wanglab/gogpt-training-data huggingface dataset:
Protein: Early growth response protein 1 (EGR-1) (Zinc finger protein ZENK) (O73694)
Organism: Serinus canaria (Island canary) (Fringilla canaria)
Function: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Mediates responses to ischemia and hypoxia; regulates the expression of proteins that are involved in inflammatory processes (By similarity). Plays a role in regulating the expression of circadian clock genes (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm {ECO:0000250|UniProtKB:P18146}.
Interaction partners:
Sequence:
CDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGR
Protein: Vertnin (Q08C99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000269|PubMed:28928283}.
Interaction partners:
- Transmembrane protein 192
- Protein Wnt
- Prospero homeobox 2.
- ATP-binding cassette sub-family D member 4, member 4)
Sequence:
MIQRAEAVLSVLGELQEATECVGLDALTKVAVEVEQVLAPFPLPTAPCSEISSWQGIDAVAHRLYPGDAPTGLLPLVCKGEGNLLFDAASMLLVGSTSLSLELQVRAVVEMLIWKRYYLCGMIDSKVMLQAARFSLCAEESQDMLNLPIQVLEAIFDADVKASCFHGSFANMWHVYALASVLQCNIYSVYPMYNLKIRPYFNRLIRPRIWSKDTEPLTLHIMWSGDLEAGSVFKPHKFVALIHASDLKIGSPNSEQRMPLVKSLELQNQDTQLSYSNLKNKFNITKSTFYRWKRQSIEYHKKSVARYEAKHFFLTSYKQGKLIPLSQFKELFPEIPRSTYYAWKQELVSCCSLSGGSTGELSPGDSTEQDYWSSPEVKKTPGQGSFANMLAFKYEKLEGERNQNVTLMQEAKKSLQDCIVANTSFPYRIFKRKFPGISRSTYYNWRREAMLFIPFKEHSGSSEEGSDADKSQSPRSQMSPSKFDRQKLSPRVRISRRKHRSLRLAYHHRKMLREEAKMHIRRSKMSFIKFKLKFPTVSSSFYWLWRVSLNRKPEKPAVMSNSEESKSLAISPDVFQKIKTQGMFSFDGNIDCLNGQTEFTMPEYSPPDQSTNDHMFVMDVVALANFKAKAKLFLQQRFEEKAFPTFKEFRSYFPLTPRSTYYMWKRALHHGVPLIHA
Protein: Hydroxyproline O-arabinosyltransferase 1 (EC 2.4.2.58) (Q8W4E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase involved in the O-arabinosylation of several proteins including extensins and small signaling peptides. Catalyzes the transfer of the initial L-arabinose to the hydroxyl group of Hyp residues. Contributes redundantly with HPAT2 and HPAT3 to arabinosylation of EXT3.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:24036508}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Arabinosyltransferase RRA1
- Arabinosyltransferase XEG113
- Arabinosyltransferase RRA3
- Hydroxyproline O-arabinosyltransferase 2
- Hydroxyproline O-arabinosyltransferase 3
- Arabinosyltransferase RRA2
- Prolyl 4-hydroxylase 5
- Prolyl 4-hydroxylase 13
- Prolyl 4-hydroxylase 2
- Extensin-3
Sequence:
MGCGGTLFYPLLITLSVALITYNIIISANAPLKQGFPGRSSSSDISIDPVIELPRGGGSRNNDGKRIRLFHTAVTASDSVYNTWQCRVMYYWFKKIQASAGPGSEMGGFTRILHSGKPDQYMDEIPTFVAQPLPSGMDQGYVVLNRPWAFVQWLQQTDIKEDYILMSEPDHIIVKPIPNLAKDGLGAAFPFFYIEPKKYEKVLRKYYPEVRGPVTNIDPIGNSPVIVGKDALKKIAPTWMNVSLAMKKDPEADKAFGWVLEMYAYAVSSALHGVSNILHKDFMIQPPWDIEVGDKYIIHYTYGCDYDMKGKLTYGKIGEWRFDKRSYDSKPPPRNLTMPPPGVSQSVVTLVKMINEATANIPNWGS
Protein: 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5) (O00231)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome regulatory subunit 10B
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-5
- 26S proteasome non-ATPase regulatory subunit 2
Sequence:
MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTHLAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVERKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALETIQNMSKVVDSLYNKAKKLT
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q4V5H1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SD09427p
- Precursor RNA processing 3, isoform A
- NHP2-like protein 1 homolog
- U4/U6 small nuclear ribonucleoprotein Prp31
- Small nuclear ribonucleoprotein F
- FI17537p1
- Probable small nuclear ribonucleoprotein Sm D1
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm2
Sequence:
MPNWNQIQSQLRSSNNPVVFFDIAVGTTEIGRMIFELFADTVPRTAENFRQFCTGEYRPDGVPIGYKGASFHRVIKDFMIQGGDFVQGDGTGVTSIYGNTFGDENFTLKHDSPGLLSMANSGKETNGCQFFITCAKCNFLDGKHVVFGRVLDGLLIMRKIENVPTGPNNKPKLPVTISQCGQM
Protein: At4g02800 (GRIP/coiled-coil protein) (Q9SY05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAASVETPSPNHTNNEGTRLNMVSATSFDSSSPSVSPSSDKRLWSNVRNRVDVLLEENSKNHKPVTNTIAIESERSKRFKNDSMLLLKGFDSVSHTLSLLSSNLDNALQGVRELAKPPSYSEILHSNLKADQIQRQQKEEDEEEEESKGKKRKHESDVEQTEDSSNEEEKRPKERKIMKKAKNIAISMAAKANSLARELKTIKSDLSFIQERCGLLEEENKRLRDGFVKGVRPEEDDLVRLQLEVLLAEKARLANENANLVRENQCLHQMVEYHQITSQDLSPSYEQVVQGFCLDFSSPLPQYDDEEEEHETRARDVSKALNESFEKAEEEQY
Protein: tRNA (guanine(26)-N(2))-dimethyltransferase 2 (EC 2.1.1.216) (tRNA 2,2-dimethylguanosine-26 methyltransferase 2) (tRNA(guanine-26,N(2)-N(2)) methyltransferase 2) (tRNA(m(2,2)G26)dimethyltransferase 2) (Q9SRU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Interaction partners:
- tRNA-uridine aminocarboxypropyltransferase
- tRNA-uridine aminocarboxypropyltransferase A
- Probable isoaspartyl peptidase/L-asparaginase 3
- ETFB lysine methyltransferase
- F9L1.6
- tRNA-dihydrouridine synthase
- Protein arginine N-methyltransferase 1.6
- Calmodulin-lysine N-methyltransferase
- Protein TORMOZ EMBRYO DEFECTIVE
- Phosphatidylinositol N-acetyglucosaminlytransferase subunit P-like protein
Sequence:
METDLNDYTVIKEGEAEILMHKKNQVFFNKAQVNNRDMSIAVLREFLSKRKQEHEAKSSKRTRPASKVIEKDASEASKEETPSENGMNNGDHEVASEDGPSSVSKDPAKTTERFAPREPKPPKVLEALSASGLRALRYAREIEGIGQVVALDNDLASVEACQRNIKFNGSVAISKVESHHTDARVHMLTHPKEFDVVDLDPYGSPSIFLDSAIQSVTDGGLLMCTATDMAVLCGGNGEVCYSKYGSYPLRAKYCHEMALRILLASIESHANRYKRYIVPVLSVQMDFYVRVFVRVYTSASAMKNTPLKLSYVYQCIGCDSFHLQPVGRSLPKNNSVRYLPAIGPVVKQDCNHCGKKYNMGGPIWSAPMHDPEWVTSILNSVKSMKDRYPAYDRISAVLTTVSEELLDVPLFLSLHNLCATLKCISPSAAMFRSAVINANYRISGTHVNPLGMKTDAPMEVIWDIMRCWVKNHPIKAQSPEQPGSVILSKEPSHEVDFSRHIGSLSKAQAKKVARFLPNPEKHWGPKLRAGRQITSKHVSLIGHEAVNGHLSQHHEELKEEDEEAEPEDNVQDKVDPKRQKTATDNITST
Protein: Mechanosensitive ion channel protein 10 (Mechanosensitive channel of small conductance-like 10) (MscS-Like protein 10) (AtMSL10) (Q9LYG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18485707}; Multi-pass membrane protein {ECO:0000269|PubMed:18485707}.
Interaction partners:
- Mechanosensitive ion channel protein 1, mitochondrial
- Protein MID1-COMPLEMENTING ACTIVITY 1
- Mechanosensitive ion channel protein 2, chloroplastic
- Protein MID1-COMPLEMENTING ACTIVITY 2
- Mechanosensitive ion channel protein 3, chloroplastic
- Hyperosmolality-gated Ca2+ permeable channel 1.1
- Mitochondrial substrate carrier family protein
- Calpain-type cysteine protease DEK1
- Hyperosmolality-gated Ca2+ permeable channel 1.2
Sequence:
MAEQKSSNGGGGGGDVVINVPVEEASRRSKEMASPESEKGVPFSKSPSPEISKLVGSPNKPPRAPNQNNVGLTQRKSFARSVYSKPKSRFVDPSCPVDTSILEEEVREQLGAGFSFSRASPNNKSNRSVGSPAPVTPSKVVVEKDEDEEIYKKVKLNREMRSKISTLALIESAFFVVILSALVASLTINVLKHHTFWGLEVWKWCVLVMVIFSGMLVTNWFMRLIVFLIETNFLLRRKVLYFVHGLKKSVQVFIWLCLILVAWILLFNHDVKRSPAATKVLKCITRTLISILTGAFFWLVKTLLLKILAANFNVNNFFDRIQDSVFHQYVLQTLSGLPLMEEAERVGREPSTGHLSFATVVKKGTVKEKKVIDMGKVHKMKREKVSAWTMRVLMEAVRTSGLSTISDTLDETAYGEGKEQADREITSEMEALAAAYHVFRNVAQPFFNYIEEEDLLRFMIKEEVDLVFPLFDGAAETGRITRKAFTEWVVKVYTSRRALAHSLNDTKTAVKQLNKLVTAILMVVTVVIWLLLLEVATTKVLLFFSTQLVALAFIIGSTCKNLFESIVFVFVMHPYDVGDRCVVDGVAMLVEEMNLLTTVFLKLNNEKVYYPNAVLATKPISNYFRSPNMGETVEFSISFSTPVSKIAHLKERIAEYLEQNPQHWAPVHSVVVKEIENMNKLKMALYSDHTITFQENRERNLRRTELSLAIKRMLEDLHIDYTLLPQDINLTKKN
Protein: ATP-dependent RNA helicase HAS1 (EC 3.6.4.13) (Q5AK59)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis protein ERB1
- RNA-binding GTPase
- Cic1p
- Pescadillo homolog
- rRNA-binding ribosome biosynthesis protein
- Ribosome biogenesis protein YTM1
- Nucleolar GTP-binding protein 1
- Ribosome assembly factor mrt4
- Nucleolar protein 2
- mRNA-binding ribosome synthesis protein
Sequence:
MAKTTKVKGNKKKSDTSKVVSKVSRKRSHEDSESEVEDNEKVVEELDADFDEVAGLLGDDIEDPESKSQSKKEKQKAKDEAKLEQLTKPQVSNEVPDNDNDDDSSEDVLFENADFSEPTMKAIKEMGFTKMTKVQAKTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLYSLKIKPRNGTAVIIITPTRELALQIFGVARELMQFHSQTCGIVIGGADRRQEATKLAKGVNLLVATPGRLLDHLKNTQFVFSNLKALVIDEADRILEIGFEDEMKQIIKVLPNENRQSMLFSATQTTKVEDLARISLRPGPLYINVVPEKDVSTADGLEQGYVVCDSDKRFLLLFSFLKRNVKKKIIVFLSSCNSVKFYSELLNYIDLPVLDLHGKQKQQKRTNTFFEFCNAKQGILVCTDVAARGLDIPAVDWIVQFDPPDDPRDYIHRVGRTARGTQGKGKSLMFLTPSELGFLRYLKAAKVPLNEYEFPANKIANIQSQLTKLIKTNYLLNQSAKDGYRAYLQAYASHGLKTVYQIDKLDLKKVSASFGLDQVPRVNLSIGGTKTKKQKRS
Protein: Phosphatidylserine decarboxylase proenzyme 2 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain] (Q5AK66)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Important for virulence.
Subcellular location: Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- diacylglycerol cholinephosphotransferase
- Phosphatidylethanolamine N-methyltransferase
- Lysophospholipid acyltransferase
- Phospholipase
- PNPLA domain-containing protein
- Bta1p
Sequence:
MRSSGYLNSNNGSSSSLESTNVNKSTDKNQLYLKVVCNCATDLVPQDTTGTGSESKKAYSSSKSINPVLVVQLNNTIKSTSKKLNTNQPSWNDELYMPLKNQDDSSLLIFSVWDKHTRYKNYLGELRLNVKDIFVDNGNFVDKTELKWYHLNSNTKYHSFVTGSILAGFELVIKNKKKRFHSSYNDKFQQLSIDSDVESAFKKWLSSLTKPTIYSVNNKINPNDQGFYDDELVNEFELESVLTERSKKSHLNVPGGNGLLSVPGDDCHDAGSFSDASFLSDGGYASDASANLFDQKETSSDSKKSRIKSKMRLRRSKQEYENFELASRQVLGVVFIEIVSCEDLPPYKNFTRTSFDMDPFVVVSFGKKTFRTGWKRHTLNPVFNERLAFELLPHESNFSIQFLVLDKDHFSFHDNVAHISLPLRTLTEYATAKPTEGDSSDVNTSDSTSFSQTGNGFTTEDTEFPENDSVQIIENETPSNKQSRKRYLSRKKVVGTQLDLKKFKAMSLSLQLHDQKYIGKYAPKLKIRVRFETYTELRKKFWRVLLEESNSTPENRDSCDYIELISLLDTLGCVNSDELVELFYSNLGKSSWGGDLLTFDEIIDQMETYVNQNVESGKVKIFEFEKCPICNEKRVSKKQDLDIITHFAICASKDWSVVGKLLSSSYVTPTQATKKWFTKALIKLTYGKYKLGGNSANILVQDRMTGIIVEEKMSVYVRLGIRLLYKGLDKARSKRVRILLKNMSIKQGKKFDAPQSKSDIASFIKFHKLDLDECEIDDPSQFATFNDFFYRKLKPGAREIEDEKNSKIVTSPADCRSVVFESIDKATQLWIKGAGFTIPKLIHNDHSMRVSSYTLGIFRLAPQDYHRFHSPVDGVIESIKHIDGEYYTVNPMAIRSELDVFGENVRTIVTIKTKDFGNIYFIAVGAMMVGSIVLTKDTGYEISKGEELGYFKFGGSTVLLLIESDKFKFDTDLVKNSSSGLETLLRVGQSIGHSPDVEEYKRDHISFDKLDKSKQLRLIRVLTGGDLKDKHKLSNWEATKIDMEDFQEIEDEEVFDKDMPDEDASIKSED
Protein: Sodium-driven chloride bicarbonate exchanger (Solute carrier family 4 member 10) (Q6U841)
Organism: Homo sapiens (Human)
Function: Sodium/bicarbonate cotransporter which plays an important role in regulating intracellular pH. Has been shown to act as a sodium/bicarbonate cotransporter in exchange for intracellular chloride (By similarity). Has also been shown to act as a sodium/biocarbonate cotransporter which does not couple net influx of bicarbonate to net efflux of chloride, with the observed chloride efflux being due to chloride self-exchange. Controls neuronal pH and may contribute to the secretion of cerebrospinal fluid (By similarity). Reduces the excitability of CA1 pyramidal neurons and modulates short-term synaptic plasticity (By similarity). Required in retinal cells to maintain normal pH which is necessary for normal vision (By similarity). In the kidney, likely to mediate bicarbonate reclamation in the apical membrane of the proximal tubules (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:Q5DTL9}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q80ZA5}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q5DTL9}. Cell projection, axon {ECO:0000250|UniProtKB:Q5DTL9}. Perikaryon {ECO:0000250|UniProtKB:Q5DTL9}. Presynapse {ECO:0000250|UniProtKB:Q5DTL9}. Postsynapse {ECO:0000250|UniProtKB:Q5DTL9}. Note=Detected in dendrites and axon terminals of retinal OFF bipolar cells and in axon terminals of ON bipolar cells (By similarity). In amacrine cells, located in the perikaryon (By similarity). Also detected in basal and apical dendrites of hippocampal pyramidal cells (By similarity). Localized to GABAergic inhibitory presynapses (By similarity). {ECO:0000250|UniProtKB:Q5DTL9}.
Interaction partners:
Sequence:
MEIKDQGAQMEPLLPTRNDEEAVVDRGGTRSILKTHFEKEDLEGHRTLFIGVHVPLGGRKSHRRHRHRGHKHRKRDRERDSGLEDGRESPSFDTPSQRVQFILGTEDDDEEHIPHDLFTELDEICWREGEDAEWRETARWLKFEEDVEDGGERWSKPYVATLSLHSLFELRSCILNGTVLLDMHANTLEEIADMVLDQQVSSGQLNEDVRHRVHEALMKQHHHQNQKKLTNRIPIVRSFADIGKKQSEPNSMDKNAGQVVSPQSAPACVENKNDVSRENSTVDFSKGLGGQQKGHTSPCGMKQRHEKGPPHQQEREVDLHFMKKIPPGAEASNILVGELEFLDRTVVAFVRLSPAVLLQGLAEVPIPTRFLFILLGPLGKGQQYHEIGRSIATLMTDEVFHDVAYKAKDRNDLVSGIDEFLDQVTVLPPGEWDPSIRIEPPKNVPSQEKRKIPAVPNGTAAHGEAEPHGGHSGPELQRTGRIFGGLILDIKRKAPYFWSDFRDAFSLQCLASFLFLYCACMSPVITFGGLLGEATEGRISAIESLFGASMTGIAYSLFGGQPLTILGSTGPVLVFEKILFKFCKEYGLSYLSLRASIGLWTATLCIILVATDASSLVCYITRFTEEAFASLICIIFIYEALEKLFELSEAYPINMHNDLELLTQYSCNCVEPHNPSNGTLKEWRESNISASDIIWENLTVSECKSLHGEYVGRACGHDHPYVPDVLFWSVILFFSTVTLSATLKQFKTSRYFPTKVRSIVSDFAVFLTILCMVLIDYAIGIPSPKLQVPSVFKPTRDDRGWFVTPLGPNPWWTVIAAIIPALLCTILIFMDQQITAVIINRKEHKLKKGCGYHLDLLMVAVMLGVCSIMGLPWFVAATVLSITHVNSLKLESECSAPGEQPKFLGIREQRVTGLMIFILMGSSVFMTSILKFIPMPVLYGVFLYMGASSLKGIQFFDRIKLFWMPAKHQPDFIYLRHVPLRKVHLFTIIQMSCLGLLWIIKVSRAAIVFPMMVLALVFVRKLMDLLFTKRELSWLDDLMPESKKKKLEDAEKEEEQSMLAMEDEGTVQLPLEGHYRDDPSVINISDEMSKTALWRNLLITADNSKDKESSFPSKSSPS
Protein: Heavy metal-associated isoprenylated plant protein 18 (AtHIP18) (Protein maternal effect embryo arrest 56) (Q9T0K9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable heavy-metal-binding protein (By similarity). Required for female gametophyte development and function.
Interaction partners:
- At2g44240/F4I1.5
- WAT1-related protein At1g09380
- High mobility group B protein 13
- Cyclin-D4-2
- Gibberellin 20 oxidase 5
- Protein farnesyltransferase subunit beta
Sequence:
MVTGNFNLEKLLKNLKKKTGKKAEILTMNEKVEKEDVVQNEANEQETVTKKNEEGDIVDKKDETPEVEEKIDKPETSTRKLEIHIAFLSEKYEADIGKVISKFEGVKTCKVDVENKKVVITGDFDEEKLWKELEEKMRKRIVKMEKEKKDDEPITKDEENEIDRGVYMNPSSDDEKEMARWMMFSDENPNACSIS
Protein: Partner of Numb (O96561)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLETKSIAALAFTETPRKRKRETLYKNAAPPPNPQQQPPEKDAQDAAVASTESCFTNAAFSSTPKKLMVARRRLAKENSQPNPFPGLEVKSIADLAQKQQHQQHHQQQQQQQQKLPTNPFEVLRPAPKKKKRASACFENPGSRNLELPEKQFNPYEVVVRSATTPAKGFVNPALNLRGSDAPASLNPFEIHRPSEASEAACNPSGVANPALADRDSEEQLPTSLKIGLPFTPTLGCRIDFHGMSLTQLTPSKLLAEKLVFSPVPAPKRSLGAISEESSMDIGKELDRYQLELENSINEAKLRKNGVLVDRELPRNSLEVELPKNTKVSLVMETNTQELMMQEVVTVDTQVERRLVCTRRRTLTEISEASEVEEDTEKLLEQDREAEVILEQEKILEQEMVSERERHLTREKQLKQETLLEREKHLEREKLQEKLHEQLREKLQERAKHLEKEKLEEEELLERQLEEEREKEPTDGDVAYASESESDDEPDDLDFKAPARFVRAYGPAALPSKAASKESLQSIGSSKSAKSAEVKPSIGMKGMIRKSIRRLMHPTSHTTPSEVKSEDKDEHGHGQGHGQHNILNSIRHSLRRRPQKAAELEEQMEPVLADVSIIDTSERTMKLRSSVAQTEYMTIEQLTNEKKHSLRNSIRRSTRDVLRHVFHKSHDAYATAK
Protein: LD19058p (Q8MSW8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLCKQNQTYDHPDKERMIVALDLLSGLAEGLDRHIETLVANSNIMHLLYQCMQDVLPEVRQSSFALLGDLTKACFPHVHPFMADFFPILGQNLNPDFISVCNNATWAIGEICMKLGEETKQYIRLVLSDLFIIINRPNTPKTLLENTAITIGRLGYVCPVEVAPYLPEFVRQWCTSLRHIRDNDEKDSAFRGMCHMITVNPAGVVADFIFFCDAIASWVNPPEDLHQMIQKILHGFKTQVGEENWRRFVEQFPPTLAERLTTMYNI
Protein: Toxin YjjJ (Putative DNA-binding transcriptional regulator YjjJ) (Putative serine/threonine kinase toxin YjjJ) (EC 2.-.-.-) (P39410)
Organism: Escherichia coli (strain K12)
Function: Toxic when overexpressed in E.coli, leading to long filamentous cells. The toxic effect is neutralized by non-cognate antitoxin HipB. Does not seem to inhibit DNA, RNA or protein synthesis, and unlike paralogous toxin HipA its toxic activity is not counteracted by overexpression of GltX. Binds DNA. Might be a protein kinase (By similarity).
Interaction partners:
Sequence:
MSELTDLLLQGPRSAPELRQRLAISQATFSRLVAREDRVIRFGKARATRYALLRPYRGIERIPVWRVDDTGKAHKFADIRLCWPQGSCLVTGADGDEQWFDGLPWYLTDLRPQGFLGRAWGRKLAAQLNLTDDIRLWQEEDVLYALTVFNGEYTGGWLVGEGNYQRWITAQHPAEIPLDQKLTHYEQLASDALAGEIVGSSAGGEQPKFTYYAQTPSGNKHVLVKFTVPQQTAVSQRWGDLLIAESIAAQILRDGGIHAIESTVLVTSNRQVFLEAERFDCKGNDGRLPIVSLEAVQSEFISSPGSWPQAMRRLCEQQLVTHQSVAQTEVIWAFGRLIANSDMHAGNLSFYLSEPPFALTPVYDMLPMVYAPNSAGMLRDAAIEVKFDLNVSKSAWLTAIPLAQQFWQTVARDPRISEAFRHIAQEMPEKIRQIEEKVARMGG
Protein: Phosphatidylinositol-3-phosphatase myotubularin-2 (AtMTM2) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64) (F4JWB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphatase with phosphoinositide 3'-phosphatase activity that can use phosphatidylinositol-3-phosphate (PtdIns3P) and phosphatidylinositol-3,5-diphosphate (PtdIns3,5P(2)) as substrates and produces phosphatidylinositol-5-phosphate (PtdIns5P); participates in pathway(s) that transfer gene regulatory signals to the nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22324391}. Note=Highly concentrated at the peripheral lobes of the epidermal cells.
Interaction partners:
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Phosphatidylinositol 3-kinase VPS34
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 4-kinase beta 1
- Phosphoinositide phosphatase SAC3
- Phosphoinositide phosphatase SAC5
- Phosphoinositide phosphatase SAC4
- Phosphoinositide phosphatase SAC2
- Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1D
Sequence:
MTALRPLSGRSRSLRCSSEKMEGTGSWDVLEWTKLDSASWSGSYSNLDCLLESERIIFEACGVILINTDEAGTLLLSNFRILFLSEGTRKLVPLGTIPFVAIEKFNKLAPKVQSNKYHNNENAPTRLLQVTGKDMRIVVYGFRPGTKQRHTVVDTLLRCNKPERVWDLYAFTCGPSQFGNTNPKERLLNEYFRLLGKSSQRASMNMIEDGSFTLSNDLWRITNLNSNYDLCQSYPFALMVPKSISDEELLQTSTFRARCRLPVISWCHPGSGAVIARSSQPLVGLMMNMRSNSDEKLVASFCTQLAGHKGARRKLYIVDARPRKNALANGAKGGGSESSSNYLQSEIVFLGIDNIHAMRESFSRLRDYLDMHGTTSSDGTSSFLRHGGWTWGGGNLSSMSASVSVLGDSGWLSHIQSILAGVAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFSGFQALVEKDWLSFGHPFSDRVGMPNVSESGNFELPIQSSSARSFPSSPVRQSPGSAAAQSSSSSYGLNNYSPIFLQWLDCISQLMRMYPSAFEFSPTFLVDFIDCLLSCRFGNFLCNSEKERQQCGISETCGCIWAYLADLRSSSGTSHVHCNPFYDPSRYDGPLLPPAAALAPTLWPQFHLRWACPVEPNVTETEDQCRAMTVKYSEMKKEKEEAERKVDELSSAMESLNEELLNERDISRAARESAKRATKERAVISRAVQSLGCKVKFTRNGDCTVEVEDGPQKCSHSIPQKQSEDNTTDVSESISSVTEQNVCEAVCPLRTREGTCRWPDAGCARIGNQFLGLKTNFEAFDNLCVYDSYFTAE
Protein: Serine/threonine-protein kinase YPK1 (EC 2.7.11.1) (J9W0G9)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Probable serine/threonine-protein kinase which may act in the sphingolipid-mediated signaling pathway. May act downstream of TORC2 (TOR complex 2) and PDK1 to regulate sphingolipid metabolism.
Interaction partners:
Sequence:
MMSWKFGKKFKEGGFLSGKHHSSNNNSPSDTSRSTTPTPGNPHPEDAVKPPVPRSGMLKIRVTAAKGLSLPQGVSVPAPVQEALTTHPTLASRIATSPPTAIVKAAGANRDSLQRRQVWWLPYLVLEFDKNEVLVDALGGDLASPVWMYSATFDVSRISEISATVYLRTREPHAEGREKSNGEGEGEDMGNSDLCLGSIRFTPNLDSLRVTDDWVTVQGGGGSGSINVQVSFKPASGQILTIDSFELLKVIGKGSFGKVMQVRKRDTLRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVNCPFIVPLKFSFQSKEKLYLVLAFINGGELFHHLQREGKFNETRSRFYSAQLLLALEHLHSFNVIYRDLKPENILLDYAGNIALCDFGLCKLNMSNSDTTNTFCGTPEYLAPELLSGHGYTKCVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILTEPLRFPDGVRSEARSLLTGLLNRDPRQRLGVNGAQDIKNHPFFAKHINFTKLWNKQIQPPFKPAVASAIDTSNFDEEFTNEVPLDSVVDDSHLSQTVQQQFEGFSWSVSPLGESVGRY
Protein: Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.11.23) (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (Protein kinase minibrain homolog) (MNBH) (RP86) (P85051)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Plays an important role in double-strand breaks (DSBs) repair following DNA damage. Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A. May play a role in a signaling pathway regulating nuclear functions of cell proliferation (By similarity). Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits p53/TP53 activity and apoptosis. Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434' (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11311120}.
Interaction partners:
Sequence:
QPSISDQQVSALPYSDQIQQPLTNQVMPDIVMLQRRWMDRYEIDSLIGKVEQEWVAIKAFLNQAQIEVRHDTEMKYYIVHLKIVDFGSSCQLGQRIVEVLGIPPAHILDQAPKFFEKLPDGTWSLKKLHNILGVETGGPGGRFKDLILRMLDYDPKIQPYYALQHSFFKQETGIAGHPTYQFSANTGPAHYMTEGHLAMR
Protein: DNA N-6-adenine-methyltransferase (DAM) (EC 2.1.1.72) (Orphan methyltransferase M.EcoT1Dam) (M.EcoT1Dam) (Q38156)
Organism: Escherichia phage T1 (Bacteriophage T1)
Function: Methyltransferase that methylates adenine residues in the dsDNA sequence 5'-GATC-3'. May prevent degradation of viral DNA by the host restriction-modification antiviral defense system.
Interaction partners:
Sequence:
MKDFNDIETIDFAETGCSFTREAIASGGYYQALKTPTCKEISGRRYKGTNTPDAVRDLWSTPREVIAYLEGRYGKYDLDAAASEENKVCEKFYSQETNCLKRWWGKNKHVWLNPPYSRPDIFVKKAIEQMEHNNQIDMLLPADNSTAWFTEARQNAAEIIWIEADLTEDIDGNEYARSGRLAFISGETGKAVDGNNKGSVIFIMRELKEGEVQQTHYIPITSICPSVKNKRAKVRKVD