wanglab/gogpt-training-data huggingface dataset:
Protein: 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (CMK) (EC 2.7.1.148) (4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase) (P62615)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. Phosphorylates isopentenyl phosphate at low rates. Also acts on isopentenol, and, much less efficiently, dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a substrate.
Interaction partners:
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 1-deoxy-D-xylulose-5-phosphate synthase
- Ribosomal RNA small subunit methyltransferase A
- Farnesyl diphosphate synthase
- Isopentenyl-diphosphate Delta-isomerase
- Outer-membrane lipoprotein LolB
Sequence:
MRTQWPSPAKLNLFLYITGQRADGYHTLQTLFQFLDYGDTISIELRDDGDIRLLTPVEGVEHEDNLIVRAARLLMKTAADSGRLPTGSGANISIDKRLPMGGGLGGGSSNAATVLVALNHLWQCGLSMDELAEMGLTLGADVPVFVRGHAAFAEGVGEILTPVDPPEKWYLVAHPGVSIPTPVIFKDPELPRNTPKRSIETLLKCEFSNDCEVIARKRFREVDAVLSWLLEYAPSRLTGTGACVFAEFDTESEARQVLEQAPEWLNGFVAKGANLSPLHRAML
Protein: Calpain catalytic domain-containing protein (Q387D8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNNTVGELALNLLRSDRDYLHLAPEGVPIEELPLEVDAKFCALEAERAMLKGENNPKNASMILSLEEKLNERARQLAQEQLLEDLKELSSFQHCVPLSLLSPHTDVQFAADVAEFRRLKKEGEQNTPAIQGVVGRLNARANELAEEYLRTDRASYLNPEQLGVPLDLLSLDTDSEFVSLEAERLKLLLDRDGYVSYINVLETRLNDRVRELCRLSLLDFPEFLLDVSNFGVPLEELCLFEDDGYRRHICSWYKLRRTPEVDNERISCEACIVEIVREKAKLYTEEILRSLPLVYRGIPLRDADLFRNDGFINSVKRFRRAVREKRDESEIVEAEDNMKNIAFDIIDGLILKERGSLDQEPEGISINNVPLDYDNAYLEMEAELHSLLKQQSMCEAASILQLRKAMNDRVHHLALIELAKMRTFLDPEIFGIPIKDLRLEGDMDFRNAEISRYKKLKNEANADVKDLEVLMTARALEVAKAFVARERAFLEPEPHGLLLEELLLDTHKVFTDLERERRVLLKEPGLCENTVKIKSLQDKMRAVVNELAVAYVAESRKFLDPAPEGVPLEELSLDSNELFIELEKRRFGLLREGKGDEGNLKDVEKSMQDCIRELAKGLLKENRAYLNQKPLGIPLDYLPLNNDKKLRELERKRRELLNTYDNDSPQVKSIEGVIIKRIDKIAARYLEGERSFLDPCPQTVPLRYLPLNADTNFCSLEQRRRELRRGGDTAEDDAMIKELEIRINDRAHELAKEVLHNGRLFLHPEILGVAVSDIPLSDHEPFVQLEEALRRIKVDNPINSFMEVDLREKLKQCARQVTEKMLDEERSFLDQNPLGIPLNSLMLNYDPKMQELERVRRKKLRDKVDANEEEREMVRRVNEMAEEELRRQRMYLPATPLGIPFQYLGLDSDGKFGQMENFLRTLKRDPLSKEKAIRDQENANRQYVFRTAAEYKRRERAYLNPEPNGVSLKRLSLDTDPKFQKLEQMRRMLMHSSDSNDAQIGHLEHLANEYVLQLALQQLGWQDAEFHDRNRHLADDWVRISELYPEGKYVPFEPTKANGCSVVSAPNDASYLAPFIAALSRCPDMLRQLCDTTSHPVNGPYSFIFFDPNSNPVRVDIDDRVPVDAKCEPKFTRVPHRSWYPLLLEKAYAKFVGGYAKLDQCTPHETLRDLTGRPVLHIPFDDRLADAANTGDFRSVKFWKGIKRNLAAGDVITCISNHESVDGLHSQCSYALLSVIETVHESNDVSDIVIKLHNCYYDSPTYDGPLCNDDDNWTDGLKRLCHYNPEEDALYIPVPVFLRNFSSMQRCHINCGDRLTAPGEWTGVSCGGNPKFTTFRNNPIYLVENKTSRPVTILAELRHHAPAYRDPDDVNHYHQSGLALLKAINTRMPVSPILTSVTHRFLHRGMMLDAREVCAQMELPPSTTCYLVPYTLGRENYGKFHISVYPGLAKVNLAPLRTAALFASPVVISMSLKTELRNGVKVEFVVSRACDAHVLLCQRRPKVIDVCKSDLLGDFSVNMAVYDENGILLMNTGEPRNAREVAVSFRVPQQGLYSAVIMALGVDRRGNHRGCPCHLTIFTSKKAKVRLLGTVPNFPRRATPRTSIRSQSAEIMTPVSLTPRDGPKTAGSFHLPYISGGQSTTDSPFVMGIK
Protein: Immunomodulating metalloprotease (EC 3.4.24.-) (IMPa) (Q9I5W4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Protease that degrades several proteins of the host immune system. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1), leading to its functional inhibition; PSGL-1 is a leukocyte cell-surface receptor essential for leukocyte recruitment to the site of infection. Next to PSGL-1, targets host CD43 and CD44 that are also involved in leukocyte homing. Thus, prevents neutrophil extravasation and thereby protects P.aeruginosa from neutrophil attack. Is also able to inhibit the decay accelerating factor (CD55), but not the cell-surface receptors CD46 and CD31.
Subcellular location: Secreted {ECO:0000269|PubMed:22309196}.
Interaction partners:
- Chitin-binding protein CbpD
- Peroxiredoxin
- Serralysin
- Lysyl endopeptidase
- Aminopeptidase
- Elastase
- Probable hydrolase
- Protease LasA
Sequence:
MSLSTTAFPSLQGENMSRSPIPRHRALLAGFCLAGALSAQAATQEEILDAALVSGDSSQLTDSHLVALRLQQQVERIRQTRTQLLDGLYQNLSQAYDPGAASMWVLPANPDNTLPFLIGDKGRVLASLSLEAGGRGLAYGTNVLTQLSGTNAAHAPLLKRAVQWLVNGDPGAATAKDFKVSVVGVDKTAALNGLKSAGLQPADAACNALTDASCASTSKLLVLGNGASAASLSATVRARLQAGLPILFVHTNGWNQSSTGQQILAGLGLQEGPYGGNYWDKDRVPSSRTRTRSVELGGAYGQDPALVQQIVDGSWRTDYDWSKCTSYVGRTTCDDVPGLSDFSKRVDVLKGALDAYNQKAQNLFALPGTTSLRLWLLWADAVRQNIRYPMDKAADTARFQETFVADAIVGYVREAGAAQKELGSYAGQRQQSMPVSGSEETLTLTLPSAQGFTAIGRMAAPGKRLSIRIEDAGQASLAVGLNTQRIGSTRLWNTRQYDRPRFLKSPDIKLQANQSVALVSPYGGLLQLVYSGATPGQTVTVKVTGAASQPFLDIQPGEDSSQAIADFIQALDADKADWLEIRSGSVEVHAKVEKVRGSIDKDYGGDVQRFIRELNEVFIDDAYTLAGFAIPNQAKTPAIQQECAARGWDCDSETLHKLPGTQHINVDQYAQCGGGCSGNPYDQTWGLNPRGWGESHELGHNLQVNRLKVYGGRSGEISNQIFPLHKDWRVLREFGQNLDDTRVNYRNAYNLIVAGRAEADPLAGVYKRLWEDPGTYALNGERMAFYTQWVHYWADLKNDPLQGWDIWTLLYLHQRQVDKSDWDANKAALGYGTYAQRPGNSGDASSTDGNDNLLLGLSWLTQRDQRPTFALWGIRTSAAAQAQVAAYGFAEQPAFFYANNRTNEYSTVKLLDMSQGSPAWPFP
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (Q9HXM5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Bifunctional purine biosynthesis protein PurH
- Probable purine/pyrimidine phosphoribosyl transferase
- Xanthine phosphoribosyltransferase
- Amidophosphoribosyltransferase
- dITP/XTP pyrophosphatase
- 5'-nucleotidase SurE
- Phosphoribosylformylglycinamidine cyclo-ligase
- Adenylosuccinate lyase
Sequence:
MLRISQEALTFDDVLLIPGYSEVLPKDVSLKTRLTRGIELNIPLVSAAMDTVTEARLAIAMAQEGGIGIIHKNMGIEQQAAEVRKVKKHETAIVRDPVTVTPSTKIIELLQMAREYGFSGFPVVEQGELVGIVTGRDLRVKPNAGDTVAAIMTPKDKLVTAREGTPLEEMKAKLYENRIEKMLVVDENFYLRGLVTFRDIEKAKTYPLASKDEQGRLRVGAAVGTGADTGERVAALVAAGVDVVVVDTAHGHSKGVIERVRWVKQTFPDVQVIGGNIATAEAAKALAEAGADAVKVGIGPGSICTTRIVAGVGVPQISAIANVAAALEGTGVPLIADGGIRFSGDLAKAMVAGAYCVMMGSMFAGTEEAPGEIELFQGRSYKSYRGMGSLGAMSGSQGSSDRYFQDASAGAEKLVPEGIEGRVPYKGALSAIVHQLMGGLRAAMGYTGSADIQQMRTQPQFVRITGAGMAESHVHDVQITKEAPNYRVG
Protein: 5''-phosphoribostamycin phosphatase (EC 3.1.3.88) (Butirosin biosynthesis protein P) (Q4H4E4)
Organism: Niallia circulans (Bacillus circulans)
Function: Catalyzes dephosphorylation of 5''-phosphoribostamycin to generate ribostamycinin the biosynthetic pathway of butirosin.
Interaction partners:
Sequence:
MRLILIRHAQARCNILEDDALMDAYDPHCELTEAGIGQAVKLRDEYPVSLTPSVIYSSPLKRARETAGIFRGRYPSVPFVEDERLSELKAPESFIPPITQGQWDLYLEQRIRSPHLEIVKGLESLDVQRERIERFYKDLFRKYAEEACNIVIFTHAFSIQLSILFFLGLGNEQLLQWQIKASNTAMHIIHYDPTSGSFLLESLNNRSHLQTTG
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (Q9TUB2)
Organism: Sus scrofa (Pig)
Function: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}.
Interaction partners:
- E3 ubiquitin-protein ligase Mdm2
- Protein Mdm4
- histone acetyltransferase
- Serine-protein kinase ATM
- histone acetyltransferase
- protein acetyllysine N-acetyltransferase
- Ubiquitin carboxyl-terminal hydrolase 7
- Bcl-2-like protein 1
- Cyclin-dependent kinase inhibitor 1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MEESQSELGVEPPLSQETFSDLWKLLPENNLLSSELSLAAVNDLLLSPVTNWLDENPDDASRVPAPPAATAPAPAAPAPATSWPLSSFVPSQKTYPGSYDFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTCPVQLWVSSPPPPGTRVRAMAIYKKSEYMTEVVRRCPHHERSSDYSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPILTIITLEDASGNLLGRNSFEVRVCACPGRDRRTEEENFLKKGQSCPEPPPGSTKRALPTSTSSSPVQKKKPLDGEYFTLQIRGRERFEMFRELNDALELKDAQTARESGENRAHSSHLKSKKGQSPSRHKKPMFKREGPDSD
Protein: Probable succinate dehydrogenase [iron-sulfur subunit] (Succinic dehydrogenase) (O53669)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Succinate dehydrogenase 2 membrane subunit SdhC
- Probable succinate dehydrogenase [membrane anchor subunit]
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Probable succinate dehydrogenase SdhD
- Succinate dehydrogenase flavoprotein subunit
- Fumarate reductase flavoprotein subunit
- Fumarate reductase subunit C
- Fumarate reductase subunit D
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
Sequence:
MTYSASMRVWRGDESCGELREFTVEVNEGEVVLDVILRLQQTQTPDLAVRWNCKAGKCGSCSAEINGKPRLMCMTRMSTFDEDEIVTVTPMRTFPVIRDLVTDVSFNYQKAREIPSFAPPKELQPSEYRMAQVDVARSQEFRKCIECFLCQNVCHVVRDHEENKDAFAGPRFLMRIAELEMHPLDTRDRRSQAQEEHGLGYCNITKCCTEVCPENIKITDNALIPMKERVADRKYDPVVWLGSKLFRR
Protein: Vomeronasal 2, receptor 65 (G3X931)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Vomeronasal type-1 receptor
Sequence:
MLSFMSFFLILEYFLLLSVAHPKCFWRIKQNENKVGDVEDNCFFYIYTRQGPLLNDPFNGNPDILLTTRNIHLILALLFAIKQINRNIHILPNISLIVNVNCAKKEDLQMTNMYSNRDATIPNYNCKHGRRILTVLTGPRWFSSAILGPFLHIFAIPQLYYGPFHPLLSDREHYPYLYQMSPKNTFLTLAMTALVVYFSWNWVGLVISDDELGIEFLFKLRGEMHKHKVCIAFVNMIIQNIQLYQKRAEKYYNQILTSSAKVIIIYGDSDILTVHFRLWQHLGIKRLWITTSHWDENTSKGDLLLSSFNGIFIFSHPHSKIPGFKKFIQTVHPSNYSKDTSLARLWWLYFNCSLPSHCKTLKNCSTKILLEWLSRHQFEVSMSEPSYNLYNAVYAVAYALHEMLIQHTEHWQKDIGKELEFYSWKVAPFLENNKFIIPSEYQYRRGKLDTEYDILYAMDLLPALGLNVKIGKFSQHFLHFQQLYIAEDMIDWTIDIRQTLQSVCSVPCSVGFRKFIQKGKAVCCFDCTPCPENEISNMTDMDQCVKCPNDQYANIKQTHCLKKVVTFLAYEDPLGMTLTCLALLFSALTTVILSILLKHQDNPIVKANNRLLSYILLISLIFCFLCSLLYIGHPHMATCILQQTTFAVVFTVAVSTILAKTITVVMAFKITDPRKKIRQMLVTRAPNYIIPICTMIQLILCGTWIGTSPPFVDSDPHFEHGHIIIVCNKGSVIAFYCVLGYLGLLALGSFTVAFLARNLPDRFNEAKFLTFSMLVFCSVWITFLPVYHSTKGKAMVVVEIFSILTSSAGLLVCIFFPKCFTILLKQKVNFTQKFSDTHSKIEYNH
Protein: AP-4 complex accessory subunit Tepsin (ENTH domain-containing protein 2) (Epsin for AP-4) (Tetra-epsin) (Q96N21)
Organism: Homo sapiens (Human)
Function: Associates with the adapter-like complex 4 (AP-4) and may therefore play a role in vesicular trafficking of proteins at the trans-Golgi network.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:26542808, ECO:0000269|PubMed:26756312}; Peripheral membrane protein {ECO:0000269|PubMed:26756312}. Cytoplasmic vesicle {ECO:0000269|PubMed:22472443}. Cytoplasm, cytosol {ECO:0000269|PubMed:22472443}. Note=Extensively colocalizes with AP-4 which mediates the recruitment of TEPSIN to the trans-Golgi network. {ECO:0000269|PubMed:22472443, ECO:0000269|PubMed:26542808}.
Interaction partners:
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit sigma-1
- AP-4 complex subunit mu-1
- AP-4 complex subunit beta-1
Sequence:
MAAAPPLRDRLSFLHRLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRTAVRHQPGQAGGGWDELDSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSGASREPGDLAERVEVVALSDCQQELSLVRTVTRGPRAFLSREEAQHFIKACGLLNCEAVLQLLTCHLRGTSECTQLRALCAIASLGSSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPSEAEARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPGSEPSAFAFLNA
Protein: Sentrin-specific protease 8 (EC 3.4.22.-) (Deneddylase-1) (NEDD8-specific protease 1) (Protease, cysteine 2) (Sentrin/SUMO-specific protease SENP8) (Q96LD8)
Organism: Homo sapiens (Human)
Function: Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53.
Interaction partners:
- Ubiquitin-like protein NEDD8
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- Iron-responsive element-binding protein 2
- Cullin-1
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- NEDD8-activating enzyme E1 catalytic subunit
- Sentrin-specific protease 3
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- NEDD8-activating enzyme E1 regulatory subunit
Sequence:
MDPVVLSYMDSLLRQSDVSLLDPPSWLNDHIIGFAFEYFANSQFHDCSDHVSFISPEVTQFIKCTSNPAEIAMFLEPLDLPNKRVVFLAINDNSNQAAGGTHWSLLVYLQDKNSFFHYDSHSRSNSVHAKQVAEKLEAFLGRKGDKLAFVEEKAPAQQNSYDCGMYVICNTEALCQNFFRQQTESLLQLLTPAYITKKRGEWKDLITTLAKK
Protein: CD163 molecule (A0A8I5ZQF0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGMDRLEIILQFHMSYKGFVHLGFFVVAVSSLLSVSAVTQAPEGRKKELRLAGGENNCSGRVELKIHEKWGTVCGNGWSMNEVSVVCQQLGCPTLIKAPGWANASAGSGDIWMDKVSCTGNESALWDCKHEGWGKHNCTHEQDAGVTCADGSNLEMRLVNSGDNRCSGRVEIKFQGKWGTVCDDNFSKDHASVICKQLGCGSAISFSGSAKLGAGSGQIWLDDLACNGNESAIWDCKHRGWGRHNCDHAEDVGVICLDGADLSLRLVDGVSKCSGRLEVRFQGEWGTVCDDSWDRRDASVVCKQLGCPTAITAIGRVNASEGSGPIWLDSISCEGHEPALWECKHQEWGKHYCNHKEDAGVTCSDGADLELRLVGGGSRCAGMVEVEIQKLTGKVCSRGWTLTDADVVCRQLGCGSALQTQSKIYSKTKTEATNTWLFPGSCSGNETSLWQCKNWQWGGLSCDHFEEAQVTCSGHRKPRLVGGEIPCSGRVEVKHGDTWGSVCDFDLSLEAAGVVCRELQCGTVVSILGGAHFGEGSGQIWGEEFQCSGDESHLSLCSVAPPLDRTCSHSRDVSIVCSRYIDIRLADGKSSCEGRVELKTLGAWGPLCSSHWDIEDAHVLCQQLKCGVALSTPGGAHFGKGAGQVWRHKFHCTGTEEHIGDCPMTALGTPMCSDGQVASVICSGNQSHTLLPCSSSSSVQTTSSTIAKDSDVPCIASGQLRLVGGGGRCAGRVEVYHEGSWGTICDDSWDLTDANVVCKQLDCGVAINATGSAYFGEGTGDIWLDEIDCSGKESHIWQCHSHGWGRHNCRHKEDAGVVCSEFMSLRLTNEAHRVNCTGRLEVFYNGTWGSIGSSNMSPTTVGVVCRQLGCADNGTVKPTSSDKTPTRPMWTDSVQCPKGVDTLWQCPSSPWKQRQASPSQESWIVCDDKIRLQEGHTDCSGRVEIWHRGSWGTVCDDSWDLNDAEVACKQLGCGQAVEALKEAAFGPGTGPIWLNEMKCRGNESSLWDCPARPWSHSDCGHKEDASVKCLPRMTLESQHGTGHSTLTALLVCGAILLVLLIAFLLWTLKRRQTQRLTVSSRGEVLIHQVQYQEMDSKTDDLDLLKSSGQ
Protein: Parathyroid hormone 4 (A0A1L2F565)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Neuroendocrine peptide which is produced by a subset of neurons in the hypothalamus. Activates the G-protein coupled receptors pth1ra, pth1rb and pth2r with similar affinity. Receptor binding stimulates intracellular cAMP production. Plays a role in bone mineralization by regulating expression of factors involved in phosphate homeostasis. Important for embryonic bone development.
Subcellular location: Secreted {ECO:0000305|PubMed:28148780}.
Interaction partners:
- Parathyroid hormone
Sequence:
MLKMQRSQQRVALMMLMVVAAVHCQESESRRAVTEHQLMHDRGRSIQSLKRLIWLSSAIEGLHTAQARTLEPDSRWRSRGAQLYSQPGREESSGGQKRALETLLSDLYRAHLTFGLGEPEK
Protein: Delayed-rectifier potassium channel regulatory subunit KCNS3 (Delayed-rectifier K(+) channel alpha subunit 3) (Delayed-rectifier potassium channel subunit Kv9.3) (Kv9.3) (Potassium voltage-gated channel subfamily S member 3) (Q9BQ31)
Organism: Homo sapiens (Human)
Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. Heterotetrameric channel activity formed with KCNB1 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:10484328}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 (PubMed:10484328). {ECO:0000269|PubMed:10484328}.
Interaction partners:
- Potassium voltage-gated channel subfamily B member 1
- Ubiquitin-like protein FUBI
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-3
- Voltage-gated potassium channel subunit beta-2
- Potassium voltage-gated channel subfamily A member 2
Sequence:
MVFGEFFHRPGQDEELVNLNVGGFKQSVDQSTLLRFPHTRLGKLLTCHSEEAILELCDDYSVADKEYYFDRNPSLFRYVLNFYYTGKLHVMEELCVFSFCQEIEYWGINELFIDSCCSNRYQERKEENHEKDWDQKSHDVSTDSSFEESSLFEKELEKFDTLRFGQLRKKIWIRMENPAYCLSAKLIAISSLSVVLASIVAMCVHSMSEFQNEDGEVDDPVLEGVEIACIAWFTGELAVRLAAAPCQKKFWKNPLNIIDFVSIIPFYATLAVDTKEEESEDIENMGKVVQILRLMRIFRILKLARHSVGLRSLGATLRHSYHEVGLLLLFLSVGISIFSVLIYSVEKDDHTSSLTSIPICWWWATISMTTVGYGDTHPVTLAGKLIASTCIICGILVVALPITIIFNKFSKYYQKQKDIDVDQCSEDAPEKCHELPYFNIRDIYAQRMHTFITSLSSVGIVVSDPDSTDASSIEDNEDICNTTSLENCTAK
Protein: Peptidyl-prolyl cis-trans isomerase E (PPIase E) (EC 5.2.1.8) (Cyclophilin E) (Cyclophilin-33) (Rotamase E) (Q9UNP9)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:8977107}.
Interaction partners:
- RNA helicase aquarius
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-processing factor 19
- Crooked neck-like protein 1
- SNW domain-containing protein 1
- Protein BUD31 homolog
- Pre-mRNA-splicing factor SYF2
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SPF27
- Pre-mRNA-splicing factor RBM22
Sequence:
MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKAETQEGEPIAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIEAQGSKDGKPKQKVIIADCGEYV
Protein: Glyoxalase ElbB (EC 4.2.1.-) (Sigma cross-reacting protein 27A) (SCRP-27A) (P0ABU5)
Organism: Escherichia coli (strain K12)
Function: Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate. However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate.
Interaction partners:
- Protein/nucleic acid deglycase 2
- Biosynthetic peptidoglycan transglycosylase
- Protein/nucleic acid deglycase 1
- Protein/nucleic acid deglycase 3
Sequence:
MKKIGVILSGCGVYDGSEIHEAVLTLLAISRSGAQAVCFAPDKQQVDVINHLTGEAMTETRNVLIEAARITRGEIRPLAQADAAELDALIVPGGFGAAKNLSNFASLGSECTVDRELKALAQAMHQAGKPLGFMCIAPAMLPKIFDFPLRLTIGTDIDTAEVLEEMGAEHVPCPVDDIVVDEDNKIVTTPAYMLAQNIAEAASGIDKLVSRVLVLAE
Protein: Protein S100 (S100 calcium-binding protein) (Q5T7Y6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00004369}.
Interaction partners:
Sequence:
MEEPQTKTPSAEFPPYRAQPAQPATAPAATFATLAICPEPAPTSGPGQPCTAAMGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
Protein: SNF4/AMP-activated protein kinase gamma subunit, isoform I (Q0KI34)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLQLHFYSNHAGRLVLGGGNRRPTDVLCYPLESIKEFEQISEAWKRLLAELLKKEEDDSQIFVKFFRFHKCYDLIPTSAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFIKILQMYYKSPNASMEQLEEHKLDTWRSVLHNQVMPLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKSLRELKIGTYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEWFEGVQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRPSGEGVGGSESSLRASDPVLLRKVAEVEIPATAAAATTTTPPRSPSAGSGNRSLIEDIPEEETAPARSDDADSDNNKSASEDKANNNQHDQTTTAATANGDSNNSPVEVSFADEAQEEEAADQVERSNCDDDDQPALAEIERKNASMDDDEDDGMSSAVSAASALGQSLTPAAQEMALVSE
Protein: TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L) (PCAF-associated factor 65-alpha) (PAF65-alpha) (Q8R2K4)
Organism: Mus musculus (Mouse)
Function: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (By similarity). With TAF5L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state. Functions with MYC to activate target gene expression through RNA polymerase II pause release.
Subcellular location: Nucleus {ECO:0000269|PubMed:31005419}.
Interaction partners:
- TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L
- Transcription initiation factor TFIID subunit 10
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 12
- STAGA complex 65 subunit gamma
- Transcription factor SPT20 homolog
- SPT3, SAGA and STAGA complex component
- SAGA-associated factor 29
- Transcriptional adapter 1
- Transformation/transcription domain-associated protein
Sequence:
MSEREERRFVEIPRESVRLMAESTGLELSDEVAALLAEDVCYRLREATQNSSQFMKHTKRRKLTVEDFNRALRWSSVEAVCGYGSQEALPLRPAREGDLYFPEDREVSLVELALATNIPKGCAETAVRVHVSYLDGKGNLAPQGSVPSAVSSLTDDLLKYYQQVTRAVLGDDPQLMKVALQDLQTNSKIAALLPYFVYVVSGVKSVSHDLEQLHRLLQVARSLIRNPHLCLGPYVRSLVGSVLYCVLEPLAASINPLNDHWTLRDGAALLLSHIFWTHGDLVSGLYQQILLSLQKVLTDPVRPLCSHYGAVVGLHALGWKAVERVLYPHLPTYWTNLQAVLDDYSVSNAQVKADGHKVYGAILVAVERLLKMKAQAAEPNRGGLGGRGYRPAEDLPWDSLLLQESPPGGSSETGFGSGLPPPSGVAGPEDPSSLTLADIYRELYSFFGDSLATRFGTGQPAPTAPRPPGDKKEPAAAPDSVRKMPQLTASAVVSPQGDESPCGGTLATATAASESRPLPRVHRARGAPRQQGPGAGTRDVFQKSRFAPRGAPHFRFIIAGRQAGRRCRGRLFQTAFPAPYGPSPASRYVQKLPMIGRTGRPARRWALSDYSLYLPL
Protein: N-acetylgalactosaminide beta-1,3-galactosyltransferase (EC 2.4.1.122) (Q7JRF9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- N-acetylgalactosaminyltransferase 4
- Polypeptide N-acetylgalactosaminyltransferase 3
- Putative polypeptide N-acetylgalactosaminyltransferase 9
- Protein Lilipod
- Mucin 30E
Sequence:
MTSASLLSRSLLTEAPRSKNRSVFTLIAGLVVGYCLAQIFSSIAPHESLYPYLSRRFSDSQVATGGQLAPEQSGLKHDHRNDNVSVAEQLKKEVRILCWVMTNPTNHKKKARHVKRTWGKRCNILLFMSSGADEELPTVKLDVGEGRENLWAKVKEAFKYVYHHHYNDADFFYKADDDTYAVIENMRYMLYPYNPETPVHFGFKFKPFVKQGYMSGGAGYILSREALRRFVVEGIPNPKMCLPGTVVNEDIEIGRCMENLNVTAGDSRDEIGRGRMFPFIPEHHLIPAKADKNFWYWNYLYYKTDDGLDCCSDLAISFHYVAPNSFYVLDYLIYHLKPYGLLRSLEPLPAKLKVGQFLPPPVEARGRLASNEDSADDYDRIYTTTTEKPKEPDAREMDSKEVEKEDAKYREKLSKEDEEREDSRKTDNDSEYTEEETEKRSKSKETSKEN