wanglab/gogpt-training-data huggingface dataset:
Protein: Probable dimethyl sulfoxide reductase chain YnfF (DMSO reductase) (EC 1.8.99.-) (P77783)
Organism: Escherichia coli (strain K12)
Function: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Probable anaerobic dimethyl sulfoxide reductase chain YnfG
- Anaerobic dimethyl sulfoxide reductase chain YnfH
- Putative dimethyl sulfoxide reductase chain YnfE
- Tat proofreading chaperone DmsD
- Anaerobic dimethyl sulfoxide reductase chain B
- Probable hypoxanthine oxidase XdhD
- Putative oxidoreductase YgfK
- Anaerobic dimethyl sulfoxide reductase chain C
- Thioredoxin reductase
- Sulfate adenylyltransferase subunit 2
Sequence:
MKIHTTEALMKAEISRRSLMKTSALGSLALASSAFTLPFSQMVRAAEAPVEEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLAKIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV
Protein: NF-kappa-B essential modulator (IkB kinase-associated protein 1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (NF-kappa-B essential modifier) (A0A087WUW6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
Protein: Multidrug resistance protein MexA (P52477)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: The periplasmic linker component of the MexAB-OprM efflux system that confers multidrug resistance. Also functions as the major efflux pump for n-hexane and p-xylene efflux. Over-expression of the pump increases antibiotic and solvent efflux capacities. Required for assembly of the MexA/MexB/OprM complex. Implicated in the secretion of the siderophore pyoverdine.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10671490}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:10671490}. Note=The membrane anchor is not necessary for antibiotic efflux as the protein is functional when targeted to the periplasm by a foreign signal peptide.
Interaction partners:
- Multidrug resistance protein MexB
- Outer membrane protein OprM
- Efflux pump membrane transporter
- Efflux pump membrane transporter
- Outer membrane protein OprJ
- Efflux pump membrane transporter
- Multidrug efflux outer membrane protein OprN
- Probable Resistance-Nodulation-Cell Division
- Protein CyaE
- Pyoverdine export ATP-binding/permease protein PvdT
Sequence:
MQRTPAMRVLVPALLVAISALSGCGKSEAPPPAQTPEVGIVTLEAQTVTLNTELPGRTNAFRIAEVRPQVNGIILKRLFKEGSDVKAGQQLYQIDPATYEADYQSAQANLASTQEQAQRYKLLVADQAVSKQQYADANAAYLQSKAAVEQARINLRYTKVLSPISGRIGRSAVTEGALVTNGQANAMATVQQLDPIYVDVTQPSTALLRLRRELASGQLERAGDNAAKVSLKLEDGSQYPLEGRLEFSEVSVDEGTGSVTIRAVFPNPNNELLPGMFVHAQLQEGVKQKAILAPQQGVTRDLKGQATALVVNAQNKVELRVIKADRVIGDKWLVTEGLNAGDKIITEGLQFVQPGVEVKTVPAKNVASAQKADAAPAKTDSKG
Protein: C-type lectin domain family 4 member A (C-type lectin superfamily member 6) (Dendritic cell immunoreceptor) (CD antigen CD367) (Q9QZ15)
Organism: Mus musculus (Mouse)
Function: May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation (By similarity). May be involved in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UMR7}; Extracellular side {ECO:0000250|UniProtKB:Q9UMR7}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 11
- C-type lectin domain family 5 member A
- C-type lectin domain family 12 member A
- Lymphocyte antigen 75
Sequence:
MASEITYAEVKFKNESNSLHTYSESPAAPREKPIRDLRKPGSPSLLLTSLMLLLLLLAITFLVAFIIYFQKYSQLLEEKKAAKNIMHNELNCTKSVSPMEDKVWSCCPKDWRLFGSHCYLVPTVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDTGHRQWQWVDQTPYEESITFWHNGEPSSGNEKCATIIYRWKTGWGWNDISCSLKQKSVCQMKKINL
Protein: Tripartite motif-containing protein 46 (A0A0G2JXN2)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-associated protein that is involved in the formation of parallel microtubule bundles linked by cross-bridges in the proximal axon. Required for the uniform orientation and maintenance of the parallel microtubule fascicles, which are important for efficient cargo delivery and trafficking in axons. Thereby also required for proper axon specification, the establishment of neuronal polarity and proper neuronal migration.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:26671463}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26671463}. Note=Microtubule-associated. Localizes to the proximal part of the axon. {ECO:0000269|PubMed:26671463}.
Interaction partners:
- Calmodulin-regulated spectrin-associated protein 2
Sequence:
MAEGEDMQTFTSIMDALVRISTSMKNMEKELLCPVCQEMYKQPLVLPCTHNVCQACAREVLGQQGYIGHGGDPSSEPTSPASTPSTRSPRLSRRTLPKPDRLDRLLKSGFGTYPGRKRGALHPQTILFPCPACQGDVELGERGLSGLFRNLTLERVVERYRQSVSVGGAILCQLCKPPPLEATKGCSECRATFCNECFKLFHPWGTQKAQHEPTLPTLSFRPKGLMCPDHKEEVTHYCKTCQRLVCQLCRVRRTHSGHKITPVLSAYQALKDKLTKSLAYILGNQDTVQTQICELEETIRHTEVSGQQAKEEVSQLVRGLGAVLEEKRSSLLQAIEECQQERLSRLSAQIHEHQSLLDGSGLVGYAQEVLKETDQPCFVQAAKQLHNRIARATEALQTFRPAASSSFRHCQLDVGREMKLLTELNFLRVPEAPVIDTQRTFAYDQIFLCWRLPPHSPPAWHYTVEFRRTDVPAQPGPTRWQRREEVRGTSALLENPDTGSVYVLRVRGCNKAGYGEYSEDVHLHTPPAPVLHFFLDGRWGASRERLAISKDQRAVRSIPGLPLLLAAERLLTGCHLSVDVVLGDVAVTQGRSYWACAVDPASYLVKVGVGLESKLQESFQGAPDVISPRYDPDSGHDSGAEDAAVEALPPFAFLTIGMGKILLGSGASSNAGLTGRDGPAASCTVPLPPRLGICLDYERGRVSFLDAVSFRGLLECPLDCSGPVCPAFCFIGGGAVQLQEPVGTKPERKVTIGGFAKLD
Protein: phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC 3.1.3.95) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (D3ZW40)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3
- Phosphatidylinositol-3-phosphatase SAC1
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- FIG4 phosphoinositide 5-phosphatase.
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate-4-phosphatase type I A
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Type II inositol 3,4-bisphosphate 4-phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Inositol polyphosphate-5-phosphatase F
Sequence:
MGEEGPPSLEYIQAKDLFPPKELVKEEENLQVPFTVLQGEGVEFLGRAADALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFSTFKQCQEWLSRLSRATARPAKPEDLFAFAYHAWCLGLTEEDQHTHLCQPGEHIRCRQEAELARMGFDLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIAKACALDPGTRASGGSLSAGTNDASEACDTDFDSSLTACSGVESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVVFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVKLVQHTYSCLYGTFLANNPCEREKRNIYKRTCSVWALLRAGNKNFHNFLYTPGSDMVLHPVCHVRALHLWTAVYLPASSPCTLGEENMDLYLSPVAQSQEFSGRSLDRLPKTRSMDDLLSACDTSSPLTRTSSDPNLNNHCQEVRVSLEPWHSNPEGAEAVIESGVGSPQLTVGDVGLPPPLPSSQKDYLSNKPFKGHKSCSLSYKLLNTSVSWEMKNTSEIKVLEETEALAPGPPAREEQSRTSDGLGKPPEQCPEKEATSSLSNVSSKCGGACDFPGEPPQDSFTGTPQQPHLDSMQAVPIRCTPDHGQGSLCNPPSAASQTLQEPNTDLISQDPPGSMAGISYQEQPSSVSDLIYKKEDAGKRGSKNGQLVENPRFGKMPLELARKPISQSQISEFSFLGSNWDSFQGMMTSFPSGETTPRRLLAYGCCSKRPSNKHIRAAAPCFGGQWAQREGMKSPVCSSHSNGHCTGPGGKNNRMWFSSHPKQVSSTKPSLLSCPSPVPPLYLDDDGLPFPTDVIQHRLRQIEAGYKQEVEQLRRQVRELQMRLDIRHCCAPPAEPPMDYEDDFTCLKESDGSDTEDFGSDHSEDCLSEASWEPVDKKETEVTRWVPDHMASHCYNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHIQVSRARELMSQHLKKPIATASS
Protein: BTB/POZ domain-containing protein 2 (O74778)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- BTB/POZ domain-containing protein 1
- BTB/POZ domain-containing protein 3
- Cullin-3
- RING-box protein pip1
- Elongin-C
Sequence:
MSMNSSTEISQEPSIMKPVSSISSFVFNAGFLQGTFSDTTLIIKGETYHLHALFLGRSPVLLQKLIENNPKGDVHYTIEVETEDPYVTKESCLFVLSTLYCDSPRIPAEVNVCSVLAVSDLLGLDTLAFEASSLIEKSIRPETMESVIRFLDPNFEGLERLKMGMYPRFTSGLFNKAIQVMYNTLVSNWNTEYARLLCNLPFEVIKDLLESDKLTVGASSMARYKLANEIVKMRASFRKQNHIEGKGDESVVLAFDEGSRGIQLVHIAPGAESRRKIWKATSVR
Protein: Vacuolar protein sorting-associated protein 28 homolog (ESCRT-I complex subunit vps28) (O13872)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process.
Subcellular location: Endosome {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein sorting-associated protein 27
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein sorting-associated protein 24
- Vacuolar-sorting protein snf7
- ESCRT-III complex subunit did4
- Vacuolar protein-sorting-associated protein 46
- ER membrane protein complex subunit 4
- Vacuolar-sorting protein dot2
Sequence:
MTEYYDLNLLEKETSEENNFHTKNQQVREDLSILYSILVALEQLEKAFTKDAVSTSDFNSTCELLIQQWESCFSDERVTQAFGSFEDFCSKYRLQCPRAIKRIQEGISDERSQSNSTFSNAISTTAEPSIAMNDTTPQTVNPTKAPSNPSASIAKSIAGLVQNFITTLDAIRLNFIAKDQLHPLLSELIVSMDDLTESLKIQVSCRNKLVQWLIKINNMNITDQLNDVEKRELLYDLEQAYAECYSLL
Protein: AP-1 complex subunit gamma-1 (Adaptor protein complex AP-1 large subunit gamma-1) (Adaptor-related protein complex 1 subunit gamma-1) (Clathrin assembly protein complex 1 gamma-1 large chain) (At-g-Ad) (At-gamma-Ad) (Gamma-adaptin 1) (Q84K16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- AP-1 complex subunit mu-2
- Beta-adaptin-like protein A
- Beta-adaptin-like protein B
- Beta-adaptin-like protein C
- Clathrin heavy chain 2
- AP-1 complex subunit sigma-2
- AP-1 complex subunit sigma-1
- AP-4 complex subunit sigma
- AP-4 complex subunit mu
- AP-1 complex subunit mu-1
Sequence:
MNPFSSGTRLRDMIRAIRACKTAAEERAVVRKECADIRALINEDDPHDRHRNLAKLMFIHMLGYPTHFGQMECLKLIASPGFPEKRIGYLGLMLLLDERQEVLMLVTNSLKQDLNHSNQYVVGLALCALGNICSAEMARDLAPEVERLIQFRDPNIRKKAALCSTRIIRKVPDLAENFVNAAASLLKEKHHGVLITGVQLCYELCTINDEALEYFRTKCTEGLIKTLRDITNSAYQPEYDVAGITDPFLHIRLLRLLRVLGQGDADASDLMTDILAQVATKTESNKNAGNAVLYECVETIMAIEDTNSLRVLAINILGRFLSNRDNNIRYVALNMLMKAITFDDQAVQRHRVTILECVKDPDASIRKRALELVTLLVNENNVTQLTKELIDYLEISDEDFKEDLSAKICFIVEKFSPEKLWYIDQMLKVLCEAGKFVKDDVWHALIVVISNASELHGYTVRALYKSVLTYSEQETLVRVAVWCIGEYGDLLVNNVGMLGIEDPITVTESDAVDVIEDAITRHNSDSTTKAMALVALLKLSSRFPSISERIKDIIVKQKGSLLLEMQQRAIEYNSIVDRHKNIRSSLVDRMPVLDEATFNVRRAGSFPASVSTMAKPSVSLQNGVEKLPVAPLVDLLDLDSDDIMAAPSPSGTDFLQDLLGVDLGSSSAQYGATQAPKAGTDLLLDILSIGTPSPAQNSTSSIGLLSIADVNNNPSIALDTLSSPAPPHVATTSSTGMFDLLDGLSPSPSKEATNGPAYAPIVAYESSSLKIEFTFSKTPGNLQTTNVQATFTNLSPNTFTDFIFQAAVPKFLQLHLDPASSNTLLASGSGAITQNLRVTNSQQGKKSLVMRMRIGYKLNGKDVLEEGQVSNFPRGL
Protein: E3 SUMO-protein ligase PIAS4 (EC 2.3.2.27) (PIASy) (Protein inhibitor of activated STAT protein 4) (Protein inhibitor of activated STAT protein gamma) (PIAS-gamma) (Q8N2W9)
Organism: Homo sapiens (Human)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin.
Subcellular location: Nucleus, PML body {ECO:0000269|PubMed:11248056, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457}. Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. {ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457}.
Interaction partners:
- Small ubiquitin-related modifier 2
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 1
- Serine-protein kinase ATM
- NF-kappa-B essential modulator
- Small ubiquitin-related modifier 4
- Protein kinase C zeta type
- E3 ubiquitin-protein ligase RNF168
- Cellular tumor antigen p53
- Signal transducer and activator of transcription 1-alpha/beta
Sequence:
MAAELVEAKNMVMSFRVSDLQMLLGFVGRSKSGLKHELVTRALQLVQFDCSPELFKKIKELYETRYAKKNSEPAPQPHRPLDPLTMHSTYDRAGAVPRTPLAGPNIDYPVLYGKYLNGLGRLPAKTLKPEVRLVKLPFFNMLDELLKPTELVPQNNEKLQESPCIFALTPRQVELIRNSRELQPGVKAVQVVLRICYSDTSCPQEDQYPPNIAVKVNHSYCSVPGYYPSNKPGVEPKRPCRPINLTHLMYLSSATNRITVTWGNYGKSYSVALYLVRQLTSSELLQRLKTIGVKHPELCKALVKEKLRLDPDSEIATTGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWMCPVCDKPAPYDQLIIDGLLSKILSECEDADEIEYLVDGSWCPIRAEKERSCSPQGAILVLGPSDANGLLPAPSVNGSGALGSTGGGGPVGSMENGKPGADVVDLTLDSSSSSEDEEEEEEEEEDEDEEGPRPKRRCPFQKGLVPAC
Protein: Kinetochore protein Spc25 (Chromosome alignment defect 2) (Mitotic chaos) (Q9V3V7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a component of the essential kinetochore-associated Ndc80 complex, which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17333235, ECO:0000269|PubMed:17895365}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17333235, ECO:0000269|PubMed:17895365}. Note=Independent of microtubules (MTs) and several other known kinetochore components. Ndc80 complex has polar orientation along the spindle axis. {ECO:0000269|PubMed:17333235, ECO:0000269|PubMed:17895365}.
Interaction partners:
- Nuf2
- CG1558-RA protein
- Kinetochore protein NDC80
- Nnf1b
- Nnf1a
- Mis12
- HDC12388
- Spc105-related, isoform B
- Mitotic spindle assembly checkpoint protein MAD2A
- Centromeric protein-C, isoform A
Sequence:
MAIIMTESSYERRVKALYEKQIHMEALEAKFIKKVFKFNSNLLDVKEAASRHQRKVGKLQKVLMERREELDKRVSFIEELDRELEATKLHNLAMKDWFKQQKMLAKQRKNEIMESIHTLSKTTRTYINQEALPARVKGVTVLRGDKRDQLIPFDLKATDVEGLDSLCQHLESLNVDVAQWQQLISLAMDMAMESRAPTTPPKEADNCKSIIEIDLTSPMSHT
Protein: Transcriptional activator protein PfeR (Q04803)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PfeR/PfeS. Activates expression of the ferric enterobactin receptor.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor protein PfeS
- histidine kinase
- Two-component response regulator
- Ferric enterobactin receptor
- histidine kinase
- histidine kinase
- histidine kinase
- Sensor protein
- Sensor protein kinase PmrB
- histidine kinase
Sequence:
MIVQPSAVAKGWPIATTLLPASCGPADPKPEPKPKQRRLCRKVFPLRARCGALAHCPIPGKNEIFTNVNHSHISIPSPRLLLVEDDPRLREDLDAHFRRRGFRVTVCGDGSHGLEAAGREAFDLVLLDIMLPGLDGLALLESLRREQATPVMLMSALGAEQDRISGFTRGADDYLPKPFSLAELDARTDALLRRVRLDRLPLAQRRDTRLVFDDQAQDVLHQGLPAGLTPSEYRLLATLREHAGEALSKPFLYRSVLHRSYTRLDRGLDVHVCNLRRKLAVVAVRHLQIQAVRGQGYLLVETEHP
Protein: Probable RNA exonuclease NGL3 (EC 3.1.-.-) (Q03210)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- RNA exonuclease NGL1
- Protein ECM12
Sequence:
MDSQVEGKISPSQKESSSTSGLVSPSEDGPAHQKIHRDQLSVDQIKKIREERAQKRQVRRNSLISQGKDPDFPTPDLQFIERPFLPINHDNSKGLTPATIQVTQDSLDVKIMTYNTLAQTLIRRDFFPESGPALKWHKRSKVLVHELKKYRPDVVSLQEVDYNELNFWQENFHKLGFDVIFKRHEGKTHGLLVAWNNKKFQLDNDWMLDYDNILAGNVISARTRTKNIALIISLYFKGITDSSSRGIIVANTHLFWHPFGVFERLRQSYLVLQKIQEIKACSKYNGWHSLLMGDFNTEPEEPPYLAITKRPLILKGPIRAMVECSLAYRYSKKRNGEESDQDDEECDEKSRGEGHSDQPQNPKPESFTATKEEKALVNQLVALHNSLHVKGVSLYGIGYGKVHPENANGSHGEPGLSNWANTWCGLLDYIFYIEGDHNQDTRQKEPLNAFEGNNNVKIIGYLRMPCAQEMPKHSQPFEGEYASDHISLMCQIRLFFGGEKVHSLK
Protein: 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (4-hydroxybenzoate hexaprenyltransferase) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) (P32378)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:24406904}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:24406904}.
Interaction partners:
- Hexaprenyl pyrophosphate synthase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Atypical kinase COQ8, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4, mitochondrial
- Flavin prenyltransferase PAD1, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- MIOREX complex component 2
Sequence:
MFIWQRKSILLGRSILGSGRVTVAGIIGSSRKRYTSSSSSSSSPSSKESAPVFTSKELEVARKERLDGLGPFVSRLPKKWIPYAELMRLEKPVGTWLLYLPCSWSILMGAMMQGATLSATAGMLGIFGVGALVMRGAGCTINDFLDRKLDQRVIRSVERPIASGRVSPRRALVFLGAQTLVGMGVLSLLPAQCWWLGLASLPIVFTYPLFKRFTYYPQAALSACFNWGALLGFPAMGVMSWPTMIPLYLSSYLWCMTYDTIYAHQDKKFDIKAGIKSTALAWGPRTKSIMKAMSASQIALLAVAGLNSGLLWGPGFIGGLGVFAYRLFSMIKKVDLDNPKNCWKYFNANINTGLYFTYALAVDYILRLFGFL
Protein: Spermatogenesis-associated protein 31H1 (Q68DN1)
Organism: Homo sapiens (Human)
Interaction partners:
- Zinc finger protein 512
- Coiled-coil domain-containing protein 121
Sequence:
MELTPGAQQQGINYQELTSGWQDVKSMMLVPEPTRKFPSGPLLTSVRFSNLSPESQQQDVKSLEFTVEPKLQSVKHVKLSSVSLQQTIKSVELAPGSLPQRVKYGEQTPRTNYQIMESSELIPRPGHQFAKYAEMIPQPKYQIPKSANLISIPIYHATESSEMAQGLAYKGIDTVEKSVGLTPKLTGRAKESLGMLLQPDLQVPKFVDLTPMVRDQGSKFLGLTPEKSYQILETMELLSQSRPRVKDVGELYMKPLQQTVEYEGITPELKHYFTEAMGLTAEARIQANEFFGMTPKPTSQATGFAERSPRLCPQNLECVEVISEKRLQGEESVVLIPKSLHHVPDSASGMTPGLGHRVPESVELTSKSGVQVEKTLQLTPKPQHHVGSPGIISGLGHQVPESVNLTCKQWLQMEESLEVPLKQTSQVIGHEESVELTSEARQHREVSMGLTKSKNQSMKSPGTTPGPLGRIVEFMRISPEPLDQVTESARTQLQVAQSEEVILIDVPKVVQSVKVTPGPPFQIVKSVTIPRPTPQMVEYIELTPKLQYVRPSEHHTGPCLQDVKSTKLITKPKHQILETVELTGFQIVKTMLIPGPSLQIVKSEELAPGPIPQVVEPIGVALESGIEAINCVDLLPRPHLQELIVPAELTPSPCTQVKSAELTSPQTSPFEEHTILTHKQGLQAVKSTVIKTEPPKVMETEDLNLGHVCQNRDCQKLTSEELQVGTDFSRFLQSSSTTLISSSVRTASELGGLWDSGIQEVSRALDIKNPGTDILQPEETYIDPTMIQSLTFPLALHNQSSDKTANIVENPCPEILGVDVISKETTKRKQMEELENSLQRHLPQSWRSRSRTFQAESGVQKGLIKSFPGRQHNVWESHAWRQRLPRKYLSTMLMLGNILGTTMERKLCSQTSLAERATADTCQSIQNLFGIPAELMEPSQSLPEKGPVTISQPSVVKNYIQRHTFYHGHKKRMALRIWTRGSTSSIIQQYSGTRVRIKKTNSTFNGISQEVIQHMPVSCAGGQLPVLVKSESSLSIFYDREDLVPMEESEDSQSDSQTRISESQHSLKPNYLSQAKTDFSEQFQLLEDLQLKIAAKLLRSQIPPDVPPPLASGLVLKYPICLQCGRCSGLNCHHKLQTTSGPYLLIYPQLHLVRTPEGHGEVRLHLGFRLRIGKRSQISKYRERDRPVIRRSPISPSQRKAKIYTQASKSPTSTIDLQSGPSQSPAPVQVYIRRGQRSRPDLVEKTKTRAPGHYEFTQVHNLPESDSESTQNEKRAKVRTKKTSDSKYPMKRITKRLRKHRKFYTNSRTTIESPSRELAAHLRRKRIGATQTSTASLKRQPKKPSQPKFMQLLFQSLKRAFQTAHRVIASVGRKPVDGTRPDNLWASKNYYPKQNARDYCLPSSIKRDKRSADKLTPAGSTIKQEDILWGGTVQCRSAQQPRRAYSFQPRPLRLPKPTDSQSGIAFQTASVGQPLRTVQKDSSSRSKKNFYRNETSSQESKNLSTPGTRVQARGRILPGSPVKRTWHRHLKDKLTHKEHNHPSFYRERTPRGPSERTRHNPSWRNHRSPSERSQRSSLERRHHSPSQRSHCSPSRKNHSSPSERSWRSPSQRNHCSPPERSCHSLSERGLHSPSQRSHRGPSQRRHHSPSERSHRSPSERSHRSSSERRHRSPSQRSHRGPSERSHCSPSERRHRSPSQRSHRGPSERRHHSPSKRSHRSPARRSHRSPSERSHHSPSERSHHSPSERRHHSPSERSHCSPSERSHCSPSERRHRSPSERRHHSPSEKSHHSPSERSHHSPSERRRHSPLERSRHSLLERSHRSPSERRSHRSFERSHRRISERSHSPSEKSHLSPLERSRCSPSERRGHSSSGKTCHSPSERSHRSPSGMRQGRTSERSHRSSCERTRHSPSEMRPGRPSGRNHCSPSERSRRSPLKEGLKYSFPGERPSHSLSRDFKNQTTLLGTTHKNPKAGQVWRPEATR
Protein: Transcription factor AP-2, isoform C (M9PG57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFLATLDASAWQERLSGHGSLGLSSGSAAYTTHSGGHTGRSGPATGHSGHSSTHGSAATMHHQSLQSDFQPPYFPPPFHHSTQSPPQQQNHGALEYLGTDPYGQPLSSLHHAPLHHYNQLAGLRSTQDQLGIHRTHREAELQGHVTQLSHGFPYTDRRSDYGSAISAGAAHGTRLGHEHESLALHQALQNAVDDVQAPALDDNVAFMSDLPLIKSMKSGKEAGNIGSGSPSEVFCAVPGRLSLLSSTSKYKVTIAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRLLREKLEKIGLNLPAGRRKAANVTLLTSLVEGEATHLAKDFHFVCETEFPARQLAEYIVRHQTEPQDSYRRKELILHSQQITKELMQILSQDRTTHFGTRSQHLLEPSMQRHLTHFSLITHGFGSPAIMAVLHAFQTFLNESLNYLEKLYPSNGGGMVSSSLDKSKIDNEKK