wanglab/gogpt-training-data huggingface dataset:
Protein: von Willebrand factor A domain-containing protein 3B (VWA domain-containing protein 3B) (Q502W6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26157035}.
Interaction partners:
Sequence:
MEKSGPSSTISEQQLQRQEGWINTKTDLAEQSLISSEKWLQLHGLKSNKLTLKQILSQIGFPHCEDYVASLGRPVASRYADGLFPQLYRAEDGRVYNLTAKSELIYQFVEHLTQAVESYKQRMDWLTSKSRQIFGVILEQCVTIVLDFGGILEGELDLCREALTMVLQEQVAHITEFNIIRVSQEPVKWQENATPVTEQSIATAISWVEKLTVELTVSEAGRLDALLEAGRDKTIESIYYFVVGDVPEESKELLLQRALEIPCPVYTVSFNARGEGTIAFLKDLSAKTHSRFHAFAERTECVEFPAFSTKDGDNVMTWNSRKLKGKLPPGAGVREDVFLVWQEMEEACSTLAQIQRLVAEPPKPDVATVDCESETTSVEIASNPEDTWDSKTWLQKYGLKAQKLSLYDVLADCSFRHADGVVDIKAKPENESVQTSAETNKKTVHAKYCSRFVHAPWKDGSLVHVNITKEKCKWYSERIHTALARIRRRIKWLQDGSQSLFGRLHNDCIYILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSALKTAFADKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGEFHFYNFGCKDPTPPEAVQNEDLTLLVKEMEQGHSDLEKMQDLYSESLIMDWWYNAEKDGDSKHQKEICSMISTPEKCAKPQSDVDSTQTSSLNMLKGPWGLSDQKVQKKKVLHAESTKTSLLRSQMSSLRSSACSERKDGLSNASSRRTALSDKEMSILLAEEWLDDKSSEKVTREGSQVYDHDSSDVSSENWLKTYGLVAKKLTLMDALSVAAVPHSSTYVPVLDKHVVSKVFDEVFPLAHVCNDTNKMTLINPQGAKLNIYKRKVEQAIQSYEKRLNKIVWRALSQEEKEKLDANKPIQYLENKTVLNQALERLNWPISLKELSMLESEILAGKMYIQQAMELQEAAKKNYANKAPGEQQKLQGNPTKKTKSKRPDPLKGQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMPCPLLQVGDYVFAKIVIPKGFDFYVPAIVIALPNKHVATEKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHIKSPPIPEDPEVEDVEARNSAFLFWPLKEADTQDSREPRREKPRRKKRPAKQPLQQAAPSDSDGSSHGISSHGSCQGTHPEPRTAHLHFPAAGRLGLSSHAIIATPPPRAALPCTLQATHSSKGLRSVPETL
Protein: AP-3 complex subunit sigma-1 (AP-3 complex subunit sigma-3A) (Adaptor-related protein complex 3 subunit sigma-1) (Clathrin-associated/assembly/adaptor protein, small 3) (Sigma-3A-adaptin) (Sigma3A-adaptin) (Sigma-adaptin 3a) (Q92572)
Organism: Homo sapiens (Human)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Interaction partners:
- AP-3 complex subunit delta-1
- AP-3 complex subunit beta-1
- AP-3 complex subunit mu-1
- AP-3 complex subunit mu-2
- AP-3 complex subunit beta-2
- AP-2 complex subunit alpha-1
- AP-2 complex subunit mu
- AP-4 complex subunit epsilon-1
- AP-5 complex subunit mu-1
- AP-4 complex subunit mu-1
Sequence:
MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGLLIGGSDNKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHNILAEMVMGGMVLETNMNEIVTQIDAQNKLEKSEAGLAGAPARAVSAVKNMNLPEIPRNINIGDISIKVPNLPSFK
Protein: Tubulin beta-8 chain (Tubulin beta 8 class VIII) (Q3ZCM7)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. TUBB8 has a key role in meiotic spindle assembly and oocyte maturation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26789871}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26789871}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin alpha-1C chain
- Tubulin alpha chain-like 3
- Tubulin alpha-8 chain
- Tubulin alpha-4A chain
- Tubulin alpha-1A chain
- Tubulin alpha-3C chain
- Tubulin alpha-3E chain
- Gap junction alpha-1 protein
- Microtubule-associated protein tau
Sequence:
MREIVLTQIGQCGNQIGAKFWEVISDEHAIDSAGTYHGDSHLQLERINVYYNEASGGRYVPRAVLVDLEPGTMDSVRSGPFGQVFRPDNFIFGQCGAGNNWAKGHYTEGAELMESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSKTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGRYLTAAAIFRGRMPMREVDEQMFNIQDKNSSYFADWLPNNVKTAVCDIPPRGLKMSATFIGNNTAIQELFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDEEYAEEEVA
Protein: Thioredoxin H2 (AtTrxh2) (Thioredoxin 2) (AtTRX2) (Q38879)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase probably involved in the redox regulation of a number of cytosolic enzymes. Possesses insulin disulfide bonds reducing activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20133584}. Mitochondrion {ECO:0000269|PubMed:20133584}.
Interaction partners:
- Peroxiredoxin-2B
- Peroxiredoxin-2F, mitochondrial
- Peroxiredoxin-2E, chloroplastic
- Glutathione reductase, chloroplastic
- Thioredoxin reductase 2
Sequence:
MGGALSTVFGSGEDATAAGTESEPSRVLKFSSSARWQLHFNEIKESNKLLVVDFSASWCGPCRMIEPAIHAMADKFNDVDFVKLDVDELPDVAKEFNVTAMPTFVLVKRGKEIERIIGAKKDELEKKVSKLRA
Protein: BAG family molecular chaperone regulator 1A (BAG-1A) (O60125)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.
Interaction partners:
- BAG family molecular chaperone regulator 1B
- UV excision repair protein rhp23
- Hsp70 nucleotide exchange factor fes1
- Uncharacterized J domain-containing protein C17A3.05c
- 26S proteasome regulatory subunit rpn11
- Ribosome-associated molecular chaperone sks2
- Probable ubiquitin carboxyl-terminal hydrolase 3
Sequence:
MSEKTSTVTIHYGNQRFPVAVNLNETLSELIDDLLETTEISEKKVKLFYAGKRLKDKKASLSKLGLKNHSKILCIRPHKQQRGSKEKDTVEPAPKAEAENPVFSRISGEIKAIDQYVDKELSPMYDNYVNKPSNDPKQKNKQKLMISELLLQQLLKLDGVDVLGSEKLRFERKQLVSKIQKMLDHVDQTSQEVAA
Protein: Probable proton-coupled zinc antiporter SLC30A4 (Dri 27 protein) (Solute carrier family 30 member 4) (Zinc transporter 4) (ZnT-4) (O55174)
Organism: Rattus norvegicus (Rat)
Function: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (By similarity). Controls zinc deposition in milk (By similarity).
Subcellular location: Endosome membrane {ECO:0000269|PubMed:10600821}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within the basal region of epithelial cells. {ECO:0000269|PubMed:10600821, ECO:0000269|PubMed:12388418}.
Interaction partners:
- Zinc transporter ZIP6
- Zinc transporter ZIP13
- Zinc transporter ZIP4
- Metal cation symporter ZIP8
- Zinc transporter 6
- Zinc transporter ZIP11
- Zinc transporter ZIP9
- Slc39a1 protein
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MAGPGAWKRLKSLLRKDDAPLFLNDTSAFDFLDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQELPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAMQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHSHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTLRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKATAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTVQLQSYRQEATRTCANCQSSST
Protein: DUF4200 domain-containing protein (Q381R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFQKSPLLASNPFKEPLRSSGGGGGDLPGTINEHEVTVAQDIKQGDAKMAADLAILTGQPNVKNPVKQLLTQRENATTGSAPSHLNKSGQHTVEIREMHNTGTFIAKKREVGLMRLALANKESEIRHLEEEMDRVDKKLRQQQEQLASTEEKFNNFLKYSNLEQDAAVRRAERESKAKQKRLIDIKKLSAQINHLEQDMRKTEVQLELCMEYKTFMDNLTPPQFFFDVLTNFRVKEINGKILQETEAAYARQARKLRKQYEEAEARRASREAEKNSNNNAIFDDMDDSNKEDEEEEELIPLETQLEGLHRRFEEEANRRQAEEVEVIRNEISALTAEEVREALHNSYPHDKIPMYFTEPEQILDIFINVEEGNLFLIQNSQELEEELERVAMEFLHEREEMDAMVKQRQTQMDSLVSRIKESQDRLAQLEERLVDLESSDAAGLSMVDSAGGRGVAGYAKTVKVAMTQEVLKKSIEQTVGDIFRCINQRPTNPSRHQDGVDGGNSPVHPSGKRKHSAVVANRGPALDKKNAAKGKKKGQTASAVAPGATGPTGTQAESETSANMGPVEMLTIIENKVDEYHRYITDPKNGVEQSLIMSVLKTRDKERRHAARVLHLAKQLAEREERNQRALERSQATVVKYRGKPIMWRSRPPANALRRTEVDPNNPAPRDPEQDDEFFRA
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q8I5Q4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uncharacterized protein
- Nucleoporin NUP221, putative
- Serine repeat antigen 3
- Cysteine proteinase falcipain 1
- Falcipain-3
- Thioredoxin-like protein
Sequence:
MLYKSLKASTIIGRKCFHWWNNLPITWKVGIACSVLFPPLWNYNERRKAKEKQIFYNKSIRDYVFFDIAIENKYVGRVLIGLYSDQVPLSTENFIQLAEGYQIKDKYIGYRNTSIHKIYPGIGLVGGNVLNDKEGLSIYGKKFPDENFDMEFVQDGDVALFNEGPHSNSSQFIITFSPMPILHKHNVVIGTVLKGMNIIRMIENVGTKLGHPMYNVRIVNCGLYKGLEKDGPPFFNFTEIIEKNKEHLISKKEFEKLSKEQRQSLLNDSNKTEKKKKQAL
Protein: Tsukushi (C-TSK) (Leucine-rich repeat-containing protein 54) (Q65Z91)
Organism: Gallus gallus (Chicken)
Function: Contributes to various developmental events through its interactions with multiple signaling pathways. Dorsalizing factor involved in the induction of Hensen's node by inhibiting bone morphogenetic proteins during gastrulation and by enhancing DVR1/VG1 activity. Wnt signaling inhibitor which competes with WNT2B for binding to Wnt receptor FZD4 and represses WNT2B-dependent development of the peripheral eye.
Subcellular location: Secreted {ECO:0000269|PubMed:15363410}.
Interaction partners:
Sequence:
MQFLAWFNMLLLLPCFSTTKTCFPGCHCEVESFGLFDSFSLTKVDCSGIGSHIVPVPIPLDTSYLDLSSNKLETINESMLTGPGYTTLVSLDLSYNNIAKISSTTFSRLRYLESLDLSHNSLEVLPEDCFSSSPLGDIDLSNNKLLDIALDVFASKGQGKPLNVDLSNNMLSKITRNHEKSIPNIQNLNLSGNRLTSVPNLQGIPLRYLNLDGNPLAKIEKGDFKGLKGLIHLSLSGLHDFRELSPYSFKELPALQVLDLSNNPNLRSLTAEVIFGLNSIQELNLSGTGVSSLPKTVLKYLPSLKSITLRKNIQCFKTIKEGQYHRQIGLTKLGLGAEELLWCKTPCPRPVCRCRDKPLQSAPQNLPTP
Protein: SUMO-activating enzyme subunit 1 (Ubiquitin-like 1-activating enzyme E1A) (Q6IQS6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: The heterodimer acts as an E1 ligase for sumo1, sumo2, and sumo3. It mediates ATP-dependent activation of sumo proteins followed by formation of a thioester bond between a sumo protein and a conserved active site cysteine residue on uba2/sae2 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- SUMO-activating enzyme subunit 2
- SUMO-conjugating enzyme UBC9-A
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier
- SUMO-conjugating enzyme UBC9-B
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 3-like
- BTB/POZ domain-containing protein KCTD2
- Rhomboid domain-containing 1.
Sequence:
MIDTIEKEDTIISEEEAAQYDRQIRLWGLDAQKRLRGSRVLLVGLRGLGAEVAKNLILAGVKGLTLLDHEQVTEESRRAQFLIPVDADGQNHAQASLERAQFLNPMVEVKADTEPVESKPDDFFFQFDAVCLTRCSRDLMVRVDQLCASRNIKVFCGDVYGYNGYMFSDLGQEYHYVEEKPKVVKGSNEANDGPEAKKPKIDPNETTMVKKTISFCSLKEALEVDWTTEKAKSSLKRIPADYFLLQVLLKFRTDKGRDPQPDSFAEDSQLLLQIRDDVLETMGLSSDLLPNTFVSYCFSEMSPVCAVVGGVLGQEIVKALSQRDAPHRNFFFFDGLKGSGVVDYFSSK
Protein: DNA polymerase zeta catalytic subunit (EC 2.7.7.7) (Protein reversionless 3) (P14284)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Nonessential DNA polymerase. Required for DNA damage induced mutagenesis. Involved in DNA repair, mitochondrial DNA repair and translesion synthesis. Translesion synthesis in S.cerevisiae may use a specialized DNA polymerase that is not required for other DNA replicative processes. Has a role in the bypass of abasic (AP) sites. Highly inefficient in incorporating nucleotides opposite the AP site, but efficiently extends from nucleotides, particularly an A, inserted opposite the lesion.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16452144}. Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase delta subunit 3
- DNA polymerase eta
- DNA polymerase delta small subunit
- DNA polymerase zeta processivity subunit
- DNA repair protein REV1
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- Proliferating cell nuclear antigen
- DNA repair protein RAD5
- Ubiquitin-conjugating enzyme variant MMS2
- DNA polymerase epsilon catalytic subunit A
Sequence:
MSRESNDTIQSDTVRSSSKSDYFRIQLNNQDYYMSKPTFLDPSHGESLPLNQFSQVPNIRVFGALPTGHQVLCHVHGILPYMFIKYDGQITDTSTLRHQRCAQVHKTLEVKIRASFKRKKDDKHDLAGDKLGNLNFVADVSVVKGIPFYGYHVGWNLFYKISLLNPSCLSRISELIRDGKIFGKKFEIYESHIPYLLQWTADFNLFGCSWINVDRCYFRSPVLNSILDIDKLTINDDLQLLLDRFCDFKCNVLSRRDFPRVGNGLIEIDILPQFIKNREKLQHRDIHHDFLEKLGDISDIPVKPYVSSARDMINELTMQREELSLKEYKEPPETKRHVSGHQWQSSGEFEAFYKKAQHKTSTFDGQIPNFENFIDKNQKFSAINTPYEALPQLWPRLPQIEINNNSMQDKKNDDQVNASFTEYEICGVDNENEGVKGSNIKSRSYSWLPESIASPKDSTILLDHQTKYHNTINFSMDCAMTQNMASKRKLRSSVSANKTSLLSRKRKKVMAAGLRYGKRAFVYGEPPFGYQDILNKLEDEGFPKIDYKDPFFSNPVDLENKPYAYAGKRFEISSTHVSTRIPVQFGGETVSVYNKPTFDMFSSWKYALKPPTYDAVQKWYNKVPSMGNKKTESQISMHTPHSKFLYKFASDVSGKQKRKKSSVHDSLTHLTLEIHANTRSDKIPDPAIDEVSMIIWCLEEETFPLDLDIAYEGIMIVHKASEDSTFPTKIQHCINEIPVMFYESEFEMFEALTDLVLLLDPDILSGFEIHNFSWGYIIERCQKIHQFDIVRELARVKCQIKTKLSDTWGYAHSSGIMITGRHMINIWRALRSDVNLTQYTIESAAFNILHKRLPHFSFESLTNMWNAKKSTTELKTVLNYWLSRAQINIQLLRKQDYIARNIEQARLIGIDFHSVYYRGSQFKVESFLIRICKSESFILLSPGKKDVRKQKALECVPLVMEPESAFYKSPLIVLDFQSLYPSIMIGYNYCYSTMIGRVREINLTENNLGVSKFSLPRNILALLKNDVTIAPNGVVYAKTSVRKSTLSKMLTDILDVRVMIKKTMNEIGDDNTTLKRLLNNKQLALKLLANVTYGYTSASFSGRMPCSDLADSIVQTGRETLEKAIDIIEKDETWNAKVVYGDTDSLFVYLPGKTAIEAFSIGHAMAERVTQNNPKPIFLKFEKVYHPSILISKKRYVGFSYESPSQTLPIFDAKGIETVRRDGIPAQQKIIEKCIRLLFQTKDLSKIKKYLQNEFFKIQIGKVSAQDFCFAKEVKLGAYKSEKTAPAGAVVVKRRINEDHRAEPQYKERIPYLVVKGKQGQLLRERCVSPEEFLEGENLELDSEYYINKILIPPLDRLFNLIGINVGNWAQEIVKSKRASTTTTKVENITRVGTSATCCNCGEELTKICSLQLCDDCLEKRSTTTLSFLIKKLKRQKEYQTLKTVCRTCSYRYTSDAGIENDHIASKCNSYDCPVFYSRVKAERYLRDNQSVQREEALISLNDW
Protein: T-cell activation inhibitor, mitochondrial (Tolerance associated gene-1 protein) (TOAG-1) (Q66JZ4)
Organism: Mus musculus (Mouse)
Function: May regulate T-cell apoptosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19684086}.
Interaction partners:
Sequence:
MFCHLRPLRRFGLRKVLPHWLHYSRALSGAEAINALRPFYFAVHPDFFGQHPREREVNENSLKRLSVYLENLQKPGFKSLKPTQLTFYIREKTAQNSSEGQEPISTTGFRAVRFTLHSSDLLSTVLYILNSCSLPVEHVQSLNTNVHSQPLKEATGMPDRPIKWHRSYYSFTGFKDPDEDLTHVSRVETTLTSWLGSNGKGAVKKLRNSLPLRKELDRLKNELSELLQLSDIRWQRGWGVAHRCSQLHSLSRLAQQNPGPLQNVKGCTVVFTDRSGMSALGHVMLGTMDVHHHWTRLFESLPSYFDLQRRMSALEAQISNLLGGIQVVYIEELQPALTLDQYYSLLHTFYNQLLRSRVPPHPHPQSLSGLQMILSSDRYAPSLHELGHFDIPALSDPASLQSFMRTKAQQARENMTRREKLKVMENELIQASTKQFSLEKLYKEPSISSRQMVDCCKRLLEQSLPYLHGMHLCVSHFYSVMQDGDLCIPWNWKKGEAMK
Protein: External alternative NAD(P)H-ubiquinone oxidoreductase B2, mitochondrial (EC 1.6.5.9) (External alternative NADH dehydrogenase NDB2) (NADH:ubiquinone reductase (non-electrogenic) NDB2) (Q94BV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). Calcium-dependent NAD(P)H dehydrogenase; more efficient on NADH. Binds calcium ions.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side {ECO:0000269|PubMed:21841088}. Peroxisome {ECO:0000250}.
Interaction partners:
- Ubiquinol oxidase 1a, mitochondrial
- Ubiquinol oxidase 1c, mitochondrial
- Mitochondrial uncoupling protein 1
- Ubiquinol oxidase 1b, mitochondrial
- Ubiquinol oxidase 3, mitochondrial
- Alternative NAD
- Cytochrome c oxidase subunit 6b-1
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Cytochrome c oxidase subunit 2
- Acyl-CoA N-acyltransferases
Sequence:
MRNFSVFERFSKAFKDHPSLTRILVVSTISGGGLIAYSEANASYGANGGAVVETGTKKKKVVLLGTGWAGTSFLKNLNNSQYEVQIISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIGRKNVDTSYLEAECFKIDPASKKVYCRSKQGLSSNGKKEFSVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRKTVIDSFEKASLPELSDEERKRILHFVVVGGGPTGVEFAAELHDFVTEDLVSLYPRAKGSVRITLLEAADHILTMFDKRITEFAEEKFSRDGIDVKLGSMVTKVNEKDISAKTKGGEVSSIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRRALATDEWLRVEGTDNIYALGDCATINQRKVMEDVSAIFSKADKDKSGTLTLKEFQEAMDDICVRYPQVELYLKSKRMRGIADLLKEAETDDVSKNNIELKIEEFKSALSQVDSQVKFLPATAQVAAQQGAYLAKCFDRMEECEKSPEGPIRMRGEGRHRFRPFRYRHLGQFAPLGGEQTAAQLPGDWVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSSI
Protein: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (EC 3.5.1.52) (Peptide:N-glycanase 1) (O74739)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- UV excision repair protein rhp23
Sequence:
MDFHAISQRFIDMMRSKNSQNASQPPETYPFYHEVRQMSQHPWMYEDPELQDYALSILPLDKLFQDASELEKEGDGSWGYQDYVIQALLKWFKREFFVWVNQPPCEKCGGETHMTGNGPPNEEEKWNGVRNVELYQCNVCGHNQRFPRYNRIRALLDSRKGRCGEWANCFTFLCRALGSRARWIWNAEDHVWTEVYSNKQQRWVHVDSGEESFDEPLIYEQGWGKKMSYCLGFGIDSVRDVSHRYIRHPENGLPRDRCPESVLQQALHEINIEFRSRLTDSERKALEEEDKREKDELDGYMRPVSQATPTNTDLPARQTGNVEWKEKRGEAGK
Protein: Neuromodulin (Axonal membrane protein GAP-43) (Growth-associated protein 43) (P35001)
Organism: Gallus gallus (Chicken)
Function: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:9813098}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side {ECO:0000250|UniProtKB:P17677}. Synapse {ECO:0000269|PubMed:9813098}. Cell projection, filopodium membrane {ECO:0000269|PubMed:9813098}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}.
Interaction partners:
- Brain acid soluble protein 1 homolog
- Abhydrolase_2 domain-containing protein.
- Glial fibrillary acidic protein
- Neurotrophic factor BDNF precursor form
- Microtubule-associated protein.
- ELAV-like protein
- Microtubule-associated protein.
- MARVEL domain-containing protein.
- Synaptophysin.
- Neural cell adhesion molecule 1
Sequence:
MLCCMRRTKQVEKNEDGDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKADAPASESEAADKKDEGPAGGAAENKESEASAATEASAADSAQLDEGSKDSSVPAEEKKGNGAADTGSEQPAPQAATPAASSEEKPAAAAETESATKASTDNSPSLKADEAQDKEEPKQADVPAADTTATTTPAAEDATAKATAQPQMETVESSQTEEKTDAVEETKPTESAQQEEVKEEESKADQENA
Protein: Helix-loop-helix protein 30 (H2KZZ2)
Organism: Caenorhabditis elegans
Function: Transcription factor which regulates the expression of genes involved in lipid metabolism and autophagy in response to nutrient availability, bacterial pore-forming toxins or heat shock. Binds to the E-box motif 5'-CACGTG-3'. Under fasting conditions, binds to the promoter and activates the expression of lipase genes lipl-2, lipl-3 and lipl-5, and to a lesser extent, lipl-1, thereby regulating lipolysis. Involved in modulating longevity in response to TOR signaling, dietary restriction, germline signaling, heat shock and the insulin-like signaling pathway. Involved in the immune response to infection by the S.aureus bacterium, probably acting downstream of the protein kinase dkf-1, leading to the transcriptional activation of host defense genes. May also play a role in lysosomal biogenesis in response to nutrient availability.
Subcellular location: Nucleus {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:28198373}. Cytoplasm {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:28198373, ECO:0000269|PubMed:34323215}. Note=Localization to nucleus enhanced during fasting and on mutant backgrounds involved in modulating longevity: glp-1, let-363 (tor), eat-2, daf-2, clk-1 or rsks-1 (PubMed:23604316, PubMed:23925298). Nuclear localization abolished on mml-1;glp-1 or mxl-2;glp-1 mutant backgrounds (PubMed:27001890). Localization to nucleus enhanced as a result of bacterial pore-forming toxin treatment, or heat shock (PubMed:27875098, PubMed:28198373). {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:23925298, ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27875098}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27184844}. Note=(Microbial infection) Localization to nucleus enriched rapidly after Staphylococcus aureus infection. {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27184844}.
Interaction partners:
- Forkhead box protein O
- Target of rapamycin homolog
- Protein lgg-1
- Protein mxl-3
- Defective pharyngeal development protein 4
- Lipase lipl-3
- Lipase lipl-1
- ZZ-type domain-containing protein
- Nuclear hormone receptor family member nhr-49
- Protein skinhead-1
Sequence:
MIRQLNSPGGGGGLGLNNPRAQQPPGAQQQQQPQQAQQQFYDDEPYQANASQFRFGAGKSMEQRRETGNLIPIAQRSMGSTSTPFGSAPTQSYFGGGSSGAALSSPRKMQQTHQMLFGNIQPPRGSPPSDGSDKIHRFGESPTPGGVGGVFGTELDDLIIDELMGMEDDQRMRPGATRPMTIGGEKTMSMARPIPGASSRAGSGHSGSPITIPNAMSNNFRQVVSSSAPTSSIDIEKMIGAVSNGGGNSGGDNDPEDYYRDRRKKDIHNMIERRRRYNINDRIKELGQMLPKNTSEDMKLNKGTILKASCDYIRVLQKDREQAMKTQQQQKSLESTAHKYADRVKELEEMLARQGVQVPPSHLPPIPKVIERPIKQEIDESPPNHTPTGSFVSSSGFLSEVTNNTAAMQITSPNDSRPNNFMNNSAPSDSFFSVGSASPPDYRTSSGTASWKLPGSNAFSDLMMDDLNPMMNGDPLISSAGAHPSPHFHSSQMSPDIHWDASGFSPDPINTQQSNSGHYHMDFS