMed:14644153). Found to concentrate in splicing factor compartments (SFCs) within the nucleus of interphase cells (PubMed:11087665). The acylation-negative form may be only cytoplasmic and nuclear. Acylation seems to allow the sequestering to the intracellular membranes. Myristoylation may mediate targeting to the intracellular non-Golgi membranes and palmitoylation may mediate the targeting to the Golgi membranes. Dual acylation is required to stabilize the interaction with Golgi membranes. {ECO:0000269|PubMed:11087665, ECO:0000269|PubMed:14644153}.
Interaction partners:
- Neuronal migration protein doublecortin
- Solute carrier family 12 member 4
- Phosphatidylcholine-sterol acyltransferase
- Proteasome subunit beta type-10
- Solute carrier family 12 member 2
- E3 ubiquitin-protein ligase TM129
Sequence:
MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKSDVYKHFITEVDSVGPVKAGFPAASQYAHPCPGPPTAGHTEPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYSGEPWPSVSNLAKDFIDRLLTVDPGARMTALQALRHPWVVSMAASSSMKNLHRSISQNLLKRASSRCQSTKSAQSTRSSRSTRSNKSRRVRERELRELNLRYQQQYNG
Protein: Inhibitory POU protein (I-POU) (Abnormal chemosensory jump 6 protein) (P24350)
Organism: Drosophila melanogaster (Fruit fly)
Function: Modulates gene transcription; simultaneously generates both a specific activator and an inhibitor of gene transcription, capable of modulating two distinct regulatory programs during neural development. Has a role in olfactory behavior.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein onecut
- Protein atonal
- POU domain protein CF1A
- DLim1
- P53, isoform B
Sequence:
MTMSMYSTTDKMKMSAPSCFPGRYSPSYRSSEQMRRCMPNPSIHISSSCDSLESRLLEDASLLCNSWSARQNGDIFAGINDGILSRAEALAAVDIQKHQAQHVHSQMPSQIKHDVMYHHHSMSGPPQRPLQENPFSRQMHHSMDQLDMLDPTGSMTTLAPISESPLTPTHQHLHGSYHSMNHMMSHHHPGTLSGHTGGHHGHSAVHHPVITAAVAAAGLHPDTDTDPRELEAFAERFKQRRIKLGVTQADVGKALANLKLPGVGALSQSTICRFESLTLSHNNMIALKPILQAWLEEAEAQAKNKRRDPDAPSVLPAGEKKRKRTSIAAPEKRSLEAYFAVQPRPSGEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRIVSSVTPSMTGHGSAGFGY
Protein: Uncharacterized protein C19orf18 (Q8NEA5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDKVQSGFLILFLFLMECQLHLCLPYADGLHPTGNITGLPGSKRSQPPRNITKEPKVFFHKTQLPGIQGAASRSTAASPTNPMKFLRNKAIIRHRPALVKVILISSVAFSIALICGMAISYMIYRLAQAEERQQLESLYKNLRIPLLGDEEEGSEDEGESTHLLPENENELEKFIHSVIISKRSKNIKKKLKEEQNSVTENKTKNASHNGKMEDL
Protein: Transaldolase (EC 2.2.1.2) (K0BE10)
Organism: Escherichia coli O104:H4 (strain 2009EL-2071)
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0A870}.
Interaction partners:
Sequence:
MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPTLLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL
Protein: ATP synthase F(1) complex subunit epsilon, mitochondrial (ATPase subunit epsilon) (ATP synthase F1 subunit epsilon) (P05632)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
Sequence:
MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE
Protein: Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Germ cell tumor 1) (Protein asunder homolog) (Sarcoma antigen NY-SAR-95) (Q9NVM9)
Organism: Homo sapiens (Human)
Function: Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis. Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing.
Subcellular location: Nucleus {ECO:0000269|PubMed:23904267, ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000269|PubMed:23097494, ECO:0000269|PubMed:23904267}. Note=Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000269|PubMed:17974005}.
Interaction partners:
- Integrator complex subunit 5
- Integrator complex subunit 1
- Integrator complex subunit 14
- Integrator complex subunit 6
- Integrator complex subunit 3
- Integrator complex subunit 10
- Integrator complex subunit 7
- Integrator complex subunit 11
- Integrator complex subunit 4
- Integrator complex subunit 2
Sequence:
MKIFSESHKTVFVVDHCPYMAESCRQHVEFDMLVKNRTQGIIPLAPISKSLWTCSVESSMEYCRIMYDIFPFKKLVNFIVSDSGAHVLNSWTQEDQNLQELMAALAAVGPPNPRADPECCSILHGLVAAVETLCKITEYQHEARTLLMENAERVGNRGRIICITNAKSDSHVRMLEDCVQETIHEHNKLAANSDHLMQIQKCELVLIHTYPVGEDSLVSDRSKKELSPVLTSEVHSVRAGRHLATKLNILVQQHFDLASTTITNIPMKEEQHANTSANYDVELLHHKDAHVDFLKSGDSHLGGGSREGSFKETITLKWCTPRTNNIELHYCTGAYRISPVDVNSRPSSCLTNFLLNGRSVLLEQPRKSGSKVISHMLSSHGGEIFLHVLSSSRSILEDPPSISEGCGGRVTDYRITDFGEFMRENRLTPFLDPRYKIDGSLEVPLERAKDQLEKHTRYWPMIISQTTIFNMQAVVPLASVIVKESLTEEDVLNCQKTIYNLVDMERKNDPLPISTVGTRGKGPKRDEQYRIMWNELETLVRAHINNSEKHQRVLECLMACRSKPPEEEERKKRGRKREDKEDKSEKAVKDYEQEKSWQDSERLKGILERGKEELAEAEIIKDSPDSPEPPNKKPLVEMDETPQVEKSKGPVSLLSLWSNRINTANSRKHQEFAGRLNSVNNRAELYQHLKEENGMETTENGKASRQ
Protein: 3'-5' exonuclease crn-4 (EC 3.1.-.-) (Cell death-related nuclease 4) (Q10905)
Organism: Caenorhabditis elegans
Function: Involved in the degradation of chromosomal DNA. Contributes to cell killing.
Interaction partners:
- Exosome complex component RRP46 homolog
- Flap endonuclease 1
- Exosome complex component 10 homolog
- Endonuclease G, mitochondrial
- Probable oligoribonuclease
- Cell death-related nuclease 6
- Histone RNA hairpin-binding protein
- DNA polymerase delta catalytic subunit
- Bestrophin homolog
- Deoxyribonuclease TATDN1
Sequence:
MAYQHCPFDTLLILDFETTSDAANQDYPCEVIQFAIVAYDVPNDKIREDISFNKYVKPVLNRTLTKNCVDFTGIPQRSIDTADTFDVVYEQFQQWLITLGLEEGKFAFVCDSRQDLWRIAQYQMKLSNIQMPAFFRQYINLYKIFTNEMDRMGPKELSATTNIGKMNEYYDLPTIGRAHDAMDDCLNIATILQRMINMGAKVTVNELLTCCASWRRQPLVYNKEWRSSFMDAGKIFERVLPLVVTTIRAGDFRLEMYGVCRYCRKGMDVCGTSHQQTPHDLYKNEEDPIHFAKIAGYY
Protein: SH3 domain-binding glutamic acid-rich-like protein 3 (SH3 domain-binding protein 1) (SH3BP-1) (TNF inhibitory protein B1) (TIP-B1) (Q9H299)
Organism: Homo sapiens (Human)
Function: Could act as a modulator of glutaredoxin biological activity (Probable). May play a role in cytoskeleton organization.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10554026, ECO:0000269|PubMed:11137621, ECO:0000269|PubMed:11344125, ECO:0000269|PubMed:15907482}. Cell projection, ruffle membrane {ECO:0000269|PubMed:34380438, ECO:0000305|PubMed:11344125}. Nucleus {ECO:0000269|PubMed:11444877}.
Interaction partners:
- Profilin-1
Sequence:
MSGLRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRALAGNPKATPPQIVNGDQYCGDYELFVEAVEQNTLQEFLKLA