wanglab/gogpt-training-data huggingface dataset:
Protein: Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein 1) (Nervous system nuclear protein induced by axotomy protein 1 homolog) (Protein deglutamylase CCP1) (Q9UPW5)
Organism: Homo sapiens (Human)
Function: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins such as MYLK. Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:23085998}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000269|PubMed:23085998}. Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. Note=Localizes in both the cytoplasm and nuclei of interphase and dividing cells. {ECO:0000269|PubMed:23085998}.
Interaction partners:
- Tubulin monoglutamylase TTLL4
Sequence:
MSKLKVIPEKSLTNNSRIVGLLAQLEKINAEPSESDTARYVTSKILHLAQSQEKTRREMTAKGSTGMEILLSTLENTKDLQTTLNILSILVELVSAGGGRRVSFLVTKGGSQILLQLLMNASKESPPHEDLMVQIHSILAKIGPKDKKFGVKARINGALNITLNLVKQNLQNHRLVLPCLQLLRVYSANSVNSVSLGKNGVVELMFKIIGPFSKKNSSLIKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPVIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDVEAENETENEDDLDQNFKNDDIETDINKLKPQQEPGRTIEDLKMYEHLFPELVDDFQDYDLISKEPKPFVFEGKVRGPIVVPTAGEETSGNSGNLRKVVMKENISSKGDEGEKKSTFMDLAKEDIKDNDRTLQQQPGDQNRTISSVHGLNNDIVKALDRITLQNIPSQTAPGFTAEMKKDCSLPLTVLTCAKACPHMATCGNVLFEGRTVQLGKLCCTGVETEDDEDTESNSSVEQASVEVPDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQSDIIDRVVYDLDNPNYTIPEEGDILKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNSCPLVTITAMPESNYYEHICHFRNRPYVFLSARVHPGETNASWVMKGTLEYLMSNNPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPSPDLHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSIKETVWHTNDNATSCDVVEDTGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKGLQIGTRELEEMGAKFCVGLLRLKRLTSPLEYNLPSSLLDFENDLIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDELDIELAENVGDYEPSAQEEVLSDSELSRTYLP
Protein: Protein VAC14 homolog (Q80WQ2)
Organism: Mus musculus (Mouse)
Function: Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:19037259}. Microsome membrane {ECO:0000250|UniProtKB:Q80W92}. Note=Mainly associated with membranes of the late endocytic pathway. {ECO:0000250|UniProtKB:Q08AM6}.
Interaction partners:
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- DNA repair and recombination protein RAD54-like
- Divergent protein kinase domain 2A
- DNA repair and recombination protein RAD54B
- Protein MTSS 2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Amyloid-beta precursor protein
Sequence:
MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVRDFVAQNNTMQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESSKFDLVSFIPLLRERIYSNNQYARQFIISWILVLVSVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDEPDEPKSVAQKQTEPNPEDSLPKQEGTASGGPGSCDSSFGSGINVFTSANTDRAPVTLHLDGIVQVLNCHLSDTTIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVVLKDLEVLAEIASSPAGQTDDPGAPDGPDLRVNHSELQVPTSGRANLLNPPSTKGLEGSPSTPTMNSYFYKFMINLLQTFSSERKLLEARGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHTLNTILLTSTELFQLRNQLKDLQTPESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLTEVDKLVQLIECPIFTYLRLQLLDVKNNPYLIKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDCLKAAPKSQKGDSPSIDYTELLQHFEKVQKQHLEVRHQRSGRGDHLDRRVIL
Protein: Transcription factor MYC2 (AtMYC2) (Basic helix-loop-helix protein 6) (AtbHLH6) (bHLH 6) (Protein JASMONATE INSENSITIVE 1) (R-homologous Arabidopsis protein 1) (RAP-1) (Transcription factor EN 38) (Z-box binding factor 1 protein) (bHLH transcription factor bHLH006) (rd22BP1) (Q39204)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator. Common transcription factor of light, abscisic acid (ABA), and jasmonic acid (JA) signaling pathways. With MYC3 and MYC4, controls additively subsets of JA-dependent responses. In cooperation with MYB2 is involved in the regulation of ABA-inducible genes under drought stress conditions. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the MYC recognition site (5'-CACATG-3'), and to the G-box (5'-CACNTG-3') and Z-box (5'-ATACGTGT-3') of promoters. Binds directly to the promoters of the transcription factors PLETHORA1 (PLT1) and PLT2 and represses their expression. Negative regulator of blue light-mediated photomorphogenic growth and blue- and far-red-light regulated gene expression. Activates multiple TIFY/JAZ promoters. Positive regulator of lateral root formation. Regulates sesquiterpene biosynthesis. Subjected to proteasome-dependent proteolysis. The presence of the destruction element (DE) involved in turnover is required for the function to regulate gene transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15208388, ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23169619, ECO:0000269|PubMed:24890857, ECO:0000269|PubMed:27357749}.
Interaction partners:
- Protein TIFY 6B
- Protein TIFY 10A
- Protein TIFY 7
- Protein TIFY 9
- Protein TIFY 11A
- Protein TIFY 10B
- Protein TIFY 3B
- Protein TIFY 11B
- Protein TIFY 3A
- Protein ETHYLENE INSENSITIVE 3
Sequence:
MTDYRLQPTMNLWTTDDNASMMEAFMSSSDISTLWPPASTTTTTATTETTPTPAMEIPAQAGFNQETLQQRLQALIEGTHEGWTYAIFWQPSYDFSGASVLGWGDGYYKGEEDKANPRRRSSSPPFSTPADQEYRKKVLRELNSLISGGVAPSDDAVDEEVTDTEWFFLVSMTQSFACGAGLAGKAFATGNAVWVSGSDQLSGSGCERAKQGGVFGMHTIACIPSANGVVEVGSTEPIRQSSDLINKVRILFNFDGGAGDLSGLNWNLDPDQGENDPSMWINDPIGTPGSNEPGNGAPSSSSQLFSKSIQFENGSSSTITENPNLDPTPSPVHSQTQNPKFNNTFSRELNFSTSSSTLVKPRSGEILNFGDEGKRSSGNPDPSSYSGQTQFENKRKRSMVLNEDKVLSFGDKTAGESDHSDLEASVVKEVAVEKRPKKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAIAYINELKSKVVKTESEKLQIKNQLEEVKLELAGRKASASGGDMSSSCSSIKPVGMEIEVKIIGWDAMIRVESSKRNHPAARLMSALMDLELEVNHASMSVVNDLMIQQATVKMGFRIYTQEQLRASLISKIG
Protein: Polyadenylate-binding protein (PABP) (A2A5N3)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1
- Eukaryotic translation initiation factor 4E
- Cytoplasmic polyadenylation element-binding protein 1
- PAN2-PAN3 deadenylation complex catalytic subunit Pan2
- Ataxin-2
- Poly
- Ataxin-2-like protein
- Eukaryotic initiation factor 4A-I
- Poly
Sequence:
MDTGGHGCSLSSLYVGDLHPDVTESMLYEMFSPIGNILSIRVCRDVATRRSLGYAYINFQQPADAERALDTMNFEVIKGQPIRIMWSHRDPGLRKSGMGNIFIKNLENSIDNKALYDTFSTFGSILSSKVVYNEHGSRGFGFVHFETHEAAQKAINTMNGMLLNDRKVFVGHFKSRQKREAELGARALGFTNIYVKNLHANVDEQRLQDLFSQFGNMQSVKVMRDSNGQSRGFGFVNFEKHEEAQKAVDHMNGKEVSGQLLYVGRAQKRAERQSELKRRFEQMKQERQNRYQGVNLYVKNLDDSINDERLKEVFSTYGVITSAKVMTESSHSKGFGFVCFSSPEEATKAVTEMNGRIVGTKPLYVALAQRKEERKAILTNQYRRRPSHPVLSSFQQPTSYLLPAVPQSTAQAVYYSSGSITPMQPDPRWTAQPHGPPSTCPPAASVVQPLSTTQHPCIHLRGASQVSSQVPHTQRVVNIGTQTTGPGGEGSSIPGQLLVPHRGTSAVHSAHGVQESAVYVPGHQPLTVSMLAAAPLHEQKQMIGERLYSLIHDACAPLTGKITGMLLELDNLELLLLLESPESLHAKIEEAVAVLQVHREMESTDRN
Protein: Forkhead box protein G1 (Brain factor 1) (BF-1) (BF1) (Brain factor 2) (BF-2) (BF2) (hBF-2) (Forkhead box protein G1A) (Forkhead box protein G1B) (Forkhead box protein G1C) (Forkhead-related protein FKHL1) (HFK1) (Forkhead-related protein FKHL2) (HFK2) (Forkhead-related protein FKHL3) (HFK3) (P55316)
Organism: Homo sapiens (Human)
Function: Transcription repression factor which plays an important role in the establishment of the regional subdivision of the developing brain and in the development of the telencephalon.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:21280142}.
Interaction partners:
- Serum response factor
- Methyl-CpG-binding protein 2
- Transducin-like enhancer protein 1
- Lysine-specific demethylase 5B
- Cyclin-dependent kinase-like 5
- Paired box protein Pax-6
- T-box brain protein 1
- Mothers against decapentaplegic homolog 3
- Homeobox protein EMX1
- Homeobox protein OTX2
Sequence:
MLDMGDRKEVKMIPKSSFSINSLVPEAVQNDNHHASHGHHNSHHPQHHHHHHHHHHHPPPPAPQPPPPPQQQQPPPPPPPAPQPPQTRGAPAADDDKGPQQLLLPPPPPPPPAAALDGAKADGLGGKGEPGGGPGELAPVGPDEKEKGAGAGGEEKKGAGEGGKDGEGGKEGEKKNGKYEKPPFSYNALIMMAIRQSPEKRLTLNGIYEFIMKNFPYYRENKQGWQNSIRHNLSLNKCFVKVPRHYDDPGKGNYWMLDPSSDDVFIGGTTGKLRRRSTTSRAKLAFKRGARLTSTGLTFMDRAGSLYWPMSPFLSLHHPRASSTLSYNGTTSAYPSHPMPYSSVLTQNSLGNNHSFSTANGLSVDRLVNGEIPYATHHLTAAALAASVPCGLSVPCSGTYSLNPCSVNLLAGQTSYFFPHVPHPSMTSQSSTSMSARAASSSTSPQAPSTLPCESLRPSLPSFTTGLSGGLSDYFTHQNQGSSSNPLIH
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FUW5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MILNPALFLNKCVCIYTTLILLLLTNGGYATSSNDISLASKDPTTFPLGCSPDITTPKKGLSMELYSYDFRKKGSYPCWDAAYLDPNYPRTGYKSHRLLAKVDGVTGNINFYYHATKGCTPQLGHLPASYNYPKPLTMTNFTMLLYGYFRPKVTGFHTFTISADDLLFVNFGAGNAFDCCRRDSSADHFGNYQAYAIWGSKTAKDELTVHLDAGVYYPIRLFYNNREYDGALSFTFKTESNENTVSDFSEYFFSLDDTEEGCPGLISYDSSCASVKTSKIIGIDYHTETPNENLVPITKTIYHLGIPCTGTTTTPLCGSGFYDPLANKCVTINTSSTSSVTKTTSHTTSKEVSFHSSISSQKTLIPKSIPSPYGPIKSQSIPTEMETSSEISSSEYAFSDVISTPSHSPYTKKHSSLNSSSYTSTVIHSLTSYSISQGIFSTSLSEQNITSKSSTDKFSTATSMSNSITQSSIIISQSSTNNENYTTTSMHTSSDKISTETLNNSISTTTSILFSNSSTILKNNTTIISSDKDTHYHPVNPTIVCSTNKTEIICASITQPSISNSNNHWSSSVLRFNSTTVRSTLPSSAGSNETSINVPFSSSTESNASTSSTSTSNSKTVRSTLPSSAGSNETSINVPFSSSTESNTSTSSTSTSNSKTVRSTLPSSAGSNETSINVPFSSSTESNASTSSTSTSNSKTVRSTPFSSAGIIMTSLSQRNNKSASSYASSNSKCYNTADSCRKVHSTPSYLLTSSYTSEGVDYDCSLVSTKLKINDTNCLNNKHTTKSCLKTSVTTTIPTLEIKTARKSSSNTIGLHSYPTSSPNKSISSAPIIGYISSFKTIKTASPSYQTSDLTTITTITSLNNPGSTAVENTHESNDKSRKTSSNDISSKHSVIKETKDAVESSNKSHQTNTLKCSSIIIASSSHNSYESLGGTTLTLTLSKVYSPQNNDTLPFLEISEVNPSRTVLPESSKMMQYLTSTEERNKTARNTIATNIVSISTFHFEGEGNAIRMGYTQLLLMLIGIIVMNIGT
Protein: Rifin (O96288)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKMHYSEILFFSLSLNILITSSYAHSENKQYITPYTPNTSSRVLTECDIKMSIYDNDGDMKSVKENFDRQTSERFEEYDERMKDKRRKCKEQCDKDIQEIIVKDKMEKSLAKKVEKGCLRCGCGLGGVAASVGIIGPIAVNEVKKAALVAAAQKGIEVGMAKAIEELGKIVGLSDFSYLNWSAMITATTYYKPMKLVNIVNSANSMCTDSNPAFTSLFCKASYRINSEVSSSRFTEVISQEAAKAASAAGEAAKNAEKAQIALVNEESAHLYSAIGYSVIAILIILLVMVIIYLILRYRRKKKMNKKLQYTKLLNQ
Protein: Interferon-inducible double-stranded RNA-dependent protein kinase activator A (PKR-associated protein X) (PKR-associating protein X) (RAX) (Protein activator of the interferon-induced protein kinase) (Protein kinase, interferon-inducible double-stranded RNA-dependent activator) (Q9WTX2)
Organism: Mus musculus (Mouse)
Function: Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1 (By similarity). Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Endoribonuclease Dicer
- Protein argonaute-1
- RISC-loading complex subunit TARBP2
- Ribonuclease 3
- Interferon-induced, double-stranded RNA-activated protein kinase
- Protein argonaute-2
- Protein argonaute-3
- Microprocessor complex subunit DGCR8
- Protein argonaute-4
- Exportin-5
Sequence:
MSHSRHRAEAPPLQREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQVHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSLPNTDYIQLLSEIASEQGFNITYLDIEELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
Protein: Protein phosphatase 1 regulatory subunit 15B (Q5SWA1)
Organism: Homo sapiens (Human)
Function: Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Neurabin-2
- Leucine-rich repeat protein SHOC-2
- Protein phosphatase 1 regulatory subunit 15A
- Eukaryotic translation initiation factor 2 subunit 1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Actin, alpha skeletal muscle
- Eukaryotic translation initiation factor 1
- Exocyst complex component 8
Sequence:
MEPGTGGSRKRLGPRAGFRFWPPFFPRRSQAGSSKFPTPLGPENSGNPTLLSSAQPETRVSYWTKLLSQLLAPLPGLLQKVLIWSQLFGGMFPTRWLDFAGVYSALRALKGREKPAAPTAQKSLSSLQLDSSDPSVTSPLDWLEEGIHWQYSPPDLKLELKAKGSALDPAAQAFLLEQQLWGVELLPSSLQSRLYSNRELGSSPSGPLNIQRIDNFSVVSYLLNPSYLDCFPRLEVSYQNSDGNSEVVGFQTLTPESSCLREDHCHPQPLSAELIPASWQGCPPLSTEGLPEIHHLRMKRLEFLQQASKGQDLPTPDQDNGYHSLEEEHSLLRMDPKHCRDNPTQFVPAAGDIPGNTQESTEEKIELLTTEVPLALEEESPSEGCPSSEIPMEKEPGEGRISVVDYSYLEGDLPISARPACSNKLIDYILGGASSDLETSSDPEGEDWDEEAEDDGFDSDSSLSDSDLEQDPEGLHLWNSFCSVDPYNPQNFTATIQTAARIVPEEPSDSEKDLSGKSDLENSSQSGSLPETPEHSSGEEDDWESSADEAESLKLWNSFCNSDDPYNPLNFKAPFQTSGENEKGCRDSKTPSESIVAISECHTLLSCKVQLLGSQESECPDSVQRDVLSGGRHTHVKRKKVTFLEEVTEYYISGDEDRKGPWEEFARDGCRFQKRIQETEDAIGYCLTFEHRERMFNRLQGTCFKGLNVLKQC
Protein: Glutamine synthetase (EC 6.3.1.2) (Q8JI34)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Amidophosphoribosyltransferase
- Protein kinase domain-containing protein
- Multifunctional protein CAD
- Multifunctional protein CAD
- Delta-1-pyrroline-5-carboxylate synthase
- Delta-1-pyrroline-5-carboxylate synthase
- Uncharacterized protein
- Aldehyde dehydrogenase domain-containing protein
- Serine hydroxymethyltransferase
- Glutamine amidotransferase type-2 domain-containing protein
Sequence:
MATSESASLSKTVKQHYMDLSQGDKVQAMYIWIDGTGEGLRCKTRTLDSEPKNIDDLPEWNFDGSSTYQSEGSNSDMYLIPAAMFRDPFRKDPNKLVLCEVLKYNRKPTETNLRLMCKKIMEMVENQVPWFGMEQEYTILGTDGHPFGWPSNGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGVKICGTNAEVMPAQWEFQVGPCEGINMGDHLWAARFILHRVCEDFGVVASFDPKPIPGNWNGAGCHTNFSTKEMREDGGLRGIEDSIEKLGRRHRYHIRAYDPKGGLDNARRLTGHHETSNIHEFSAGVANRGASIRIPRSVGQDKKGYFEDRRPSANCDPYAVTEALIRTCLLSEEGEEPKEYSK
Protein: SKP1-like protein 19 (AtSK19) (O81058)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-like protein 3
- Cullin-2
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Elongin-C
- Cullin-3A
Sequence:
MSSKKIVLTSSDGESFKVEEVVARKLQIVGHIIEDDCATNKIPIPNVTGEILAKVIEYCKKHVEDDDDVVETHESSTKGDKTVEEAKKKPDDVAVPESTEGDDEAEDKKEKLNEWDAKFMKDFDIKTIFDIILAANYLNVQGLFDLCSKTIADYIKDMTPEEVRELFNIENDFTPEEEEAIRNENAWTFEQDGKQQVPKP
Protein: 3',5'-cyclic-AMP phosphodiesterase (EC 3.1.4.53) (Q8BTA5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASLQPLQPNYLSVCLFPEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKVRTPLSLTTTGAPGSSLSVDLVEVRQHFLCSYLATTVS
Protein: Propionyl-CoA carboxylase, carboxyltransferase subunit (PCC) (EC 6.4.1.3) (I3R7F1)
Organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Function: Part of the propionyl coenzyme A carboxylase (PCC) complex involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. The complex catalyzes the carboxylation of propionyl-CoA to methylmalonyl-CoA. PCC is also able to catalyze the carboxylation of acetyl-CoA.
Interaction partners:
- Propionyl-CoA carboxylase, biotin carboxylase and biotin-carboxyl carrier subunit
- Propionyl-CoA carboxylase, protein PccX subunit
- Methylmalonyl-CoA epimerase
- 3-ketoacyl-CoA thiolase
- acetyl-CoA C-acyltransferase
- Acetyl-CoA C-acyltransferase
- AMP-dependent synthetase
- Acetate--CoA ligase
- Acyl-CoA synthetase
- acetate--CoA ligase
Sequence:
MTMEDRIDELREKREEALKGGGEDRIASQHDKGKMTARERIDYFLDDGTFREFDQFRTHRNHKFGMEETKLPGDGVITGHGEVDGRTVFVFAHDFTVFGGSLGEVFAEKICKVMDKAMEVGAPVIGLNDSAGARIQEGVQSLGGFGEIFRRNTEASGVVPQISAIMGPCAGGAVYSPALTDFTFMVRDTSHMFITGPDVIKTVTGEEVTFDELGGATTHTSTSGVAHFATDTEEQALDDIRHLLSYLPQNNVEDPPRVEPWDDPERVADELEEIVPDQPRKPYDIHDVLNGVLDEGSFFGVQEDFAKNIVVGFGRLDGHSVGIVANQPRVNAGTLDIEASEKGARFIRFCDSFNIPILSFVDVPGFLPGTDQEHNGIIRHGAKLLYAYSEATVPLMTVITRKAYGGAYDVMASKHLGADVNYAWPTAEIAVMGPQGAVNILYRDELEAADDPDARRDELIEEYREEFANPYTAADRGFVDDVIEPGDTRNRLIADLRMLKSKRKSQPDKKHGNIPL
Protein: Serine/threonine-protein kinase PLK3 (EC 2.7.11.21) (Cytokine-inducible serine/threonine-protein kinase) (FGF-inducible kinase) (Polo-like kinase 3) (PLK-3) (Q60806)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase (By similarity). {ECO:0000250}.
Interaction partners:
- Lymphocyte-specific protein 1
- Kinase suppressor of Ras 1
- RAF proto-oncogene serine/threonine-protein kinase
- M-phase inducer phosphatase 3
- Cellular tumor antigen p53
- Separin
Sequence:
MEPAAGFLSPRPFPRAAVPSAPPAGPGPPANASPRSEPEVLAGPRAPDPPGRLITDPLSGRTYTKGRLLGKGGFARCYEATDTESGIAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITDNMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIEQILRHDFFTKGYTPDRLPVSSCVTVPDLTPPNPARSLFAKVTKSLFGRKKNKNKNHSEDQDNVSCLAPVVSGQAPASLIETAAEDSSPRGTLASSGDGFEEGLTVATVVESALCALRNCVAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSMGSVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEAEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDQSPA
Protein: 18.5 kDa class IV heat shock protein (18.5 kDa heat shock protein) (AtHsp18.5) (O64564)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 21.7 kDa class VI heat shock protein
- 17.7 kDa class II heat shock protein
- 14.7 kDa heat shock protein
- 15.4 kDa class V heat shock protein
- 23.6 kDa heat shock protein, mitochondrial
- 22.0 kDa heat shock protein
- 26.5 kDa heat shock protein, mitochondrial
- Heat shock protein 21, chloroplastic
- 17.6 kDa class II heat shock protein
- Probable protein phosphatase 2C 8
Sequence:
MSMIPISNRRRLSPGDRIWEPFELMNTFLDFPSPALFLSHHFPSLSREIFPQTSSSTVNTQLNWTETPTAHVFKAYLPGVDQDEVIAFVDEEGYLQICTGDNKFMSRFKLPNNALTDQVTAWMEDEFLVVFVEKDASSSPPQLPEIEENRNVRVVEITGDDD
Protein: Uncharacterized protein (Q4W8X0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MAGYKVNCKNGYSLEVGADGGQAWYGTPHGNFRWTQGYDRSDNFIVWDNWRGIMNFMLAFVTPIAMVPNYEKRVRMIFQSGSSAEGGSGCCNHSVDVFSASNLKVRSNC
Protein: Matrix protein (M protein) (P03519)
Organism: Vesicular stomatitis Indiana virus (strain San Juan) (VSIV)
Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly.
Subcellular location: Virion {ECO:0000269|PubMed:35476516}. Host endomembrane system; Peripheral membrane protein {ECO:0000269|PubMed:1850035}. Host nucleus membrane; Peripheral membrane protein. Host nucleus {ECO:0000269|PubMed:28888655}. Host cytoplasm {ECO:0000269|PubMed:1850035, ECO:0000269|PubMed:28888655}. Note=In the virion, forms a double layer around the helical nucleocapsid, the inner matrix layer binding to the N helix and the outer matrix layer binding to the envelope glycoprotein (PubMed:35476516). About 2480 copies of M are present in the virion (PubMed:35476516). {ECO:0000269|PubMed:35476516}.
Interaction partners:
Sequence:
MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTYDPNQLRYEKFFFTVKMTVRSNRPFRTYSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHTHCEGRAYLPHRMGKTPPMLNVPEHFRRPFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSISHFK