wanglab/gogpt-training-data huggingface dataset:
Protein: EEF1A lysine methyltransferase 2 (EC 2.1.1.-) (Methyltransferase-like protein 10) (Protein-lysine N-methyltransferase METTL10) (Q5JPI9)
Organism: Homo sapiens (Human)
Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000269|PubMed:25144183}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000269|PubMed:25144183}.
Interaction partners:
- Elongation factor 1-alpha 1
- eEF1A lysine and N-terminal methyltransferase
- Protein-lysine N-methyltransferase EEF2KMT
- Probable methyltransferase-like protein 25
- EEF1A lysine methyltransferase 1
- Protein-lysine methyltransferase METTL21C
- Protein N-lysine methyltransferase METTL21A
- Protein N-lysine methyltransferase METTL21D
- Electron transfer flavoprotein beta subunit lysine methyltransferase
- EEF1A lysine methyltransferase 4
Sequence:
MSSGADGGGGAAVAARSDKGSPGEDGFVPSALGTREHWDAVYERELQTFREYGDTGEIWFGEESMNRLIRWMQKHKIPLDASVLDIGTGNGVFLVELAKFGFSNITGIDYSPSAIQLSGSIIEKEGLSNIKLKVEDFLNLSTQLSGFHICIDKGTFDAISLNPDNAIEKRKQYVKSLSRVLKVKGFFLITSCNWTKEELLNEFSEGFELLEELPTPKFSFGGRSGNSVAALVFQKM
Protein: ADP-ribosylation factor GTPase-activating protein 2 (Zinc finger protein 289) (E9PN48)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}.
Interaction partners:
Sequence:
MAAEPNKTEIQTLFKRLRAVPTNKACFDCGAKNPSWASITYGVFLCIDCSGVHRSLGVHLSFIRSTELDSNWNWFQLRCMQVGGNANATAFFRQHGCTANDANTKYNSRAAQMYREKIRQLGSAALARHGTDLWIDNMSSAVPNHSPEKKDSDFFTEHTQPPAWDAPATEPSGTQQPAPSTESSGLAQPEHGPNTDLLGTSPKASLESVYLSAKGALPARELKSSIIGKKKPAAAKKGLGAKKGLGAQKVSSQSFSEIERQAQVAEKLREQQAADAKKQAEESMVASMRLAYQELQIDRKKEEKKLQNLEGKKREQAERLGMGLVSRSSVSHSVLSEMQVIEQETPVSAKSSRSQLDLFDDVGTFASGPPKYKDNPFSLGESFGSRWDTDAAWGMDRVEEKEPEVTISSIRPISERATNRREVESRSSGLESSEARQKFAGAKAISSDMFFGREVDAEYEARSRLQQLSGSSAISSSDLFGDMDGAHGAGSVSLGNVLPTADIAQFKQGVKSVAGKMAVLANGVMNSLQDRYGSY
Protein: Leucine-rich repeat protein kinase family protein (A0A178WLG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- BAG family molecular chaperone regulator 2
- AT4g00280 protein
Sequence:
MMTSKAKALTFICCVALLNLAIAQDQSGFISIDCGLQPENSSYTETSTDIKYVSDSSYTDTGTSYFVAPENRQNMKQSMWSVRSFPEGIRNCYTIAVNSSTKYLIRADFMYGNYDSRNEIPGFDLHLGPNKWDTVELVSPLQTVSKEIIYYVLTDTIQVCLVNTGNGTPFISVLELRQLPNSSYAAQSESLQLFQRLDFGSTTNLTVRYPNDVFDRIWFPATPNGTKPLSDPSTSLTSNSTGNFRLPQVVMRTGIVPDNPRGFVDFGWIPDDPSLEFFFYLYFTELQQPNSGTVETREFVILLNGKSFGEPLSLNYFRTLALFTSNPLKAESFQFSLRQTQSSSLPPLINAMETYFVNKLPQSSTDPNDLSAMRNIKSAYKVKRNWEGDVCVPQAYTWEGLNCSFNGTNMPRVIALNLSSAGLTGEITSDISRLSQLQILDLSNNNLSGPAVPAFLAQLQFLRVLHLANNQLSGPIPSSLIERLDSFSISGNPSICSANACEEVSQNRSKKNKLPSFVIPLVASLAGLLLLFIISAAIFLILMRKKKQGRTINRTVTATSNGPSLQRRDTGSMRPSMQRRETGFSTRPSLQRIESGMTDYGGNETAVDAFDLEPSNRKFTYAEIVNITNGFDRDQGKVGFGRNYLGKLDGKEVTVKLVSSLSSQGYKQLRAEVKHLFRIHHKNLITMLGYCNEGDKMAVIYEYMANGNLKQHISENSTTVFSWEDRLGIAVDVAQGLEYLHTGCKPPIIHRNVKCTNVFLDESFNAKLGGFGLSRAFDAAEGSHLNTAIAGTPGYVDPEYYTSNMLTEKSDVYSFGVVLLEIVTAKPAIIKNEERMHISQWVESLLSRENIVEILDPSLCGDYDPNSAFKTVEIAVACVCRNSGDRPGMSQVVTALKESLAVEVERKKHLPVGSTDSLEELALGFGSNPPPRLR
Protein: 60S ribosomal protein L27, putative (Q381J6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S4
- 60S ribosomal protein L35A, putative
- 40S ribosomal protein S5, putative
- Ribosomal protein L37
- 60S ribosomal subunit protein L31, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S27, putative
- 40S ribosomal protein S33, putative
- 60S ribosomal protein L37a, putative
Sequence:
MKFLKPGKVVIMTSGRYAGKKAVIVQNTDTRNKERPYGHSLLAGIKKYPRKVVRGMSKRSITRRSQVGVFLRVVNHKHFLPTRYNMDLSRELRGRINVSDASKKAKSKQLVKRLFQARYNAGNNRWFFQRLRF
Protein: Cholesterol ring-cleaving hydrolase IpdA subunit (EC 4.1.99.-) ((3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA hydrolase alpha subunit) (COCHEA-CoA hydrolase alpha subunit) (P9WPW1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the final steps of cholesterol and steroid degradation. Opens the last steroid ring of cholesterol by catalyzing the hydrolysis of (3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA (COCHEA-CoA) to 6-methyl-3,7-dioxodecanedioyl-CoA (MeDODA-CoA).
Interaction partners:
- Cholesterol ring-cleaving hydrolase IpdB subunit
- (7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA hydrolase (HIEC-CoA hydrolase)
- 
- Probable short-chain type dehydrogenase/reductase
- Acyl-CoA dehydrogenase IpdE1
- Probable short-chain type dehydrogenase/reductase
- 
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B
- Probable acyl-CoA dehydrogenase FadE31
- Putative amidase AmiD
Sequence:
MPDKRTALDDAVAQLRSGMTIGIAGWGSRRKPMAFVRAILRSDVTDLTVVTYGGPDLGLLCSAGKVKRVYYGFVSLDSPPFYDPWFAHARTSGAIEAREMDEGMLRCGLQAAAQRLPFLPIRAGLGSSVPQFWAGELQTVTSPYPAPGGGYETLIAMPALRLDAAFAHLNLGDSHGNAAYTGIDPYFDDLFLMAAERRFLSVERIVATEELVKSVPPQALLVNRMMVDAIVEAPGGAHFTTAAPDYGRDEQFQRHYAEAASTQVGWQQFVHTYLSGTEADYQAAVHNFGASR
Protein: Uncharacterized protein (Q3UYW8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MIKIPRHEVTEISNTDVETQPGKTVIRLPSGSGPASPTTGSAVDIRAGAISASGPELEGAGHSKFQVTVPGAKVGSLDVNVKAKGLDLGGKGGIRVPGVDVSSSLGAGSVEVQAPSLQSGDIGKIKIPTM
Protein: Histone H4 (P84040)
Organism: Drosophila melanogaster (Fruit fly)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3
- Histone H2A
- Histone H2B
- Histone H3-like centromeric protein cid
- Chromatin assembly factor 1 p55 subunit
- Histone H3.3A
- Histone chaperone asf1
- Chromosome alignment defect 1
- Histone acetyltransferase MOF
- Protein male-specific lethal-3
Sequence:
MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Protein: Conjugal transfer protein (Q48B15)
Organism: Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6))
Interaction partners:
Sequence:
MMIKRTLVPNKDELCILLVALACLPDIASADWYTTLQQWGSIVRLGLYTLAGTLGLICLIWSGAKWMIARSTGDRSHTFMDYLESMGVLLVVGASVLLGTAAWQVFGTGVPG
Protein: Acid-sensing ion channel 3 (ASIC3) (Amiloride-sensitive cation channel 3) (Dorsal root ASIC) (DRASIC) (O35240)
Organism: Rattus norvegicus (Rat)
Function: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:9261094}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q6X1Y6}. Note=Preferentially expressed at the plasma membrane of the soma and cellular processes of neurons (PubMed:11842212). In part cytoplasmic in cochlea cells (By similarity). Localized in specialized sensory nerve endings (By similarity). {ECO:0000250|UniProtKB:Q6X1Y6, ECO:0000269|PubMed:11842212}.
Interaction partners:
- Transient receptor potential cation channel subfamily V member 1
- Stomatin like 3
- Stomatin
- Acid-sensing ion channel 1
- P2X purinoceptor 3
- Sodium channel protein type 10 subunit alpha
- Transient receptor potential cation channel subfamily A member 1
Sequence:
MKPRSGLEEAQRRQASDIRVFASSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQVAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDPAEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVIFTRMGQCYTFNSGAHGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRVQIHSQDEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASLDPDDFDPEPSDPLGSPRPRPSPPYSLIGCRLACESRYVARKCGCRMMHMPGNSPVCSPQQYKDCASPALDAMLRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARKYNRSESYITENVLVLDIFFEALNYEAVEQKAAYEVSELLGDIGGQMGLFIGASLLTILEILDYLCEVFQDRVLGYFWNRRSAQKRSGNTLLQEELNGHRTHVPHLSLGPRPPTTPCAVTKTLSASHRTCYLVTRL
Protein: Clathrin heavy chain 1 (P49951)
Organism: Bos taurus (Bovine)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Plays a role in early autophagosome formation.
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Melanosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00610}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:Q00610}.
Interaction partners:
- Clathrin light chain B
- Clathrin light chain A
- AP-1 complex subunit beta-1
- Cyclin-G-associated kinase
- Beta-arrestin-1
- Beta-arrestin-2
- Auxilin
- AP-2 complex subunit alpha
- AP-2 complex subunit mu
- Arrestin-C
Sequence:
MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAEELFARKFNALFAQGNYSEAAKVAANAPKGILRTPDTIRRFQSVPAQPGQTSPLLQYFGILLDQGQLNKYESLELCRPVLQQGRKQLLEKWLKEDKLECSEELGDLVKSVDPTLALSVYLRANVPNKVIQCFAETGQVQKIVLYAKKVGYTPDWIFLLRNVMRISPDQGQQFAQMLVQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLYDIKRAVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICVQVASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDVIKNLILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLIDQVVQTALSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPAYGQPQPGFGYSM
Protein: Methylosome protein WDR77 (Methylosome protein 50) (MEP-50) (WD repeat-containing protein 77) (Q99J09)
Organism: Mus musculus (Mouse)
Function: Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BQA1}. Cytoplasm {ECO:0000250|UniProtKB:Q9BQA1}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Methylosome subunit pICln
- Serine/threonine-protein kinase RIO1
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein-associated protein B
- Protein arginine N-methyltransferase 1
- Cyclin-dependent kinase 4
- Coordinator of PRMT5 and differentiation stimulator
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MRKDTPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGSLLLGVSSLSGRCWVGSLWFFKDPSAAPNEGFCSAGVQTEAGVADLTWVGDKGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVTVLSSGTQAVSGSKDCCIKIWDLAQQVSLNSYRAHAGQVTCVAASPHKDSVFLSCSEDSRILLWDTRCPKPASQMACNASGYLPTALAWHPQQSEVFVFGDENGSVSLVDTKNASCTLSSAVHSQGVTRLVFSPHSVPLLTSLSEDCSLAVLDSSLSEVFRSRAHRDFVRDATWSPLNHSLLTTVGWDHQVIHHVVPLEPLPNPGPDSVVE
Protein: AT20289p (CG11037 protein) (CG11037-PA) (Q8T429)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Accessory gland protein Acp36DE
- Uncharacterized protein, isoform A
- IP20609p
- Accessory gland-specific peptide 26Aa
- GEO08953p1
- Serpin 28F
- Accessory gland-specific peptide 26Ab
- Lectin-29Ca
- Serpin 38F, isoform A
- procollagen-proline 4-dioxygenase
Sequence:
MEWHLVCCVLACTLVSTQVYGQEQEKIVLSLPDESGQPGKNLTLDVAQLAKIVLPSPHETRVIGGHVTTNAKLGGYLTALLYEDDFVCGGTLLNENIVLTAAHCFLGRMKASEWIVAAGISNLNQKGIRRHVKDFILSEQFREDDMNMDVAVVLLKTPLKAKNIGTLSLCSVSLKPGVELVVSGWGMTAPRGRGPHNLLRTVTVPIIHKKNCRAAYQPTAKITDSMICAAVLGRKDACTFDSGGPLVFKKQVCGIVSFGIGCASNRYPGVYTDVMYVKPFIEKSIKALLAKR
Protein: Phosphatidylinositol 4-kinase lsb6 (PI4-kinase) (PtdIns-4-kinase) (EC 2.7.1.67) (Q9UT42)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in endocytic and/or exocytic pathways.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphatidylinositol 4-kinase pik1
- Phosphatidylinositol 4-kinase stt4
- Phosphatidylinositol 4-phosphate 5-kinase its3
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Uncharacterized protein C3C7.01c
- Uncharacterized protein C19F5.03
- Phosphatidylinositol 3-kinase pik3
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphoinositide 3-phosphatase
- Inositol-1,4,5-trisphosphate 5-phosphatase 2
Sequence:
MESTFHSDTLDSFPNYQENSLNTNEEQTNPLESLRDGWASSNSSSSSSLLLPDENEGNEVFGSLKGLVTQSKFGQWANKLSKSLQARRRKSESISKPRVYYSVFMAPSWVLHAEKHWEEYPHYAGYDYKDYVRLLDATKEAIAHGVFPVLISKGSSGSYFVKNKVQKNIAVFKPKDEEPYGKLNPKWTKWFHRNLFPCFFGRSCLIPNTSYLSEAAACVLDRGLGLYLVPYTSVASISSPTFNYDYFARKAFLTRNKPLPEKTGSFQQFLDGFVVASKFFAQHPWPGTRHRETREYTESVASSEDFDIFDPFLAENEIETEFWTEELRLKFRFEFEKLVLLDYLMRNTDRNLDNWMIKICYEPCDNEEYYKSINLLSTNLTPNMSANSVDPAISQTSDFWKGPHFQIGAIDNSLAFPYKHPDSWRSFPYGWLSLPRSLFTQPFTEFTRQLFLHKLTSREWWEKLSDDLRNVFNQDLDFDEKMFSRQLSLVKGQAYNIVEVLKNPLMNIYDLLELPNLYVVEDVVRIEVNEPTSANSEEAEFGLPIKRDYGSILHPSCSQTFPPYPGSQLLQATPGRSFSSNAEALLPLNYITLLSKDSSSPKMLKDVIFERLQCASSNAVFSTC
Protein: Vigilin 1 (KH domain-containing protein vgl1) (O59810)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cell survival under thermal stress.
Subcellular location: Endoplasmic reticulum. Cytoplasm. Note=Under thermal stress, relocalizes from the ER to cytoplasmic foci that are distinct from P-bodies but contain stress granule markers.
Interaction partners:
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Small ribosomal subunit protein RACK1
Sequence:
MEHLSNLEQPTTMDSYDFQKLTNDENLQGTESQVPSGSKSASTNGLLSAASSAAGSSFGLTPSAILQQKHENAQQGKKQNNSKSFSKKPAIDVHSEDAFPTLLSKTGPSKPRIVSWVRKTASNTSVAGSDSVSRDKIPFSASSRASSTKSTLSSVKETDFVTETLILSPDNQAPRMSFVGKPNSVAEIVRTVMHQTSTRINVSTASKTKNTTFLIQGKTSAVKAARRQILKLIGRRETKTMPCPVFVVGAIIGTNGQNLKSIMDRTSTRIQIPKRNNTANESSDDAKKPEKEENSAASTLDDLEPQYEMTTITIEGDFEGVELAQKDIEAIINERTSNTTVRISHISTELYSLLRGPDGKNIKELEEGRDLKVQIPFAYLDPSAPVNPIVLSGEKSAVRECALYLQGQAEELLRTTIPTMLPIPRRQHRFINGEKGVGIQDILRKSGCSVILPPINGDSDVVSVRGPALNISEGIRLTLERANSTIVDAVNITTAYASSKNPFDIASIVARLFLRSRKLIPLEEECAVQYHLPKREELQSNSNKTVIIEISGKSQEAVREGRAKLLALVNQFPESKFYKVTIDPLLQRYVIGSKGKNLQKLRNEHQVELLVGEYGEEDPDVIVCYIGADDGKSPDQIQKELADLAESVKSSAEASAKIVSEIIQVPSVYHKHIVGPKGTTLNAIIGKSEENVIVQLGKVSYRPDSTDDDVYIRGFSKDVERVVSEIKQVVRDAKNHEILHSHVEEFDFPAQYSKNVIGKNGSNVSSLREDLGVQINVEEGHIRIQGIKKNVEETAARIKSQIEALIDDTILRVNIPNDFHRQLIGSNGKYVRRLEEKFSVRVRFPREDDSSNSTGNELMKPTSPDEVVIRGGKKSVAAAKQELLELYEYEKSIAYTSTIDIPSKAVSRVVGRNGSTVENIRTQFDVKIDIGDVSTEETTPVSVRGAKADVENAIKEISAIAEEVKNLVEKVIKIDREYHRYLIGPNGSKLQNTIKECGGSTDKTETARLISFSNGNSEEERNSVVLRGDKEIVEALETRLLEIVEELKNQVEEKIEVPQRCISSIIGRMGSTRRDIERKTSTMLNIPNVLDPEETVTITIVGSPENCEKAKEMIQEKVASQYTQMITVPDTVYESIMKGILMKKLRSDLKVFVDTPEIKPVQPTEVVLEDHEDGVFPWKLVTHDYTGSSSSEWAVRGHKENVEKAIASLEKSIKQVMENCIAYLGIPTNLHRRIIGSGGSIINKIRKIAQVKIDVPRTPGDEIVVVQGSRAGVVKAKDLIFERLQENQNQE
Protein: Guanine nucleotide-binding protein subunit gamma 4 (Heterotrimeric G protein gamma-subunit 4) (OsGGC3) (Protein DENSE AND ERECT PANICLE 1) (Protein ERECT POSE) (Q67UU9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems (Probable). The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (Probable). Involved in the regulation of plant architecture, panicle erectness, panicle and grain length, grain weight, and grain yield. Involved in the regulation of grain size.
Subcellular location: Nucleus {ECO:0000269|PubMed:19305410, ECO:0000269|Ref.2}. Cell membrane {ECO:0000269|PubMed:30441812, ECO:0000269|Ref.2}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein subunit gamma 2
- Guanine nucleotide-binding protein alpha-1 subunit
Sequence:
MGEEAVVMEAPRPKSPPRYPDLCGRRRMQLEVQILSREITFLKDELHFLEGAQPVSRSGCIKEINEFVGTKHDPLIPTKRRRHRSCRLFRWIGSKLCICISCLCYCCKCSPKCKRPRCLNCSCSSCCDEPCCKPNCSACCAGSCCSPDCCSCCKPNCSCCKTPSCCKPNCSCSCPSCSSCCDTSCCKPSCTCFNIFSCFKSLYSCFKIPSCFKSQCNCSSPNCCTCTLPSCSCKGCACPSCGCNGCGCPSCGCNGCGCPSCGCNGCGLPSCGCNGCGSCSCAQCKPDCGSCSTNCCSCKPSCNGCCGEQCCRCADCFSCSCPRCSSCFNIFKCSCAGCCSSLCKCPCTTQCFSCQSSCCKRQPSCCKCQSSCCEGQPSCCEGHCCSLPKPSCPECSCGCVWSCKNCTEGCRCPRCRNPCCLSGCLC
Protein: Zinc finger protein GLI1 (Glioma-associated oncogene) (Oncogene GLI) (P08151)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator. Binds to the DNA consensus sequence 5'-GACCACCCA-3'. Regulates the transcription of specific genes during normal development. Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling. Plays a role in cell proliferation and differentiation via its role in SHH signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:24076122}. Nucleus {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:2105456}. Note=Tethered in the cytoplasm by binding to SUFU (PubMed:10806483). Activation and translocation to the nucleus is promoted by interaction with STK36 (PubMed:10806483). Phosphorylation by ULK3 may promote nuclear localization (PubMed:19878745). Translocation to the nucleus is promoted by interaction with ZIC1 (PubMed:11238441). {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:19878745}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19706761}. Nucleus {ECO:0000269|PubMed:19706761}.
Interaction partners:
- Suppressor of fused homolog
- Kinesin-like protein KIF7
- Speckle-type POZ protein
- Protein smoothened
- F-box/WD repeat-containing protein 1A
- Sonic hedgehog protein
- Protein patched homolog 1
- Serine/threonine-protein kinase 36
- cAMP-dependent protein kinase catalytic subunit alpha
- Indian hedgehog protein
Sequence:
MFNSMTPPPISSYGEPCCLRPLPSQGAPSVGTEGLSGPPFCHQANLMSGPHSYGPARETNSCTEGPLFSSPRSAVKLTKKRALSISPLSDASLDLQTVIRTSPSSLVAFINSRCTSPGGSYGHLSIGTMSPSLGFPAQMNHQKGPSPSFGVQPCGPHDSARGGMIPHPQSRGPFPTCQLKSELDMLVGKCREEPLEGDMSSPNSTGIQDPLLGMLDGREDLEREEKREPESVYETDCRWDGCSQEFDSQEQLVHHINSEHIHGERKEFVCHWGGCSRELRPFKAQYMLVVHMRRHTGEKPHKCTFEGCRKSYSRLENLKTHLRSHTGEKPYMCEHEGCSKAFSNASDRAKHQNRTHSNEKPYVCKLPGCTKRYTDPSSLRKHVKTVHGPDAHVTKRHRGDGPLPRAPSISTVEPKREREGGPIREESRLTVPEGAMKPQPSPGAQSSCSSDHSPAGSAANTDSGVEMTGNAGGSTEDLSSLDEGPCIAGTGLSTLRRLENLRLDQLHQLRPIGTRGLKLPSLSHTGTTVSRRVGPPVSLERRSSSSSSISSAYTVSRRSSLASPFPPGSPPENGASSLPGLMPAQHYLLRARYASARGGGTSPTAASSLDRIGGLPMPPWRSRAEYPGYNPNAGVTRRASDPAQAADRPAPARVQRFKSLGCVHTPPTVAGGGQNFDPYLPTSVYSPQPPSITENAAMDARGLQEEPEVGTSMVGSGLNPYMDFPPTDTLGYGGPEGAAAEPYGARGPGSLPLGPGPPTNYGPNPCPQQASYPDPTQETWGEFPSHSGLYPGPKALGGTYSQCPRLEHYGQVQVKPEQGCPVGSDSTGLAPCLNAHPSEGPPHPQPLFSHYPQPSPPQYLQSGPYTQPPPDYLPSEPRPCLDFDSPTHSTGQLKAQLVCNYVQSQQELLWEGGGREDAPAQEPSYQSPKFLGGSQVSPSRAKAPVNTYGPGFGPNLPNHKSGSYPTPSPCHENFVVGANRASHRAAAPPRLLPPLPTCYGPLKVGGTNPSCGHPEVGRLGGGPALYPPPEGQVCNPLDSLDLDNTQLDFVAILDEPQGLSPPPSHDQRGSSGHTPPPSGPPNMAVGNMSVLLRSLPGETEFLNSSA
Protein: Thermoregulatory protein LcrF (P28808)
Organism: Yersinia pestis
Function: Transcriptional activator of the thermally regulated virulent yopE gene. LcrF activity could be modulated by the interaction with an inducer molecule serving as a temperature messenger. The availability of the messenger would in turn be controlled by a temperature-responsive process serving as a cellular thermometer.
Interaction partners:
Sequence:
MASLEIIKLEWVTPIFKVVEHSQDGLYILLQGQISWQSSGQTYDLDEGNMLFLRRGSYAVRCGTKEPCQLLWIPLPGSFLSTFLHRFGSLLSEIGRDNSTPKPLLIFNISPILSQSIQNLCAILERSDFPSVLTQLRIEELLLLLAFSSQGTLFLSALRHLGNRPEERLQKFMEENYLQGWKLSKFAREFGMGLTTFKELFGTVYGISPRAWISERRILYAHQLLLNGKMSIVDIAMEAGFSSQSYFTQSYRRRFGCTPSQARLTKIATTG
Protein: Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (Q19722)
Organism: Caenorhabditis elegans
Function: Involved in protein synthesis. Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Lysine--tRNA ligase
- Threonine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase
- Leucine--tRNA ligase
- Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein
- proline--tRNA ligase
Sequence:
MSKLYIDTDAGSDQHPGTEAQPLATLVQAMLISKNSGEFLMKKKSEEGESWEPAAKAAIKKAVKKYEAEVKKLEKAGCREKEAEEAQHAALEEAKKITFSLDKSLPEAKVIKIGESVQHRDQRVSIKAWVHRLRRQGKSLMFLVLRDGYGFLQCVLNDKLCQSYDAVTLSTETSVQVYGIIKALPDGKSAPDGHELTVDYWEVIGKAPAGGIDNVLNESAGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAEKSRTRRHLSEYQHVEAECAFITFDQLMDRIEALVCDTVDRLLADPVTKSLIEFVNPGYKAPARPFKRMPYKEAIEWLQKNDVRNEMGEKFVYGEDIAEAAERRMTDTIGVPILLNRFPHGIKAFYMPRCADDNELTESVDLLMPGVGEIVGGSMRIWKEDQLLAAFEKGGLDSKNYYWYMDQRKYGSVPHGGYGLGLERFICWLTDTNHIRDVCLYPRFVGRCAP