wanglab/gogpt-training-data huggingface dataset:
Protein: Inactive phospholipase C-like protein 1 (PLC-L1) (PRIP1) (Phospholipase C-related but catalytically inactive protein) (p130) (Q62688)
Organism: Rattus norvegicus (Rat)
Function: Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor. Acts as an inhibitor of PPP1C.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11278544, ECO:0000269|PubMed:8546702}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit epsilon
- Gamma-aminobutyric acid receptor subunit alpha-5
- Gamma-aminobutyric acid receptor subunit gamma-1
- Gamma-aminobutyric acid receptor subunit alpha-2
- Gamma-aminobutyric acid receptor subunit delta
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit alpha-4
- Gamma-aminobutyric acid receptor subunit gamma-3
Sequence:
MAEGAASREAPAPLDVAGGEDDPRAGADAASGDAAPEASGGRMRDRRSGVALPGNAGVPADSEAGLLEAARATPRRTSIIKDPSNQKCGGRKKTVSFSSMPSEKKISSAHDCISFMQAGCELKKVRPNSRIYNRFFTLDTDLQALRWEPSKKDLEKAKLDISAIKEIRLGKNTETFRNNGLADQICEDCAFSILHGENYESLDLVANSADVANIWVSGLRYLVSRSKQPLDFMEGNQNTPRFMWLKTVFEAADVDGNGIMLEDTSVELIKQLNPTLKESKIRLKFKEIQKSKEKLTTRVTEEEFCEAFCELCTRPEVYFLLVQISKNKEYLDANDLMLFLEVEQGVTHVTEDMCLDIIRRYELSEDGRQKGFLAIDGFTQYLLSPECDIFDPEQKKVAQDMTQPLSHYYINASHNTYLIEDQFRGPADINGYVRALKMGCRSIELDVSDGPDNEPILCNRNNMAMLLSFRSVLEVINKFAFVASEYPLILCLGNHCSLPQQRVMVQQMKKVFGNKLYTEAPLSSESYLPSPEKLKHMIIVKGKKLPSESDLLEGEVTDEDEEAEMSRRVSGDYNGEQKHIWLCRELSDLVSICKSVQYRDFELSMKTQNYWEICSFSETLASRIANEYPEDFVNYNKKFLSRVYPSAMRIDSSNLNPQDFWNCGCQIVAMNFQTPGPMMDLHTGWFLQNGGCGYVLRPSIMRDEVSYFSANTKGIVPGVSPLLLHIKIISGQNFPKPKGACAKGDVIDPYVCVEIHGIPADCSEQRTKTVQQNSDNPIFDETFEFQVNLPELTMVRFVILDDDYIGDEFIGQYTIPFECLQPGYRHVPLRSFVGDIMEHVTLFVHIAITNRSGGGKAQKRSLSVRMGKKVREYTMLRNIGLKTIDDIFKIAVHPLREAIDMRENMQNAIVSVKELCGLPPIASLKQCLLTLSSRLITSDSTPSVSLVMKDCFPYLEPLGTIPDVQKRMLAAYDLMIQESRVLIEMADTVQEKIVQCQKAGMEFHEELHNLGAKEGLKGRKLNKAIESFAWNITVLKGQGDLLKNAKNEAVENIKQIQLACLSCGLSKGPGSAAEAKGKRSLEAIEEKESSEENGKL
Protein: Forkhead box protein D1 (Brain factor 2) (BF-2) (Forkhead-related protein FKHL8) (Forkhead-related transcription factor 4) (FREAC-4) (HFH-BF-2) (Q61345)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in regulation of gene expression in a variety of processes including formation of positional identity in the developing retina, regionalization of the optic chiasm, morphogenesis of the kidney, and neuralization of ectodermal cells. Involved in transcriptional activation of PGF and C3 genes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Homeobox protein SIX2
- Forkhead box protein C2
Sequence:
MTLSTEMSDASGLAEETDIDVVGEGEDDEEEEDDDDEGGGGRGGGGSRLPSSAQRRRRSYAGEDDLEDLEEEDDDDLLLASRPAASPAPPGPAPAPGTGSGGCSGAGAGGGAGGGTGAGTGGGAKNPLVKPPYSYIALITMAILQSPKKRLTLSEICEFISSRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQPLLAPHAAAEALLLRGAGPAAGAGDPGAALFPPPPPPPACGYGAYGCAYGLQLPPCAPPSALFAAAAAAAAAAFHPHSPPPPPPPPPPPPGAAAELARTAFGYRSHALAAALPGPLQAAAVKAGGPGAAALARSPFSIESLIGRTRGPAAAGAHVSSGAASGTAPGPGGGGCAVQAAAGPAVALTRSLVVAAAAAASSVSSSAALGTLHQGTALSSVENFTARISNC
Protein: Solute carrier family 12 member 5 (Electroneutral potassium-chloride cotransporter 2) (K-Cl cotransporter 2) (mKCC2) (Neuronal K-Cl cotransporter) (Q91V14)
Organism: Mus musculus (Mouse)
Function: Mediates electroneutral potassium-chloride cotransport in mature neurons and is required for neuronal Cl(-) homeostasis (By similarity). As major extruder of intracellular chloride, it establishes the low neuronal Cl(-) levels required for chloride influx after binding of GABA-A and glycine to their receptors, with subsequent hyperpolarization and neuronal inhibition (By similarity). Involved in the regulation of dendritic spine formation and maturation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11395011}; Multi-pass membrane protein {ECO:0000269|PubMed:11395011, ECO:0000269|PubMed:33597714}. Cell projection, dendrite {ECO:0000269|PubMed:11395011}. Note=Detected on dendrites, but not on axons of spinal cord neurons and at GPHN-positive inhibitory synapses. {ECO:0000269|PubMed:11395011}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit gamma-2
- Neuropilin and tolloid-like protein 2
- STE20/SPS1-related proline-alanine-rich protein kinase
- Gamma-aminobutyric acid receptor subunit alpha-1
- BDNF/NT-3 growth factors receptor
- Serine/threonine-protein kinase WNK3
- Neurotrophic factor BDNF precursor form
- Glutamate decarboxylase 1
- Vesicular inhibitory amino acid transporter
- Glutamate decarboxylase 2
Sequence:
MSRRFTVTSLPPAASAASADPESRRHSVADPRRLPREDVKGDGNPKESSPFINSTDTEKGREYDGRNMALFEEEMDTSPMVSSLLSGLANYTNLPQGSREHEEAENNEGGKKKPVQAPRMGTFMGVYLPCLQNIFGVILFLRLTWVVGIAGIMESFCMVFICCSCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEILLAYLFPAMAIFKAEDASGEAAAMLNNMRVYGTCVLTCMATVVFVGVKYVNKFALVFLGCVILSILAIYAGVIKSAFDPPNFPICLLGNRTLSRHGFDVCAKLAWEGNETVTTRLWGLFCSSRLLNATCDEYFTRNNVTEIQGIPGAASGLIKENLWSSYLTKGVIVERRGMPSVGLADGTPVDMDHPYVFSDMTSYFTLLVGIYFPSVTGIMAGSNRSGDLRDAQKSIPTGTILAIATTSAVYISSVVLFGACIEGVVLRDKFGEAVNGNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAISRDGIVPFLQVFGHGKANGEPTWALLLTACICEIGILIASLDEVAPILSMFFLMCYMFVNLACAVQTLLRTPNWRPRFRYYHWTLSFLGMSLCLALMFICSWYYALVAMLIAGLIYKYIEYRGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLVRVDQDQNVVHPQLLSLTSQLKAGKGLTIVGSVLEGTFLDNHPQAQRAEESIRRLMEAEKVKGFCQVVISSNLRDGVSHLIQSGGLGGLQHNTVLVGWPRNWRQKEDHQTWRNFIELVRETTAGHLALLVTKNVSMFPGNPERFSEGSIDVWWIVHDGGMLMLLPFLLRHHKVWRKCKMRIFTVAQMDDNSIQMKKDLTTFLYHLRITAEVEVVEMHESDISAYTYEKTLVMEQRSQILKQMHLTKNEREREIQSITDESRGSIRRKNPANPRLRLNVPEETACDNEEKPEEEVQLIHDQSAPSCPSSSPSPGEEPEGERETDPEVHLTWTKDKSVAEKNKGPSPVSSEGIKDFFSMKPEWENLNQSNVRRMHTAVRLNEVIVNKSRDAKLVLLNMPGPPRNRNGDENYMEFLEVLTEQLDRVMLVRGGGREVITIYS
Protein: COP9 signalosome complex subunit 1 (SGN1) (Signalosome subunit 1) (G protein pathway suppressor 1) (GPS-1) (JAB1-containing signalosome subunit 1) (Protein MFH) (Q13098)
Organism: Homo sapiens (Human)
Function: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:9535219}.
Interaction partners:
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 7b
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 6
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
Sequence:
MPLPVQVFNLQGAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLRELQNAPDAIPESGVEPPALDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCLLLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMMLRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM
Protein: m-AAA protease-interacting protein 1, mitochondrial (Matrix AAA peptidase-interacting protein 1) (Q8WWC4)
Organism: Homo sapiens (Human)
Function: Promotes sorting of SMDT1/EMRE in mitochondria by ensuring its maturation. Interacts with the transit peptide region of SMDT1/EMRE precursor protein in the mitochondrial matrix, leading to protect it against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:27642048}.
Interaction partners:
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Prohibitin 1
- Essential MCU regulator, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Prohibitin-2
Sequence:
MALAARLLPQFLHSRSLPCGAVRLRTPAVAEVRLPSATLCYFCRCRLGLGAALFPRSARALAASALPAQGSRWPVLSSPGLPAAFASFPACPQRSYSTEEKPQQHQKTKMIVLGFSNPINWVRTRIKAFLIWAYFDKEFSITEFSEGAKQAFAHVSKLLSQCKFDLLEELVAKEVLHALKEKVTSLPDNHKNALAANIDEIVFTSTGDISIYYDEKGRKFVNILMCFWYLTSANIPSETLRGASVFQVKLGNQNVETKQLLSASYEFQREFTQGVKPDWTIARIEHSKLLE
Protein: Vanadate resistance protein (Q00314)
Organism: Candida albicans (Yeast)
Interaction partners:
Sequence:
MFLLVTYTIYSRVLTGDSRIPQSQDRQQSPTNDNNHEVYKVTKDGVYKQEVTGVVEEVEEEELKEVTTEDLYKSNVDIFDLNDYQGSQEGAKNGDILLFLMPLRNAEHVLPMAFYNLMNLTYDHRLIDIAFLVSDCSPDDTTLETVFEYSVALQNGTLVDKLKHEEELKNSGNVRGTSDLYQSYMEPSYIESVKKAYSNPESHHPNYRTPFRSVTIFKKDFGQVIGQGFSDRHAVKVQGIRRKLMGRARNWLTSAALKPYHSWVYWRDADIETCPGDVIEELMSHNYDVMVPNVWRPLPTFLGNEQPYDLNSWVESDAGLELAKTLNEDDVIVEGYAEYPTWRAHLAYIRDANGDPREVIDLDGVGGVSILARAKIFRQGVHFPAFTFLNHAETEAFGKMAKKMGFSVGGLPHYTIWHIYEPSEDDLKEIARLERKKRRQKS
Protein: Calcium channel, voltage-dependent, alpha 1I subunit (F6V0N5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XPRMPTSSPGAPGRGSGGAGVGGDTESHLCRHCYSPAQETLWLDSVSLIIKDSLEGELTIIDNLSGSIFHHYSSPAGCDKCHHDKQEGPVAQRSRPRLPHPSPRVTRGHHLPPQVQLAETEAFSLNSDRSSSVLLGDDLSLEDPTACPQGPKESKGELEPPEPMQAGDLDECFFPFAGEPVSAGPESLLCEMGAIPFNPVQSWLKHESNQAPPSPFSPDGSSPLLQMPAEFFHPAVSASQKGQEPGMSSGTLPKIALQGS
Protein: RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) (Killer toxin-resistance protein 33) (Ribosomal RNA cytidine acetyltransferase 1) (P53914)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) at positions 1280 and 1773 in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C at position 12 in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-rRNA-processing protein PNO1
- rRNA biogenesis protein RRP5
- Nucleolar protein 56
- Ribosome biogenesis protein BMS1
- U3 small nucleolar RNA-associated protein 15
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 21
- Protein BFR2
- U3 small nucleolar RNA-associated protein 22
- Nucleolar complex protein 4
Sequence:
MAKKAIDSRIPSLIRNGVQTKQRSIFVIVGDRARNQLPNLHYLMMSADLKMNKSVLWAYKKKLLGFTSHRKKRENKIKKEIKRGTREVNEMDPFESFISNQNIRYVYYKESEKILGNTYGMCILQDFEALTPNLLARTIETVEGGGIVVILLKSMSSLKQLYTMTMDVHARYRTEAHGDVVARFNERFILSLGSNPNCLVVDDELNVLPLSGAKNVKPLPPKEDDELPPKQLELQELKESLEDVQPAGSLVSLSKTVNQAHAILSFIDAISEKTLNFTVALTAGRGRGKSAALGISIAAAVSHGYSNIFVTSPSPENLKTLFEFIFKGFDALGYQEHIDYDIIQSTNPDFNKAIVRVDIKRDHRQTIQYIVPQDHQVLGQAELVVIDEAAAIPLPIVKNLLGPYLVFMASTINGYEGTGRSLSLKLIQQLRNQNNTSGRESTQTAVVSRDNKEKDSHLHSQSRQLREISLDEPIRYAPGDPIEKWLNKLLCLDVTLIKNPRFATRGTPHPSQCNLFVVNRDTLFSYHPVSENFLEKMMALYVSSHYKNSPNDLQLMSDAPAHKLFVLLPPIDPKDGGRIPDPLCVIQIALEGEISKESVRNSLSRGQRAGGDLIPWLISQQFQDEEFASLSGARIVRIATNPEYASMGYGSRAIELLRDYFEGKFTDMSEDVRPKDYSIKRVSDKELAKTNLLKDDVKLRDAKTLPPLLLKLSEQPPHYLHYLGVSYGLTQSLHKFWKNNSFVPVYLRQTANDLTGEHTCVMLNVLEGRESNWLVEFAKDFRKRFLSLLSYDFHKFTAVQALSVIESSKKAQDLSDDEKHDNKELTRTHLDDIFSPFDLKRLDSYSNNLLDYHVIGDMIPMLALLYFGDKMGDSVKLSSVQSAILLAIGLQRKNIDTIAKELNLPSNQTIAMFAKIMRKMSQYFRQLLSQSIEETLPNIKDDAIAEMDGEEIKNYNAAEALDQMEEDLEEAGSEAVQAMREKQKELINSLNLDKYAINDNSEEWAESQKSLEIAAKAKGVVSLKTGKKRTTEKAEDIYRQEMKAMKKPRKSKKAAN
Protein: L-threo-3-deoxy-hexylosonate aldolase (EC 4.1.2.54) (L-threo-3-deoxy-hexulosonate aldolase) (A6Y9S5)
Organism: Hypocrea jecorina (Trichoderma reesei)
Function: Mediates the conversion of 2-dehydro-3-deoxy-L-galactonate to pyruvate and L-glyceraldehyde in D-galacturonate catabolic process.
Interaction partners:
Sequence:
MAPPSLPCGIYAPTMTFFHPESEDIDIPTIKHHAQRLAKAGLAGLVVMGSNGEAVHCTRDEKIAVLSATREALDAAGFQSVPVLFGATEGSVRGTIELCKLAAAAGAAAALVLPPSYYRAQTDEASIEAYFVAVADASPIPLVLYNYPGAVSGIDMDSDLLIRLAQHKNIVGTKFTCGNTGKLTRVALATDAKTPFRDGSGYMAFGGMCDFTLQTLVSGGSGIIAGGANVMPKLCVKVWDSYSQGNRDEAEKLQKVLSRGDWPLTKAAIAGTKSAIQTYYGYGGYPRRPLKRLEQARVSAIEEGIREAMEIEKTL
Protein: Collagen alpha-1(IV) chain [Cleaved into: Arresten] (P02462)
Organism: Homo sapiens (Human)
Function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P02463}.
Interaction partners:
- Collagen alpha-2
- CD44 antigen
- Integrin alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Platelet glycoprotein VI
- Integrin alpha-5
- Laminin subunit gamma-1
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Integrin alpha-3
Sequence:
MGPRLSVWLLLLPAALLLHEEHSRAAAKGGCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVPGMLLKGERGFPGIPGTPGPPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGLSFQGPKGDKGDQGVSGPPGVPGQAQVQEKGDFATKGEKGQKGEPGFQGMPGVGEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEAGPPGPPGIVIGTGPLGEKGERGYPGTPGPRGEPGPKGFPGLPGQPGPPGLPVPGQAGAPGFPGERGEKGDRGFPGTSLPGPSGRDGLPGPPGSPGPPGQPGYTNGIVECQPGPPGDQGPPGIPGQPGFIGEIGEKGQKGESCLICDIDGYRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGVAGVPGPQGTPGLIGQPGAKGEPGEFYFDLRLKGDKGDPGFPGQPGMPGRAGSPGRDGHPGLPGPKGSPGSVGLKGERGPPGGVGFPGSRGDTGPPGPPGYGPAGPIGDKGQAGFPGGPGSPGLPGPKGEPGKIVPLPGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGAVGQPGIGFPGPPGPKGVDGLPGDMGPPGTPGRPGFNGLPGNPGVQGQKGEPGVGLPGLKGLPGLPGIPGTPGEKGSIGVPGVPGEHGAIGPPGLQGIRGEPGPPGLPGSVGSPGVPGIGPPGARGPPGGQGPPGLSGPPGIKGEKGFPGFPGLDMPGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGSMDKVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKGEVGFPGLAGSPGIPGSKGEQGFMGPPGPQGQPGLPGSPGHATEGPKGDRGPQGQPGLPGLPGPMGPPGLPGIDGVKGDKGNPGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGPKGLPGLQGIKGDQGDQGVPGAKGLPGPPGPPGPYDIIKGEPGLPGPEGPPGLKGLQGLPGPKGQQGVTGLVGIPGPPGIPGFDGAPGQKGEMGPAGPTGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPITGENIRPFISRCAVCEAPAMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
Protein: Defective proboscis extension response 5, isoform B (Q8INK5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLVEYFMALLVIMGLTAPVDKQSRRSSQYFGHLAAAEELSNLIPDNYDAIDPVFDNTTDREVIAALGTTARLHCRVRHLGDRAVSWIRQRDLHILTIGIMTYTNDQRFLARHIDNSDEWVLKIVSVQQRDAGVYECQVSTEPKISLAYKLVVVTSKAQILANRELFIQSGSDINLTCIAPQAPGPYTHMLWHKDTELVSDSARGGIRVESEQQMKTSNLVISRVQHTDSGNYTCSADNSNSDSVFVHIIKSEQHAAMQHELGSRLLLPPLPLLLLAVLLVVLLGPTSSLQIRTPLSTR
Protein: Tyrosinase copper-binding domain-containing protein (Q2UNF9)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- tyrosinase
- Tyrosinase
- Tyrosinase copper-binding domain-containing protein
- Tyrosinase copper-binding domain-containing protein
- Tyrosinase copper-binding domain-containing protein
- Tyrosinase copper-binding domain-containing protein
- Tyrosinase copper-binding domain-containing protein
- tyrosinase
- aromatic-amino-acid transaminase
- aromatic-amino-acid transaminase
Sequence:
MVALQALSLGLLASQALAFPAASQQAATATLPTTASSSTAVASSQLDQLANFAYNVTTDSVAGGSESKRGGCTLQNLRVRRDWRAFSKTQKKDYINSVLCLQKLPSRTPAHLAPGARTRYDDFVATHINQTQIIHYTGTFLAWHRYFIYEFEQALRDECSYTGDYPYWNWGADADNMEKSQVFDGSETSMSGNGEYIPNQGDIKLLLGNYPAIDLPPGSGGGCVTSGPFKDYKLNLGPAALSLPGGNMTAAANPLTYNPRCMKRSLTTEILQRYNTFPKIVELILDSDDIWDFQMTMQGVPGSGSIGVHGGGHYSMGGDPGRDVYVSPGDTAFWLHHGMIDRVWWIWQNLDLRKRQNAISGTGTFMNNPASPNTTLDTVIDLGYANGGPIAMRDLMSTTAGPFCYVYL
Protein: Phosphatidylcholine synthase (PC synthase) (PCS) (EC 2.7.8.24) (CDP-diglyceride-choline O-phosphatidyltransferase) (Q9HXE9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:Q9KJY8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9KJY8}.
Interaction partners:
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Probable CDP-alcohol phosphatidyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Probable phosphatidate cytidylyltransferase
- Non-hemolytic phospholipase C
- Hemolytic phospholipase C
- Phospholipid methyltransferase
- SnoaL-like domain-containing protein
Sequence:
MPVNLSMTPINKAKAWGVHAVTASGVILALLALLALVDNKPQACLLWLGLALLVDGLDGTLARKYEVKEMLPHFDGSVLDLVIDYLTYVFIPAIFIYRYIPLPEHFELLAVGVILVSSLFCFCNVNMKSTDNYFVGFPAAWNVVAVYFYVLDLHPWVNLATVLVLAALTLTRMKFLHPFRVRQFMPLNIAVTFVWLISSGLLIVQQPADLPILLGLWFAASAYFVGICLWRSAREWFG
Protein: Endoplasmic reticulum junction formation protein lunapark (ER junction formation factor lunapark) (Q9C0E8)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology. Involved in the stabilization of nascent three-way ER tubular junctions within the ER network. May also play a role as a curvature-stabilizing protein within the three-way ER tubular junction network. May be involved in limb development (By similarity). Is involved in central nervous system development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977}; Multi-pass membrane protein {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779}; Cytoplasmic side {ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25548161}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network (PubMed:22729086, PubMed:24223779, PubMed:25404289, PubMed:25548161, PubMed:27619977). {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977}.
Interaction partners:
- Metaxin-2
- Homeobox even-skipped homolog protein 2
- Homeobox protein Hox-D1
Sequence:
MGGLFSRWRTKPSTVEVLESIDKEIQALEEFREKNQRLQKLWVGRLILYSSVLYLFTCLIVYLWYLPDEFTARLAMTLPFFAFPLIIWSIRTVIIFFFSKRTERNNEALDDLKSQRKKILEEVMEKETYKTAKLILERFDPDSKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTPASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPPGPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAYCFFLNPARKTRPQAPRLPEFSFEKRQVVEGSSSVGPLPSGSVLSSDNQFNEESLEHDVLDDNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPELSGESLTAE
Protein: Zinc finger and BTB domain-containing protein 48 (Krueppel-related zinc finger protein 3) (hKR3) (Telomere zinc finger-associated protein) (TZAP) (Telomere-binding protein and transcriptional activator ZBTB48) (Zinc finger protein 855) (P10074)
Organism: Homo sapiens (Human)
Function: Telomere-binding protein that acts as a regulator of telomere length. Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat. Preferentially binds to telomeres that have a low concentration of shelterin complex and acts as a regulator of telomere length by initiating telomere trimming, a process that prevents the accumulation of aberrantly long telomeres. Also acts as a transcription regulator that binds to promoter regions. Regulates expression of a small subset of genes, including MTFP1. Regulates expression the J and/or S elements in MHC II promoter. Acts as a negative regulator of cell proliferation by specifically activating expression of ARF, a tumor suppressor isoform of CDKN2A.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}. Note=Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat (PubMed:28082411, PubMed:28500257). According to a report, preferentially binds to long telomeres that have a low concentration of shelterin complex, competing with the telomeric repeat binding factors TERF1 and TERF2 (PubMed:28082411). According to another report, binds telomeres regardless of their length (PubMed:28500257). {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}.
Interaction partners:
- Serine/threonine-protein kinase 11-interacting protein
Sequence:
MDGSFVQHSVRVLQELNKQREKGQYCDATLDVGGLVFKAHWSVLACCSHFFQSLYGDGSGGSVVLPAGFAEIFGLLLDFFYTGHLALTSGNRDQVLLAARELRVPEAVELCQSFKPKTSVGQAAGGQSGLGPPASQNVNSHVKEPAGLEEEEVSRTLGLVPRDQEPRGSHSPQRPQLHSPAQSEGPSSLCGKLKQALKPCPLEDKKPEDCKVPPRPLEAEGAQLQGGSNEWEVVVQVEDDGDGDYMSEPEAVLTRRKSNVIRKPCAAEPALSAGSLAAEPAENRKGTAVPVECPTCHKKFLSKYYLKVHNRKHTGEKPFECPKCGKCYFRKENLLEHEARNCMNRSEQVFTCSVCQETFRRRMELRVHMVSHTGEMPYKCSSCSQQFMQKKDLQSHMIKLHGAPKPHACPTCAKCFLSRTELQLHEAFKHRGEKLFVCEECGHRASSRNGLQMHIKAKHRNERPHVCEFCSHAFTQKANLNMHLRTHTGEKPFQCHLCGKTFRTQASLDKHNRTHTGERPFSCEFCEQRFTEKGPLLRHVASRHQEGRPHFCQICGKTFKAVEQLRVHVRRHKGVRKFECTECGYKFTRQAHLRRHMEIHDRVENYNPRQRKLRNLIIEDEKMVVVALQPPAELEVGSAEVIVESLAQGGLASQLPGQRLCAEESFTGPGVLEPSLIITAAVPEDCDT
Protein: Non-POU domain containing octamer-binding isoform 1 (A0A0S2Z4Z9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY
Protein: G protein complex beta subunit SfaD (Q4WVI4)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- G protein complex alpha subunit GpaB
- Guanine nucleotide-binding protein subunit gamma
- G-protein complex alpha subunit GpaA/FadA
- Guanine nucleotide-binding protein alpha-2 subunit
- Developmental regulator FlbA
- Serine/threonine-protein kinase ste20
- non-specific serine/threonine protein kinase
- Phosducin, putative
- Mating-type alpha-pheromone receptor PreB
- DUF7582 domain-containing protein
Sequence:
MAADMSGEQMQAKITAARREAEGLKDKIKRRKDELADTTLRQVAQNQTDALPRIGMKPRRTLKGHLAKIYAMHWSTDRRHLVSASQDGKLIIWDAYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLSSREGPTRVARELSGHSGYLSCCRFINDRRIITSSGDMTCMLWDIESGSKVTEFADHLGDVMSISINPTNQNIFVSGACDAFAKLWDIRTGKAVQTFAGHESDINAIQFFPDGNAFGTGSDDTSCRLFDIRADRELNIYQSDQILCGITSVAFSVSGRLLFAGYDDFECKVWDVLRGDKVGSLSGHENRVSCLGVSNDGISLCTGSWDSLVSALKAIKYSPLLFRFIVFLVFISQSLIFLFVVKLKVWAW