wanglab/gogpt-training-data huggingface dataset:
Protein: SOS Ras/Rac guanine nucleotide exchange factor 1 (G1TRT1)
Organism: Oryctolagus cuniculus (Rabbit)
Interaction partners:
- SHC-transforming protein 1
- Receptor protein-tyrosine kinase
- Growth factor receptor bound protein 2
- Tyrosine-protein phosphatase non-receptor type
- Abl interactor 1
- small monomeric GTPase
- small monomeric GTPase
- GRB2 associated binding protein 1
- Epidermal growth factor receptor kinase substrate 8
- Fibroblast growth factor receptor
Sequence:
VQGQVHPTLESNDDALQYVEELILQLLNMLCQAQPRSASDVEERVQKSFPHPIDKWAIADAQSAIEKRKRRNPLSLPVEKIHPLLKEVLGYKIDHQVSVYIVAVLEYISADILKLVGNYVRNIRHYEITKQDIKVAMCADKVLMDMFHQDVEDINILSLTDEEPSTSGEQTYYDLVKAFMAEIRQYIRELNLIIKVFREPFVSNSKLFSANDVENIFSRIVDIHELSVKLLGHIEDTVEMTDEGSPHPLVGSCFEDLAEELAFDPYESYARDILRPGFHDRFLSQLSKPGAALYLQSIGEGFKEAVQYVLPRLLLAPVYHCLHYFELLKQLEEKSEDQEDKECLKQAITALLNVQSGMEKICSKSLAKRRLSESACRFYSQQMKGKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASNAEYRLKEKFFMRKVQINDKDDTSEYKHAFEIILKDENSVIFSAKSAEEKNNWMAALISLQYRSTLERMLDVTMLQEEKEEQMRLPSADVYRFAEPDSEENILFEENVQPKAGIPIIKAGTVIKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERFEIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLNVCRHWVEHHFYDFERDADLLQRMEEFIGTVRGKAMKKWVESITKIIQRKKIARDNGPGHNITFQSSPPAVEWHISRPGHIETFDLLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNILKTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQNQPYCLRVESDIKRFFENLNPMGNSMEKEFTDYLFHKSLEIEPRNPKPLPRFPKKYSYPLKSPGVRPSNPRPGTMRHPTPLQQEPRKISYSRIPESETESTASAPNSPRTPLTPPPASGASSTTDVCSVFDSDHSSPFHSSSDTVFIQVTLPHGPRSASVSSISLTKGTDEVPVPPPVPPRRRPESAPAESSPSKIMSKHLDSPPAIPPRQPTSKAYSPRYSISDRTSVSDPPESPPLLPPREPVRTPDVFSSSPLHLQPPPLGKKSDHGNAFFPNSPSPFTPLPPQTPSPHGTRRHLPSPPLTQEVDLHSIAGPPVPPRQSTSQHIPKLPPKTYKREHTHPSMHRDGPPLLENAHSS
Protein: Germ cell nuclear acidic peptidase, isoform B (Q9W554)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ovarian-specific serine/threonine-protein kinase Lok
- Exonuclease 1
- MIP26334p
- Enhanced level of genomic instability 1
- Serine/threonine-protein kinase greatwall
- Origin recognition complex subunit 1
- yemanuclein
Sequence:
MADHKYRLFNAVDPSKVKVPFNQKFANLTLSSHKKRLQVSHAPKDHPEKRNDQKTRKLPAAPMRANVGAPAPSCGANTEDTELDNSDYMEALQLSADGCSQDVANVGDVELLSAGISNLKVQPINEEHSAKPEISICISSTTEENVSGDDDAASCITISDSSEDEQEPLPPDSMAVSEREIVANPGQEDIPQPMLTTEKVQRIEAFLRDVSIERREMEWNGPLTPPPLSSSQRQSRLADADTESMSPTDEDWQPPTTRPIYNSTQLANNDTQVNTICSADATRLDSSKRLADDETEANTLGSEELEPTYSSKRLADNDTEPNTLCSDSSETHNSTIHNNEPVPDESIEIPETSSEGELTPQKASSGSSTSGGDEHGSIQVSSINISAKINIKISIPTMESSSAEDDDEHYSSPRATKSLPSSEEVQHQEHQQQDPQSHQKSMLSVDDASEDEQFLTHAEKLLNQLYGKSWQTPDVIRTLKRSSGSGGKQAPLRPRNIQATAVTTAKKKKPKPDESVLGDFSIFTKPLRTNQTPLNSTRLPPMRAVQTERRPRTQKPLTRPRTNHIDEDRWRKLIDSDSGTDASDDEDADATFSESGSDSDSDKDKENKQKRGDLTYLDLSKDEVEVISNPDQDSPSPKCHRRLDDILRSCRASVKAKLPATPVQQPNIRRQLFTPNAGFENDNQAKEIVNRALDLDMLDELESDYLPGTPVHRRVQEVKKKLGIGQQGQTTPHESPILKLLTPKTAPPKGTAPPKTSAPPKVSTPPKSTKQIPKPRKQKDLSPVASGGKCGFLKSLEGQVSRDRADNEAFFYRENFARNKDQLAQHLYKMYNAQVFNNELDVPITWSKLLRNTAGRCMNKRKLNQRSSVVELSVKVLTTADRLRCTLIHELCHAAAWVFNGEGGHGRVWKMWAQRANDKFPDLPQIKVCHNYSIEFKYTYKCLSCDKASHAHSRSRKVEDLRCRICRGPITLFLNKKDKQGNTVSTPAGEAKGFAKFVKDNFQRHKRDNMTAAQVMRILSVEYAKQKGQPAEETAASIASRVETLTLDESSN
Protein: EG:4F1.1 protein (Gamma/delta-sarcoglycan-like protein SCG-GAMMA/DELTA) (MIP05534p) (Sarcoglycan delta, isoform A) (Sarcoglycan delta, isoform C) (Sarcoglycan delta, isoform D) (Sarcoglycan delta, isoform E) (O76892)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004274}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004274}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Sarcoglycan alpha, isoform C
- FI16515p1
- Dystrobrevin, isoform F
- IP02644p
- Dystroglycan 1
- MADF domain-containing protein
- trypsin
- Dystrophin, isoforms A/C/F/G/H
- LP03706p
- H/ACA ribonucleoprotein complex non-core subunit NAF1
Sequence:
MLAAGSSEITDFGPHSRQLTAGNTPKRPNKASSHRPGSGSGPGPMTTGGTSSASGNGNSGGALNAIPTTKVGSGGGGGGAMSATTVTATTGKATVSHGHSHGHALGRSETRSGRSAAAGRSNVDGFVGGIETYLGLIGWRKKCLYTLLLLLMLLIITNLVLTLWILKVMEFSTEGMGQLKIVPGGIQLSGQAIIMDMLRASTIRSRHGQPISIESSRNFSINTRDPNGMIENHLFLGHDKFECLSAGFRINDTNGRSLFSVNRDEVTIGAHALRIDGEGGAVFRESVQTPHVRAEPGRELRLESPTRQLEMTAAKDINLQSRAGGIEVVALEDVKFRALDGSLRLESSKILMPNLRTAQPPILGTAQSRDHMHRVFQLCACSNGKLFLAAPHSICAGDDSTVCR
Protein: dolichol kinase (EC 2.7.1.108) (A0A0S2Z5Y1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MTRECPSPAPGPGAPLSGSVLASIFGSTMGEIRWPGTKKTFEGTMTSIFAQIISVALILIFDSGVDLNYSYAWILGSISTVSLLEAYTTQIDNLLLPLYLLILLMA
Protein: Zinc finger protein GIS2 (P53849)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May act in the sexual differentiation pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Elongation factor 3A
- Single-stranded nucleic acid-binding protein
- rRNA-processing protein EFG1
- Restriction of telomere capping protein 4
- Polyadenylate-binding protein, cytoplasmic and nuclear
- UBP3-associated protein BRE5
- KRR1 small subunit processome component
- Small ribosomal subunit protein eS1A
- RNA-binding protein SRO9
- Ribosome biogenesis protein BRX1
Sequence:
MSQKACYVCGKIGHLAEDCDSERLCYNCNKPGHVQTDCTMPRTVEFKQCYNCGETGHVRSECTVQRCFNCNQTGHISRECPEPKKTSRFSKVSCYKCGGPNHMAKDCMKEDGISGLKCYTCGQAGHMSRDCQNDRLCYNCNETGHISKDCPKA
Protein: Pleckstrin homology domain-containing family O member 2 (PH domain-containing family O member 2) (Pleckstrin homology domain-containing family Q member 1) (PH domain-containing family Q member 1) (Q8TD55)
Organism: Homo sapiens (Human)
Interaction partners:
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
Sequence:
MEEEGVKEAGEKPRGAQMVDKAGWIKKSSGGLLGFWKDRYLLLCQAQLLVYENEDDQKCVETVELGSYEKCQDLRALLKRKHRFILLRSPGNKVSDIKFQAPTGEEKESWIKALNEGINRGKNKAFDEVKVDKSCALEHVTRDRVRGGQRRRPPTRVHLKEVASAASDGLLRLDLDVPDSGPPVFAPSNHVSEAQPRETPRPLMPPTKPFLAPETTSPGDRVETPVGERAPTPVSASSEVSPESQEDSETPAEEDSGSEQPPNSVLPDKLKVSWENPSPQEAPAAESAEPSQAPCSETSEAAPREGGKPPTPPPKILSEKLKASMGEMQASGPPAPGTVQVSVNGMDDSPEPAKPSQAEGTPGTPPKDATTSTALPPWDLPPQFHPRCSSLGDLLGEGPRHPLQPRERLYRAQLEVKVASEQTEKLLNKVLGSEPAPVSAETLLSQAVEQLRQATQVLQEMRDLGELSQEAPGLREKRKELVTLYRRSAP
Protein: Zinc finger protein ZFP1 (Q584Y9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pumillio RNA binding protein, putative
Sequence:
MHISTPTLSDVRSENSLSFSGSRNGRRGVDASKFRTQPCRNYRFGAHCSFGSRCAFSHGEKPDLPPPPPYSAAVQNEMVLPPAYASRFRHDPYSFYSVRLED
Protein: TPR repeat-containing protein ZIP4 (Protein SPO22 homolog) (AtSPO22) (Protein ZIP4 homolog) (AtZIP4) (B0M1H3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for meiotic chromosome segregation. It is involved in interference-sensitive crossovers (class I meiotic crossover) formation, in both male and female meiosis. Is specific to recombination events resulting in interference-sensitive crossovers (class I meiotic crossover). Not required for synapsis completion.
Subcellular location: Nucleus {ECO:0000269|PubMed:17530928, ECO:0000269|PubMed:18348867}. Chromosome {ECO:0000269|PubMed:17530928, ECO:0000269|PubMed:18348867}. Note=Detected in punctuate foci onto the chromosomes in prophase I meiocytes. {ECO:0000269|PubMed:17530928, ECO:0000269|PubMed:18348867}.
Interaction partners:
- ATP-dependent DNA helicase homolog MER3
- DNA mismatch repair protein MSH4
- DNA mismatch repair protein MSH5
- Basic leucine zipper 23
- Basic leucine zipper 19
- Zinc transporter 2
- Crossover junction endonuclease MUS81
- Zinc transporter 4, chloroplastic
- Meiotic recombination protein DMC1 homolog
- DNA mismatch repair protein MLH1
Sequence:
MRIAEITTPDLRLHHRETDSHTHHPLLSEIELLIQQSEAISKDQPLPQSLPISLRQFLTRLSQLAPFPDNSFKLTIWKLSFRLWNACVDLANAASLQSSLTSAENIANLRHVAADMLFLAKDVTGVPSPTIKSSLFYYKTGLVYHSLKKFDLASDCFERATEIVSKIDIAKISDAGEKKLFLDLNLARSRTAWEISDRNLAVTLLNRAKNLLFGSPDHYKSLSNQFLAFGKSSLSRGDDDCSLNDALRLMNEALDLCEKGLGTAKTREDTTEFTAMRIKTLRFISAVHLQKGEFENVIKCVKVLRNGGNGSDGADQHASLPVLAMKAWLGLGRHSEAEKELRGMVGNNDIPEAVWVSAVEAYFEVVGTAGAETAKGVFLGLLGRCHVSAKAALRVAHRVLGESRGGDNGSRIRANVVAQLVSDERVVALFASEAVTKERKAIHSVLWNSASDHFRAKDYETSAEMFEKSMLYIPHDIENRVFRAKGFRVLCLCYLGLSQLDRALEYIEEAEKLEPNIACSFLKFKIYLQKKEHSCAIGQIDAMTSCLDFSPDYLSLSAHEAISCQALPVAVASLSKFLSFYISGKKMPTTEVVVFRTLVTILTQDIGSETEALNFMLQAQSRASKLGTECFFGLGETGKREQNWFAATCWNLGSRCGKEKKYELCGEFLRLASEFYGYIDTDESGEDKLMICRSIILSVTAMIALEKQTKSALTETQVKLAAELLVRAGKIMSSSLSDGKDCIMEPELIFMYTLLAYDIHGRLNNSAFQLLVVKTFAGSKSCHYNYLLQLGIFASQSPQSNPDVSTFALNECLSALIASASPEYPTIALIIRKLISIASVHKGDTDDEEAILKMYKQAYRIMVGLKEGEYPTEEGKWLAMTAWNRAALPVRLGQFETAKKWLSIGLEIADKVTGMDTYKACMQDYLAGFQTKVSSA
Protein: Zinc finger protein DPF3 (BRG1-associated factor 45C) (BAF45C) (Zinc finger protein cer-d4) (Q92784)
Organism: Homo sapiens (Human)
Function: Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Actin-like protein 6B
- Zinc finger protein neuro-d4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- AT-rich interactive domain-containing protein 1A
- AT-rich interactive domain-containing protein 1B
- PHD finger protein 10
- Protein polybromo-1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
Sequence:
MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDIPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA
Protein: Protein FAM133A (Q8N9E0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKRDNRVAYMNPIAMARWRGPTQSVGPTIQDYLNRPRPTWEEVKKQLENKKTGSKALAEFEEKMNENWKKELEKSREKLLSGNESSSKKRERKKKRKKKSCRSSSSSSSSDSSSSSSDSEDEEKKQGKRRKKKKNRSYKSSQSSTHESESESKESVKKKKKSKDETEKEKDVRSLSKKRKKSYPDDKPLSSESSSESDYEEDVQAKKKRRCEEREQAKEKVKKKKKKQHKKHSKKKKKKSGSSHKSR
Protein: Solute carrier family 41 member 1 (Q8IVJ1)
Organism: Homo sapiens (Human)
Function: Na(+)/Mg(2+) ion exchanger that acts as a predominant Mg(2+) efflux system at the plasma membrane. Transporter activity is driven by the inwardly directed electrochemical gradient for Na(+) ions, thus directly depends on the extracellular Na(+) ion concentration set by Na(+)/K(+) pump. Generates circadian cellular Mg(2+) fluxes that feed back to regulate clock-controlled gene expression and metabolism and facilitate higher energetic demands during the day. Has a role in regulating the activity of ATP-dependent enzymes, including those operating in Krebs cycle and the electron transport chain (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18367447, ECO:0000269|PubMed:23976986}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:23661805}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1
- Ras-related protein Rab-7L1
- N-fatty-acyl-amino acid synthase/hydrolase PM20D1
- Solute carrier family 45 member 3
- Transient receptor potential cation channel subfamily M member 6
- Metal transporter CNNM2
- Transient receptor potential cation channel subfamily M member 7
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Magnesium transporter MRS2 homolog, mitochondrial
- Metal transporter CNNM4
Sequence:
MSSKPEPKDVHQLNGTGPSASPCSSDGPGREPLAGTSEFLGPDGAGVEVVIESRANAKGVREEDALLENGSQSNESDDVSTDRGPAPPSPLKETSFSIGLQVLFPFLLAGFGTVAAGMVLDIVQHWEVFQKVTEVFILVPALLGLKGNLEMTLASRLSTAANIGHMDTPKELWRMITGNMALIQVQATVVGFLASIAAVVFGWIPDGHFSIPHAFLLCASSVATAFIASLVLGMIMIGVIIGSRKIGINPDNVATPIAASLGDLITLALLSGISWGLYLELNHWRYIYPLVCAFFVALLPVWVVLARRSPATREVLYSGWEPVIIAMAISSVGGLILDKTVSDPNFAGMAVFTPVINGVGGNLVAVQASRISTFLHMNGMPGENSEQAPRRCPSPCTTFFSPDVNSRSARVLFLLVVPGHLVFLYTISCMQGGHTTLTLIFIIFYMTAALLQVLILLYIADWMVHWMWGRGLDPDNFSIPYLTALGDLLGTGLLALSFHVLWLIGDRDTDVGD
Protein: DNA polymerase kappa (Q384H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA polymerase eta
- DNA polymerase
Sequence:
MNEQRLAEGREKQLQELKRKSSLFTQLLGGERNAAQRKQWELKVSKIEQELEATRRLGTYIHLDMDMFYAAVEIKKHPEYAAIPLAIGTITRLITTNYVARGRGIRQGMPGFLALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLDDFTLEVSAYIERFEGTKTAEDVASELRVRVFGETKLTASAGIGPTAALAKIASNINKPNGQHDLNLHTRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDIYNRRVELCYILHNNLFRFLLGASIGIMQWPDAATAANTENCEGATGEQRKAISSERSITTPRTKEGMQEMLDTVFNGAYEEMRKSELMCRRISLRIRWASYRYQQYTKSLIQYSDDSATLRRAVDGLLLPHAAKYSEISLLGVRFLDLISAKDFHMKRKGGNQLSISQFIRPKKPGEVTATTGIKRERTTEPKQVVGVNLSSDDEDENDSVGLASSSTILVSTDKGTVEREVTIIE
Protein: Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Q8R4K2)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Interleukin-1 receptor-associated kinase-like 2
- Myeloid differentiation primary response protein MyD88
- Interleukin-1 receptor-associated kinase 1
- TNF receptor-associated factor 6
- NF-kappa-B essential modulator
- Toll-like receptor 4
- Interferon regulatory factor 7
- Interleukin-1 receptor-associated kinase 3
- TNF receptor-associated factor 3
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MNKPLTPSTYIRNLNVGILRKLSDFIDPQEGWKKLAVAIKKPSGDDRYNQFHIRRFEALLQTGKSPTCELLFDWGTTNCTVGDLVDLLVQIELFAPATLLLPDAVPQTVKSLPPREAATVAQTHGPCQEKDRTSVMPMPKLEHSCEPPDSSSPDNRSVESSDTRFHSFSFHELKSITNNFDEQPASAGGNRMGEGGFGVVYKGCVNNTIVAVKKLGAMVEISTEELKQQFDQEIKVMATCQHENLVELLGFSSDSDNLCLVYAYMPNGSLLDRLSCLDGTPPLSWHTRCKVAQGTANGIRFLHENHHIHRDIKSANILLDKDFTAKISDFGLARASARLAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLELITGLAAVDENREPQLLLDIKEEIEDEEKTIEDYTDEKMSDADPASVEAMYSAASQCLHEKKNRRPDIAKVQQLLQEMSA
Protein: Stardust, isoform H (EC 2.7.4.8) (Q0KHU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRILKQWNRRRSGSSIVVLDGDDLKPCLPDDYISGQHHLNHQQQLQLQQQLQQQHPLQQQHYRTHSGDIREIDQEMLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQLNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: ADP-ribosylation factor-like protein 15 (ADP-ribosylation factor-related protein 2) (ARF-related protein 2) (Q9NXU5)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein tyrosine phosphatase type IVA 1
Sequence:
MSDLRITEAFLYMDYLCFRALCCKGPPPARPEYDLVCIGLTGSGKTSLLSKLCSESPDNVVSTTGFSIKAVPFQNAILNVKELGGADNIRKYWSRYYQGSQGVIFVLDSASSEDDLEAARNELHSALQHPQLCTLPFLILANHQDKPAARSVQEIKKYFELEPLARGKRWILQPCSLDDMDALKDSFSQLINLLEEKDHEAVRM
Protein: Serpin A12 (Visceral adipose tissue-derived serine protease inhibitor) (Vaspin) (Visceral adipose-specific serpin) (Q7TMF5)
Organism: Mus musculus (Mouse)
Function: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues.
Subcellular location: Secreted {ECO:0000269|PubMed:23370777}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Retinoic acid receptor responder protein 2
- Leptin
- Nicotinamide phosphoribosyltransferase
- Resistin
- Resistin-like gamma
Sequence:
MTRMLDLGLFLAGLLTVKGLLQDRDAPDMYDSPVRVQEWRGKKDARQLARHNMEFGFKLLQRLASNSPQGNIFLSPLSISTAFSMLSLGAQNSTLEEIREGFNFKEMSNWDVHAAFHYLLHKLNQETEDTKMNLGNALFMDQKLRPQQRFLNLAKNVYDADMVLTNFQDLENTQKDINRYISQKTHSRIKNMVKSIDPGTVMILTNYIYFRGRWQYEFDPKQTKEEEFFIEKGKTVKVPMMFQRGLYDMAYDSQLSCTILEIPYRGNITATFVLPDNGKLKLLEQGLQADIFAKWKSLLSKRVVDVWVPKLRISSTYNMKKVLSRLGISKIFEENGDLTRISSHRSLKVGEAVHKAELKMDEKGMEGAAGSGAQTLPMETPRHMKLDRPFLMMIYENFMPSMVFLARIYDPSG
Protein: Alpha-ketoglutarate dehydrogenase component 4 (Alpha-ketoglutarate dehydrogenase subunit 4) (Mitochondrial ribosomal protein S36) (P82908)
Organism: Bos taurus (Bovine)
Function: May be necessary to recruit DLD/E3 to the mitochondrial 2-oxoglutarate dehydrogenase complex (OGDC) core composed of OGDH/E1-DLST/E2, hence stabilizes the complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279123, ECO:0000269|PubMed:22015679, ECO:0000269|PubMed:36854377}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein bS21m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS9m
Sequence:
MMGSKMASASRVVQVVKPHTPLIRFPDRRDNPKPNVSEVLRSAGLPSHTSSISQHSKGSKSPDWLMHQGPPDTAEMIKTLPQKYRRKLVSQEEIEFIQRGGPE
Protein: Centromere protein H (cDNA FLJ41767 fis, clone IMR322006495, highly similar to Centromere protein H (Kinetochore protein CENP-H)) (B3KVZ3)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEQPQMQDADEPADSGGEGRAGGPPQVAGAQAACSEDRMTLLLRLRAQTKQQLLEYKSMVDASEEKTPEQIMQEKQIEAKIEDLENEIEEVKVAFEIKKLALDSVLMDNMKHLLELNKLIMKSQQESWDLEEKLLDIRKKRLQLKQASESKLLEIQTEKNKQKIDLDSMENSERIKIIRQNLQMEIKITTVIQHVFQNLILGSKVNWAEDPALKEIVLQLEKNVDMM
Protein: Inositol polyphosphate multikinase (IPMK) (EC 2.7.1.127) (EC 2.7.1.151) (Inositol polyphosphate kinase 2) (Q9US14)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5). Also converts (Ins(1,3,4,5,6)P5) to InsP6 (Probable). Has also a role in transcription regulation. The catalytic activity is required for PHO gene repression by phosphate and for NCR gene activation in response to nitrogen availability, indicating a role for inositol pyrophosphates in these controls. Inositol polyphosphates may be involved in the regulation of chromatin remodeling of transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized inositol polyphosphate kinase C970.08
- Inositol-pentakisphosphate 2-kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Myo-inositol transporter 2
- Myo-inositol transporter 1
- Dibasic-processing endoprotease
- Adenylate kinase
Sequence:
MKLKLFPFQAAGHGQVLVSEDDKILIKPCIKSEVDFYKTCNDNITLYNWIPKNFGEWMPSSRDIEGINPIAESVAFSLTGKAIILENILYQMETPCVMDIKLGKQLWADDAPLEKRKRLDAVSRSTTSGSLGFRITGILSWDRTNNTYIKRSTAWGKTLTDSDVVEGLNDFFVSCSLSQKARLVESFLNLLKLFEVDLSESYIELKSSSILFVYDYSSLNPTYHCESNVVLKLIDLAHSRWTKNTIDHNTLIGVKNLIHCFAMLLKNE