wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein bud20 (Q9P370)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000250|UniProtKB:Q08004}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q08004}.
Interaction partners:
- Ribosome biogenesis protein rlp24
- Nucleolar GTP-binding protein 2
- Probable nucleolar GTP-binding protein 1
- 60S ribosomal export protein nmd3
- Eukaryotic translation initiation factor 6
- Ribosome biogenesis protein nsa2
- Ribosome assembly factor mrt4
- Ribosome production factor 2 homolog
- Probable metalloprotease arx1
- GTPase grn1
Sequence:
MGRVARKRKHHSNGNHALFRTRVYGRDLDQIHNDLTESEKFDKLPIDPDLPGLGQHYCIECARYFDSSQALLVHKKGKVHKRRLKNLREEPYTQEEAEAAVNIGQPKQSVASKLADNSNVVMAD
Protein: G antigen 5 (GAGE-5) (Cancer/testis antigen 4.5) (CT4.5) (Q13069)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSWRGRSTYYWPRPRRYVQPPEVIGPMRPEQFSDEVEPATPEEGEPATQRQDPAAAQEGEDEGASAGQGPKPEADSQEQGHPQTGCECEDGPDGQEMDPPNPEEVKTPEEGEKQSQC
Protein: T-complex protein 1 subunit delta (Q9VK69)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma
- Chaperonin containing TCP1 subunit 6
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- Peroxin-19
- Uncharacterized protein
- Probable prefoldin subunit 5
Sequence:
MAPKAAAVNIKPTAKAFKDKSKPTDVRLSNIQAAKAVSDAIRTSLGPRGMDKMIQAGNGEVSITNDGATILKQMNVLHPAAKMLVELSRAQDVAAGDGTTSVVVIAGALLEACEKLLQKGLHPTAISDSFQRCSNKAVEILKQMSTPIELDDRETLIKSASTSLNSKVVSQQSSLLAPIAVDAVLKVTDPGKETSVDLKNIKVISSLGGTVEDTELVDGLVFTCRSAGSNAPKRIEKAKIGLIQFCISAPKTDMDHNVIVSDYAAMDRVLKEERSYILNIVKQIKKSGCNVLLVQKSILRDAVSDLAQHFLDKIKCMVVKDVEREDIEFVCKTLHCRPIASLDHFTAENLSSADLVEEVASGTNKFVKITGIQNMGRTVSIICRGSNKLVLEEAARSLHDALCVVRCLVKLRAQIVGGGAPEIEMALQLAALAQTVEGVDAYCFRAFADALEVIPSTLAENAGLNPIATVTELRNRHAQGEKNAGINVRKGAITDIFAENVVQPLLVSISSITLATETIRSILKIDDIVNTFS
Protein: Alcohol dehydrogenase 2 (EC 1.1.1.1) (Alcohol dehydrogenase II) (ADHII) (YADH-2) (P00331)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2937632}.
Interaction partners:
- Alcohol dehydrogenase 4
- S-
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase 5
- Alcohol dehydrogenase 3, mitochondrial
- Pyruvate decarboxylase isozyme 1
- Pyruvate decarboxylase isozyme 3
- Pyruvate decarboxylase isozyme 2
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Potassium-activated aldehyde dehydrogenase, mitochondrial
Sequence:
MSIPETQKAIIFYESNGKLEHKDIPVPKPKPNELLINVKYSGVCHTDLHAWHGDWPLPTKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQEYATADAVQAAHIPQGTDLAEVAPILCAGITVYKALKSANLRAGHWAAISGAAGGLGSLAVQYAKAMGYRVLGIDGGPGKEELFTSLGGEVFIDFTKEKDIVSAVVKATNGGAHGIINVSVSEAAIEASTRYCRANGTVVLVGLPAGAKCSSDVFNHVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSSLPEIYEKMEKGQIAGRYVVDTSK
Protein: Dro2 protein (Drosomycin 2) (Drosomycin-like 2) (Drosomycin-like D) (Drosomycin-like H) (Q7YXH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Dorsal-related immunity factor Dif
- Embryonic polarity protein dorsal
- Splicing factor ESS-2 homolog
- Lysozyme X
Sequence:
MVQIKFLFVFLAVMTIVVLAANMADADCLSGKYKGPCAVWDNEMCRRICKEEGHISGHCSPSLKCWCEGC
Protein: Nucleolar protein 9 (Pumilio domain-containing protein nop9) (Q92347)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C3B8.09
- Uncharacterized protein C13G1.09
- 20S-pre-rRNA D-site endonuclease nob1
- Uncharacterized protein C4F10.09c
- Ribosome biogenesis protein erb1
- Multiple RNA-binding domain-containing protein 1
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 22
- Ribosome biogenesis protein enp2 homolog
- Ribosome biogenesis protein tsr1
Sequence:
MPKKRKTRGKKHSAKQKEEEVNSVVSPGIAKNDEGAGNDEGAYQVNRYTNEPVQPFFGALDPEEEKYFQQAEQAFANHFTRENEDTRFFVDSIYREVQGKELIVCNNVFGSKVLEKLFPLSTSRQIKSFFSALNGHYVELIQTTFGSYAFEKLLSHMAAILNLETQGVTEDQDDVLEGENENVFMTAETLLMYMYNEIRPEVSMLMSHKLAVHVLGKIFLLLDGYRFVYHDGNRTTMESISVPESFPQFAYSIIDSATDNLDTPELRAYCVDKYASQIMRAFIRIDFERSKKTKKKHDPRLVSKLLLSNEYDLKELPFMETLLKDETGSRILEVIVENMSASHLLRFYAVFEGRFYRLCVHPIANFIMQRYIRRLGRKEIGSVIDELKKNTDNIIRKSFLPVLRTLLEKSNHLHCYQDDIFSMIQTSVTNSGKDANIIPCLLRSKHKRDKANPENKERKLVNNLLGAQLLEEMLHCEKQHIQLLLDSVLDLSKEQILEYCLETVSSHLIEGILDLSDLNPVFLKKFLNILSGSFATLAVSAPGSHIVDKAWKATRALPLYRTRIVRELAEGGDDVKFDFYGKKVCSNWKVELFRRAPDEWYRFMKQDEPSKRVHERARQYGRIVSGSSANTQPLGEKRSTENDEELESGPKRVKV
Protein: Ferredoxin--NADP reductase, leaf isozyme, chloroplastic (FNR) (EC 1.18.1.2) (P10933)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
Subcellular location: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Stromal side {ECO:0000305}. Note=In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane.
Interaction partners:
Sequence:
MAAAVTAAVSLPYSNSTSLPIRTSIVAPERLVFKKVSLNNVSISGRVGTIRAQVTTEAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEVY
Protein: Putative uncharacterized oxidoreductase YGL039W (EC 1.1.1.-) (P53183)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Uncharacterized oxidoreductase YKL107W
- Small ribosomal subunit protein eS21B
- Small ribosomal subunit protein uS15
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL15
Sequence:
MTTEKTVVFVSGATGFIALHVVDDLLKTGYKVIGSGRSQEKNDGLLKKFKSNPNLSMEIVEDIAAPNAFDKVFQKHGKEIKVVLHIASPVHFNTTDFEKDLLIPAVNGTKSILEAIKNYAADTVEKVVITSSVAALASPGDMKDTSFVVNEESWNKDTWESCQANAVSAYCGSKKFAEKTAWDFLEENQSSIKFTLSTINPGFVFGPQLFADSLRNGINSSSAIIANLVSYKLGDNFYNYSGPFIDVRDVSKAHLLAFEKPECAGQRLFLCEDMFCSQEALDILNEEFPQLKGKIATGEPGSGSTFLTKNCCKCDNRKTKNLLGFQFNKFRDCIVDTASQLLEVQSKS
Protein: Chymotrypsin-like elastase family member 2A (EC 3.4.21.71) (Elastase-2A) (P08217)
Organism: Homo sapiens (Human)
Function: Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity.
Subcellular location: Secreted {ECO:0000269|PubMed:31358993}.
Interaction partners:
- Carboxypeptidase A1
- Carboxypeptidase A2
- Kallikrein-5
- Bile salt-activated lipase
- Chymotrypsin-like elastase family member 3B
- Inactive pancreatic lipase-related protein 1
- Carboxypeptidase B
- Chymotrypsin-like elastase family member 3A
Sequence:
MIRTLLLSTLVAGALSCGDPTYPPYVTRVVGGEEARPNSWPWQVSLQYSSNGKWYHTCGGSLIANSWVLTAAHCISSSRTYRVGLGRHNLYVAESGSLAVSVSKIVVHKDWNSNQISKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGAVPDVLQQGRLLVVDYATCSSSAWWGSSVKTSMICAGGDGVISSCNGDSGGPLNCQASDGRWQVHGIVSFGSRLGCNYYHKPSVFTRVSNYIDWINSVIANN
Protein: Nuclear receptor ROR-beta (Nuclear receptor RZR-beta) (Nuclear receptor subfamily 1 group F member 2) (Retinoid-related orphan receptor-beta) (P45446)
Organism: Rattus norvegicus (Rat)
Function: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q92753}.
Interaction partners:
- Nuclear receptor coactivator
- RAR-related orphan receptor A
- RAR-related orphan receptor C
- Nuclear receptor corepressor 2
- Nuclear receptor interacting protein 1
Sequence:
MCENQLKTKADGTAQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQNNASYSCPRQRNCLIDRTNRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLYAEVQKHQQRLQEQRQQQSGEAEALARVYSSSISNGLSNLNTETGGTYANGHVIDLPKSEGYYNIDSGQPSPDQSGLDMTGIKQIKQEPIYDLTSVHNLFTYSSFNNGQLAPGITMSEIDRIAQNIIKSHLETCQYTMEELHQLAWQTHTYEEIKAYQSKSREALWQQCAIQITHAIQYVVEFAKRITGFMELCQNDQILLLKSGCLEVVLVRMCRAFNPLNNTVLFEGKYGGMQMFKALGSDDLVNEAFDFAKNLCSLQLTEEEIALFSSAVLISPDRAWLLEPRKVQKLQEKIYFALQHVIQKNHLDDETLAKLIAKIPTITAVCNLHGEKLQVFKQSHPDIVNTLFPPLYKELFNPDCAAVCK
Protein: Protein mesh (Q0KHY3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required, together with Ssk and Tsp2A, for the proper organization of smooth septate junctions (sSJs), probably by mediating cell adhesion via its homophilic interaction. Also required for the correct subcellular localization of several sSJ components, such as Ssk, cora and l(2)gl, and for the barrier function of the midgut epithelium. Required for maintaining the three-layered structure of the proventriculus.
Subcellular location: Cell junction, septate junction {ECO:0000269|PubMed:22854041, ECO:0000269|PubMed:26848177}. Apicolateral cell membrane {ECO:0000269|PubMed:22854041, ECO:0000269|PubMed:26848177}; Single-pass type I membrane protein {ECO:0000269|PubMed:22854041}. Note=Colocalizes with Ssk, cora, dlg1, l(2)gl and Fas3 at the apicolateral region of epithelial cells in the midgut. Also localizes to the apicolateral region of epithelial cells in the outer epithelial layer of the proventriculus and Malpighian tubules.
Interaction partners:
Sequence:
MRFKLFVVCALACGFMAFVLANENISTEEFEDQIINAVPEPVKVTKPKAQAEFVEVPKATPAPKKAEADNPKTKPLALQKPTLIPVVHVSSRGTDDILTVAGLKPEKMFGALIMPNDYLGELYDVDNSGYNWDPNNNVAPPTTYSTAAGGYTITAARLAELRSNFMYWYFDKDMYGGRGDYQFDIHASMTQLHKNLNFQLPFYGFRFNYTRLSLNGYLEFSDPPEYLTYPLVFPIKDWPAKRDPSFMGIFFSKCRVGRIYPSDIDQRTPGVYFRVERDLMGRTDRFGVEVRERTMWDIRQGVVGADTFIPKHVVIATWKNVSFAGGIDNSLYTTNTFQMVLATDEVYTYIIFNYAVLNWLSHTEAGGDTTKGEGGVPAYVGFNAGNGTQAYEYNPYSQNMVIRDLANRGWANGFPGRHIFRVDEQILIGSCNKDIDAALLPLTFAPESGNMLGGQVVNITGPCFDPAIRVTCHFDTESVLGTYVDRNRVICVQPYLKAEGYIRFQISVGTQRFKWRGKYFVETPAAATEKIFFTTDDVHKKNPAEIRITWNQYNLTSNANANVMISLWGYRETKIEPQLEYIDVIEASYSNSGSYVITPSNYINRNNINRDMQFGFLQINLTQPDQYSGLAISPVLWSRPIPLAWYMAPQWERQHGKRWARALCDNWIRADRFLRNFAADLPLCPCTLDQAVLDKGRFRPDRECDKDSNPSCLRHRGAIHCVVSGTPVAQGAEQQCCYDRYGFLMLTYDQMWGSRPRRVHNLGKMPWNEASKVPSLSMWFHDMRPFYSCCYWQEEQAVGCETYRFERRPSQDCVAYQAPGIAGVFGDPHFVTFDGTAYTFNGLGEFVLARSVDESNKFEVQGRFEQLPVNYYGEVKATQLTAVAMRGNTTTTIEVRLRPLHARWRYRLDVLADGRRVYFDRESLKFQHFDGVTVYTPTYLLNQSQVVVQFDAGIGVEVVENEGYMTGRVFLPWKFINKTAGLFGNWSFNKLDDFMLPNGQVAQLNLNDLRSIHTNFGIKWMLTDREVPGVGAALFKREFGRMSGYYANATFQPNYVLDPADFLPANRSYDLERAEELCGECMQCQYDYAMTLNRDLAHFTKNYYDTIVNMQAENAVRVVSCGVLQTPRFGRKLSFDFMPGAKVSFECNEGFILIGDQRRECLSNGLWNIPEYGYTECLREVYYTRRVAFIAIGIIFLVICPLMLCIVCGVYRYRQKQLKEDPQWQMPMLPRSRASSARNLRTLNYDDDSDTDASTLKKSRSYDKVYRTNEPLPGKPQIDFPAKKWDLDENDEDVTSSEGEKPKQLGRRSLHSASGTELDQHGSPVDGDHPDEDDDFDEADVHTGTTHPVGYHQPLSPEEADQLHRQQYSPTFSGLDSRTSGASSINYTPQAATQNRFGGVPVLPSNTQYYSRPPSSVNTVPLRTAPTPLTQDTGLPSPPLATSPTPSVQKSTEV
Protein: RNA polymerase sigma-54 factor (Q9PDH1)
Organism: Xylella fastidiosa (strain 9a5c)
Interaction partners:
- Two-component system, regulatory protein
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- histidine kinase
- DNA-binding transcriptional regulator NtrC)
- DNA-directed RNA polymerase subunit omega
- Arabinose 5-phosphate isomerase
- Ribosome hibernation promoting factor
- Lipopolysaccharide export system protein LptC
Sequence:
MTLKARLRTSIGQQLVMTPQLHQSIRLLQMSNAELQLEITAAIESNPLLDWAENQSSETSEATEREVETEDWQAKESAWDINGSKSNENDDNNPAERLTTGNTLTDHLLWQLHLSPLSARDYQIGTVLIDAIEEDGYLRELLSTLTATLAPLSVDESELLPVLRHIQSFDPTGVAARSLAECLTLQLKSLKEEIPGRALALQIVNSPLLEQLPRSGVTGLARELKRPSQDVQQAVELIRGLDPRPGKKIGDLEVGTYVVPDCVIWRQHGLWQAALLERAFPQVVLHRGYEQLINRCNDANASYLRNQLQEARWLLKGLEARGETLLKVVNSLIRHQTGFLEFGQHALRPLTIRELATELALHESTVSRAIAGKYVRTPRGTLPLRTFFASGISTDSGGETSNSAIQAIIRRLIETENPRKPLSDAKLAELLKTSGIPVARRTIAKYRDAMNISASHERVRVL
Protein: Aklanonic acid methyl ester cyclase AcmA (AAME cyclase) (EC 5.5.1.23) (Methyl aklanonate cyclase) (O52646)
Organism: Streptomyces galilaeus
Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the cyclization of aklanonic acid methyl ester to yield aklaviketone. It is also able to use nogalonic acid methyl ester as substrate, but produces exclusively auraviketone with C9-R stereochemistry.
Interaction partners:
Sequence:
MSEQIAAVRRMVEAYNTGKTDDVADYIHPEYMNPGTLEFTSLRGPELFAINVAWVKKTFSEEARLEEVGIEERADWVRARLVLYGRHVGEMVGMAPTGRLFSGEQIHLLHFVDGKIHHHRDWPDYQGTYRQLGEPWPETEHRRP
Protein: Serpin B6 (Cytoplasmic antiproteinase) (CAP) (Peptidase inhibitor 6) (PI-6) (Placental thrombin inhibitor) (P35237)
Organism: Homo sapiens (Human)
Function: May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood (By similarity). Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14670919, ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170, ECO:0000269|PubMed:8486644}.
Interaction partners:
- Cathepsin G
- Plasma serine protease inhibitor
- Kallikrein-8
- Caspase-1
- Caspase recruitment domain-containing protein 16
- Tissue-type plasminogen activator
Sequence:
MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP
Protein: NADPH oxidase 2 (EC 1.6.3.-) (CGD91-phox) (Cytochrome b(558) subunit beta) (Cytochrome b558 subunit beta) (Cytochrome b-245 heavy chain) (Heme-binding membrane glycoprotein gp91phox) (Neutrophil cytochrome b 91 kDa polypeptide) (gp91-1) (gp91-phox) (p22 phagocyte B-cytochrome) (O46522)
Organism: Bos taurus (Bovine)
Function: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P04839}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04839}. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P04839}.
Interaction partners:
- Neutrophil cytosol factor 1
- Neutrophil cytosol factor 2
- Cytochrome b-245 light chain
- Ras-related C3 botulinum toxin substrate 2
- Neutrophil cytosol factor 4
- NADPH oxidase 4
- NADPH oxidase 2
- Vascular cell adhesion protein 1
- Vascular cell adhesion protein 1
- Matrix metalloproteinase-9
Sequence:
MGNWVVNEGISIFVILVWLGMNVFLFVWYYRVYDIPDKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRIRRQLDRNLTFHKMVAWMIALHTAIHTIAHLFNVEWCVNARVNNSDPYSIALSDIGDKPNETYLNFVRQRIKNPEGGLYVAVTRLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAQRIVRGQTAESLLKHQPRNCYQNISQWGKIENCPIPEFSGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPVVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFKACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNKAPNLRLKKIYFYWLCRDTHAFEWFADLLQLLETQMQEKNNTDFLSYNICLTGWDESQASHFAMHHDEEKDVITGLKQKTLYGRPNWDNEFKTIGSQHPNTRIGVFLCGPEALADTLNKQCISNSDSGPRGVHFIFNKENF
Protein: Ataxin 2 (A0A2R8YCG6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYVSTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHPSHVQPAYTNPPHMAHVPQCASEALARCGLEMRLSWIYLSEGYLAHVQSGMVPSHPTAHAPMMLMTTQPPGGPQAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL
Protein: Molecular chaperone Hsp70 (Q2UBH7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- J domain-containing protein
- STI1 domain-containing protein
- J domain-containing protein
- Endoplasmic reticulum chaperone BIP
- Uncharacterized protein
- Flavin reductase like domain-containing protein
- Molecular chaperone
- HSF-type DNA-binding domain-containing protein
- Molecular chaperone
- UBA domain-containing protein
Sequence:
MAPAVGIDLGTTYSCVGVFRDDRIEIIANDQGNRTTPSFVAFTDTERLIGDAAKNQVAMNPHNTVFDAKRLIGRRYADAEVQSDMKHWPFKIVDKGGKPIIQVEFKGEEKQFTPEEVSSMVLTKMRETAEAYLGGTVNNAVITVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDKKAEGERNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRLVNHFVNEFKRKHKKDLTTNARALRRLRTACERAKRTLSSAAQTSIEIDSLFEGIDFYTSITRARFEELCQDLFRGTMEPVERVLRDAKIDKSSVHEIVLVGGSTRIPKIQRLVSDFFNKEPNKSINPDEAVAYGAAVQAAILSGDSSSKSTNEILLLDVAPLSLGIETAGGVMTALIKRNTTIPTKKSETFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELTGIPPAPRGVPQIEVTFDVDANGIMNVSAVEKGTGKTNKITITNDKGRLSKEEIERMLADAEKYKAEDEAEASRIQAKNGLESYAYSLKNTISEGKLTISDSDKEKVTSKVDEIIGWLDSNQTATKEEYESQQKELEGVANPIISAAYGGAAGAAPGGAPGAAPGGSTRTADEVEEKPEELD
Protein: Pyruvate decarboxylase (EC 4.1.1.1) (8-10 nm cytoplasmic filament-associated protein) (P59NC) (P33287)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Subcellular location: Cytoplasm. Note=Cytoplasmic filaments.
Interaction partners:
- Alcohol dehydrogenase 1
- alcohol dehydrogenase
- Pyruvate kinase
- aldehyde dehydrogenase
- S-
- alcohol dehydrogenase
- NADP-dependent alcohol dehydrogenase C
- alcohol dehydrogenase
- Aldehyde dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
Sequence:
MVAQQQGKFTVGDYLAERLAQVGVRHHFVVPGDYNLILLDKLQAHPDLKEVGCANELNCSLAAEGYARANGISACVVTYSVGALSAFNGTGSAYAENLPLVLISGSPNTNDPSQYHILHHTLGHPDYTYQYEMAKKITCCAVAIPRAIDAPRLIDRALRAAILARKPCYIEIPTNLAGATCVRPGPISAITDPITSDKSALEAAAKCAAEYLDGKLKPVILVGPKAGRAGSEKELIEFAEAMGCAVALQPAAKGMFPEDHKQFVGIFWGQVSSDAADAMVHWADAMICVGAVFNDYSTVGWTAVPNIPLMTVDMDHVTFPGAHFSRVRMCEFLSHLATQVTFNDSTMIEYKRLKPDPPHVHTAEREEPLSRKEISRQVQEMLTDKTSLFVDTGDSWFNGIQLKLPPGAKFEIEMQWGHIGWSIPAAFGYALRHPDRHTIVLVGDGSFQVTAQEVSQMVRFKVPITIMLINNRGYTIEVEIHDGSYNKIKNWDYAMLVEAFNSTDGHAKGLLANTAGELADAIKVAESHKEGPTLIECTIDQDDCSKELITWGHYVAAANARPPRNMSVQE
Protein: Starmaker (Q57ZC1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MSKSLPPLESSSRGGEAARVGVYASHGPAATNALCVVTPRSTVNSNLRPQSAQRFLETEFTLGPLQDQSLPPYNDLEDPYLAPYWARREMLIRETAERREEMRRQKRLEQHRREVARRRFEERRQRELEELACRTGFATQRRVEAEELTSPKETTSGRKEVAKKRQRTVSSRATGSKKRAVATVPKPPKQKRPDTVGQRGGRPGACSSQGKGKTSSPPKNILLKTIRETLNSDSSRPATPQKGKGAASPVGGRKSGGGLTESSKHGAVTEDEAPISSSVAEDSATGKGSTSSVAQPSEAKRESRPSTASPQPASTEQSTSKEILKDGGNSRPASAARPSSASASASQKAMQQDTTDAEDGKDTQSDRSRPSSRKSERSGREGREKTDDEPTADTTKNDYGDEFEASESGKKDPDTEDQKDTESERSRSSSKKPEELTKDDADKTDDEPTADTTKNDYGDEFEASESGKKDPDTEDQKDTESERSRSSSKKPEDDEQKDEYTEELDKSQTSEKKDTEAEDQKDTESERSRSSSKKPEDDEQKDEYTEELDKSQTSEKKDTEAEDQKDTESERSRSSSKKPEDDEQKDEYTEELDKSQTSEKKDTESEQSRSSSKKPEDDEQKDEYTEELDKSQTSEKKDTEAEDQKDTESERSRSSSKKPEDDEQKDEYTEELDKSQTSEKKDTEAEDQKDTESERSRSSSKKPEDDEQKDEYTEELDKSQTSEKKDTESEQSRSSSKKSESSAKLEGDKFEYGDELERSPSSEKGEAVQQVVEDEHVNDQDVDELDSDAVKSEAVDEASGADAAKDSADGASSKESSSKRTSRSSSSVSKGRKNASSSSSSIGSEELSGNDVARASGTGEDEIEDEA
Protein: Gap junction alpha-3 protein (Connexin-46) (Cx46) (P29414)
Organism: Rattus norvegicus (Rat)
Function: Structural component of lens fiber gap junctions (Probable). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1659572}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9TU17}. Cell junction, gap junction {ECO:0000250|UniProtKB:Q9TU17}.
Interaction partners:
- Gap junction alpha-8 protein
- Gap junction alpha-5 protein
- Gap junction alpha-1 protein
- Gap junction alpha-4 protein
- Gap junction beta-2 protein
- Beta-crystallin B1
- Filensin
- Gap junction gamma-1 protein
- Beta-crystallin B2
- Gap junction beta-4 protein
Sequence:
MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEEVWGDEQSDFTCNTQQPGCENVCYDRAFPISHIRFWALQIIFVSTPTLIYLGHVLHIVRMEEKKKEREEELLRRDNPQHGRGREPMRTGSPRDPPLRDDRGKVRIAGALLRTYVFNIIFKTLFEVGFIAGQYFLYGFQLQPLYRCDRWPCPNTVDCFISRPTEKTIFVIFMLAVACASLVLNMLEIYHLGWKKLKQGVTNHFNPDASEVRHKPLDPLSEAANSGPPSVSIGLPPYYTHPACPTVQGKATGFPGAPLLPADFTVVTLNDAQGRGHPVKHCNGHHLTTEQNWASLGAEPQTPASKPSSAASSPHGRKGLTDSSGSSLEESALVVTPEGEQALATTVEMHSPPLVLLDPERSSKSSSGRARPGDLAI