wanglab/gogpt-training-data huggingface dataset:
Protein: Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A) (Q8R071)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P23677}.
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol polyphosphate-5-phosphatase A.
- Calmodulin-1
- Inositol-tetrakisphosphate 1-kinase
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Inositol polyphosphate 5-phosphatase K
- Kinase
- Inositol-trisphosphate 3-kinase C
- Multiple inositol polyphosphate phosphatase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
Sequence:
MTLPGRPTGMARPRGAGPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAKRRGGQVPNGLPRAAPAPVIPQLTVTSEEDVTPASPGPPDQEGNWLPAAGSHLQQPRRLSTSSLSSTGSSSLLEDSEDDLLSDSESRSRGNVQLETSEDVGQKSHWQKIRTMVNLPVMSPFRKRYSWVQLAGHTGSFKAAGTSGLILKRSSEPEHYCLVRLMADVLRGCVPAFHGIVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVTRVFEEFMQGDAEVLRRYLNRLQQIRDTLEISDFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER
Protein: Flap endonuclease 1-B (FEN-1-B) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-B) (xFEN-1b) (P70054)
Organism: Xenopus laevis (African clawed frog)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
Sequence:
MGIHGLAKLIADVAPAAIKEHDIKSYFGRKVAVDASMCIYQFLIAVRQDGNMLQNEEGETTSHLMGMFYRTIRMLEHGIKPVYVFDGKPPQMKSGELAKRSERRAEAEKLLEAAEEAGEVENIEKFNKRLVKVTKQHNEECKKLLSLMGIPYVDAPCEAEATCAALVKAGKVYAAATEDMDALTFGTPVLLRHLTASEAKKLPIQEFHLNRVFQDIGINHEQFVDLCILLGSDYCETIRGIGPKRAIDLIRQHKTIEEIIDNIDLKKYPIPENWLHKEARQLFLEPEVIDADITELKWTEPDEEGLVAFMCGEKQFSEDRIRNGAKKLAKNRQGSTQGRLDDFFKVTGSISSTKRKEVESKGSTKKKSKTGGTPAGKFKRGK
Protein: Protein lon-1 (Q09566)
Organism: Caenorhabditis elegans
Function: Regulates body size morphogenesis, but does not affect male tail development.
Interaction partners:
- Serine/threonine-protein kinase receptor sma-6
- Cuticle collagen lon-3
- Trifunctional purine biosynthetic protein adenosine-3
- Protein dbl-1
- LONg
- Cell surface receptor daf-4
- SCP domain-containing protein
- Leucine-rich repeats and immunoglobulin-like domains protein sma-10
Sequence:
MNYLLTALIALLAPISVAYNVPHGFLTGEAVTSHSGPNDLDGELPATDEVKREKRGYFFPSHFQSDSGLLSRSEHPNEYLKKWITHEHNRYRRMVPASDMNMLYWSDELAASAQRHADTCDFRHSRGRINVGENIWAAPYSNYSDAISIWFNEVHNPRCGCNHAYKHCCGHYVQVVWAKTNLVGCGFSRCRDVQGVWGRGHRNVFVCHYNPQGNTVFVTARGQLYAMPAFTWASGDNGKCSNCPANAPACYQGLCYMPKNYEAPTTTTESTTTSTTTEEPTTTCEPDEPEAEGADNNQEEEEENNDGFRMRV
Protein: Vacuolar zinc transporter ZRC1 (Zinc resistance conferring protein 1) (Zinc/cadmium resistance protein ZRC1) (P20107)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuolar transporter that regulates zinc homeostasis by mediating zinc transport and storage into the vacuole. ZRC1 senses zinc availability in the cytosol, which might be performed through the histidine repeat motifs, and transports zinc from the cytosol to the vacuole if zinc in cytosol is abundant, confering resistance to zinc toxicity. Plays a role in resistance to zinc shock resulting from sudden influx of zinc into cytoplasm when ZRT1 and ZRT2 are induced in response to zinc depletion.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11263974, ECO:0000269|PubMed:9712830}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vacuolar zinc transporter COT1
- Zinc-regulated transporter 3
- Zinc-regulated transporter 2
- Zinc-regulated transporter 1
- Protein ZRG17
- Zinc-responsive transcriptional regulator ZAP1
- Low-affinity Fe
- Metal resistance protein YCF1
- Protein CCC1
- Zinc transporter YKE4
Sequence:
MITGKELRIISLLTLDTVFFLLEITIGYMSHSLALIADSFHMLNDIISLLVALWAVDVAKNRGPDAKYTYGWKRAEILGALINAVFLIALCFSIMIEALQRLIEPQEIQNPRLVLYVGVAGLISNVVGLFLFHDHGSDSLHSHSHGSVESGNNDLDIESNATHSHSHASLPNDNLAIDEDAISSPGPSGQIGEVLPQSVVNRLSNESQPLLNHDDHDHSHESKKPGHRSLNMHGVFLHVLGDALGNIGVIAAALFIWKTEYSWRYYSDPIVSLIITIIIFSSALPLSRRASRILLQATPSTISADQIQREILAVPGVIAVHDFHVWNLTESIYIASIHVQIDCAPDKFMSSAKLIRKIFHQHGIHSATVQPEFVSGDVNEDIRRRFSIIAGGSPSSSQEAFDSHGNTEHGRKKRSPTAYGATTASSNCIVDDAVNCNTSNCL
Protein: Methylenetetrahydrofolate reductase (Q5B0P7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Methylenetetrahydrofolate reductase
- Methylenetetrahydrofolate dehydrogenase [NAD
- Serine hydroxymethyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Aminomethyltransferase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Homocysteine S-methyltransferase
- Patatin-like serine hydrolase, putative
- Thymidylate synthase
- Glycine cleavage system P protein
Sequence:
MHIKEKLAQNEAAGKIGISFEFFPPKTAQGVQNLYDRMDRMHGLGPSFIDITWGAGGRLSDLTCEMVNVAQSVYGLETCMHLTCTDMPQERVDAALQAAYKAGCTNILALRGDPPREKEVWEAADGGFRYAKDLVKYIREKYGNHFCIGVGGYPEGADDNSDVDQLIDHLKEKVDAGSSFIVTQMFYDTDNFIKWVEKCRAKGINVPIIPGIMPIQTYAAFIRRANWTKTHIPPDWLEALEPVKNDDAAVKQVGKRLIADMCRRLIASGIKHLHFYTMNLAQSTQLVLEELELTPTAEAPIPRPLPWRPSLGLNRREEDVRPIFWRNRNSSYIARTAIWDEFPNGRWTDSRSPAFGELELYGVGLKGTNEQNIKLWGEPNSLRDLAEVFVRFLEGNLDRLPWSDSPITPETSAIKDALVELNRRGFFTINSQPAVNGVKSSHPVFGWGPKNGFVYQKAYLELLVPPYVIDELIARIEANEDLTYHAVTKKGELRTNTRDSPNALTWGIFAGREVVQPTIVETVSFLAWKDEAYQLGEDWAKCHEASSPTRKLLQGIMDSWYLVNIVNNDFHNTYDLFELFKDLNVKDLELEISGGITEDKAHHNGTANGATNGTTSNGTAAEQPVKN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (E5QCG9)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMSWTFKDENGHGQPLIVKVAETFGMEKRCILWLEMFMEQKRKTSTEIESETEAAYYFTLMNLYGRIHELNGVRGAYARLSRIQIDHVYGKISMREAFGDFNSAACFARMTGKGKPFNSTEAIQKLIDELNCLEYSQIERNEQEDYLNSLKTLSQWVNIDNDIGPSPHIFSRNIEYWATESTILKMIRNDERDEIVNNAIENAKSKVIERLSECAIGGSCSYEIATPFLVELQKLNEIVELKNVSNDELSAFNSDFWKNIQKRTDDSEQKISILEPILRVRRSMLDIRMQSMTGRDKENIRSRIVEVHLQSARIARLTGCFERAQLSLINAKKVLPFENKIVLEEAKLQLQTSDELNGMSLLDSIISKNFGDLHTIYTDTQQSVNLDVQKSAKLKIEHYQEETKNLFSSVQMLRISHMIKAGNTIGFDKVYHETTQLLQCFAHSGVMYEAAWLLDYLSNYKERSKHVLPLLKAYKEVAKYEKNQVLQARAVERMTSLWLSNTRKISTHISSVPKLPEGQISDLRQNIKSMNREIQTALEHIGWRAFYPAYAVLARHIDHQDEEVTRTIKQIMKQLILRMPHQCMWQSAYLLRQNIASVKEKYMEVLTEVKRKAPCYVTLIDQYDYASGVFNTVSGKVESDDCKLSEKVDGLKTMFRDKKYDPKELVMNRRVDCDCKILSGIMVPVRSVIDESVHDTEIRDDGFEESCHLPDRYLIHDFSDKVKVLHSNTKPVIIKLTTKTGRIVRLICKKDDDLSKDYHFTKMVEMCNDLLMKDEQTRIQKMTATTYSVIPLGKQGGIIEFMEGVTSFYETLDKLMGMTSGEWLEKLKFWNTHMKPMGKEERTKYFREVACKNTPVVMGKWFRIQYPEAGQWFASRKLFAKSTAVMSVIGYIFGLGDRHTKNLMVHTTGKCIHVDFDMIFNKGETLGTPELVPFRLTQNMINGMGEVALDGEFRTVCEQALRVFRENSYEIEKYIADLPNLVADFPSNKRAPKDFDMSEAKRLVSGRLRGQIMTAKLYRSNPISHPMQVSQLASSLIELATSEEKLSEMYLGWMATL
Protein: Alcohol dehydrogenase 8a (Q6P0S5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- S-formylglutathione hydrolase
- Aldehyde dehydrogenase 9 family, member A1a, tandem duplicate 2
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase 1 family, member A2
- Aldehyde dehydrogenase 1 family member A3
- Alcohol dehydrogenase iron-containing 1.
- Aldehyde dehydrogenase 2 family member, tandem duplicate 1
- Aldehyde dehydrogenase 2 family member, tandem duplicate 2
- 4-trimethylaminobutyraldehyde dehydrogenase A
Sequence:
MATAGKVIKCRAAVAWEPKAPLMMEEIEVAPPQEGEIRIKVIATGLCHTDLYHLVDGDKRGFPVVLGHESAGVVESVGPGVTDYKPGDKVIPLFLSQCGKCKFCKCPKTNLCESSWATKYHDIMAEPTSRFTCRGQTILQFMGTSTFSEYTVINQNAVAKIDENAPLDRVFLLGCGITTGYGAAVNTAGVTPGSVCAVFGLGAVGLAAVMGCKNAGASRIFAVDINEKKFEKAKVFGATDFLNPKAYNKPISEVLIEMTNGGGVDFSIECTGNTEVMRSALESCAKGWGVSVVVGWTNVQDFSAKPIQLIYGKTWKGSLFGGFKCKDSVPKLVRDYMSGKIMLDEFITHKMNLEQVNDAINLMKTGQGIRTIMTVSK
Protein: DNA gyrase subunit A (EC 5.6.2.2) (A0A0G2Q9F8)
Organism: Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Relaxes negatively supercoiled DNA in an ATP-independent manner. A linear reaction intermediate can be trapped in the presence of the antibiotic ciprofloxacin. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
Interaction partners:
Sequence:
MTDTTLPPDDSLDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEETLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSRGRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVIEIKRDAVAKVVINNLYKHTQLQTSFGANMLAIVDGVPRTLRLDQLIRYYVDHQLDVIVRRTTYRLRKANERAHILRGLVKALDALDEVIALIRASETVDIARAGLIELLDIDEIQAQAILDMQLRRLAALERQRIIDDLAKIEAEIADLEDILAKPERQRGIVRDELAEIVDRHGDDRRTRIIAADGDVSDEDLIAREDVVVTITETGYAKRTKTDLYRSQKRGGKGVQGAGLKQDDIVAHFFVCSTHDLILFFTTQGRVYRAKAYDLPEASRTARGQHVANLLAFQPEERIAQVIQIRGYTDAPYLVLATRNGLVKKSKLTDFDSNRSGGIVAVNLRDNDELVGAVLCSADDDLLLVSANGQSIRFSATDEALRPMGRATSGVQGMRFNIDDRLLSLNVVREGTYLLVATSGGYAKRTAIEEYPVQGRGGKGVLTVMYDRRRGRLVGALIVDDDSELYAVTSGGGVIRTAARQVRKAGRQTKGVRLMNLGEGDTLLAIARNAEESGDDNAVDANGADQTGN
Protein: Uncharacterized Na(+)/H(+) exchanger YjcE (P32703)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YehI
- 2,3-diketo-L-gulonate-binding periplasmic protein YiaO
Sequence:
MEIFFTILIMTLVVSLSGVVTRVMPFQIPLPLMQIAIGALLAWPTFGLHVEFDPELFLVLFIPPLLFADGWKTPTREFLEHGREIFGLALALVVVTVVGIGFLIYWVVPGIPLIPAFALAAVLSPTDAVALSGIVGEGRIPKKIMGILQGEALMNDASGLVSLKFAVAVAMGTMIFTVGGATVEFMKVAIGGILAGFVVSWLYGRSLRFLSRWGGDEPATQIVLLFLLPFASYLIAEHIGVSGILAAVAAGMTITRSGVMRRAPLAMRLRANSTWAMLEFVFNGMVFLLLGLQLPGILETSLMAAEIDPNVEIWMLFTNIILIYAALMLVRFGWLWTMKKFSNRFLKKKPMEFGSWTTREILIASFAGVRGAITLAGVLSIPLLLPDGNVFPARYELVFLAAGVILFSLFVGVVMLPILLQHIEVADHSQQLKEERIARAATAEVAIVAIQKMEERLAADTEENIDNQLLTEVSSRVIGNLRRRADGRNDVESSVQEENLERRFRLAALRSERAELYHLRATREISNETLQKLLHDLDLLEALLIEENQ
Protein: D-isomer specific 2-hydroxyacid dehydrogenase family protein (Putative glycerate dehydrogenase) (Q67Y01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- BAHD acyltransferase DCR
- Serine--glyoxylate aminotransferase
Sequence:
MQNRSISQVATMATSSSTEKLPRVLIVKRPDAMAVLGDGFVASTKFEILKAFESPLPLPEFLAYHSDSISAIIAPVAAPVTADLIRILPNLRLVVTTSAGVDHVDLVECRRRGISVANAGSSFSEDVADTAVGLLIDVFRRISAANRFVKQRFWPLKGDYPLGSKLGRKRIGIVGLGSIGSKVATRLDAFGCQISYSSRNRKPYDVPYHYYMDIEEMAANSDALIICCELNEKTLRLINKDVLSALGKRGVIVNVARGAIIDEEEMVRCLREGEIGGAGLDVFEDEPNVPKELFELDNVVFSPHSAFMTLEGLEELGKVVVGNIEAFFSNKPLLTPVL
Protein: Importin subunit alpha-6 (IMPa-6) (Q9FWY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation.
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
Interaction partners:
- Importin subunit beta-1
- Transcription factor VIP1
- Nuclear cap-binding protein subunit 1
- Exportin-2
- Transportin
- Protein TPX2
- Nuclear pore complex protein NUP50A
- F-box protein VBF
- Nucleoporin
- Nuclear cap-binding protein subunit 2
Sequence:
MSYKPSAKTEVRRNRYKVSVDADEGRRRREDNMVEIRKNKREENLQKKRREGFNPSMASQPGQDFSSSLPTETRLENIQQMIAGVMSEDRDLQLEATASFRRLLSIERNPPINEVVQSGVVPHIVQFLSRDDFTQLQFEAAWALTNIASGTSENTRVIIDSGAVPLFVKLLSSASEEVREQAVWALGNVAGDSPKCRDHVLSCEAMMSLLAQFHEHSKLSMLRNATWTLSNFCRGKPQPAFEQTKAALPALERLLHSTDEEVLTDASWALSYLSDGTNEKIQTVIDAGVIPRLVQLLAHPSPSVLIPALRTIGNIVTGDDIQTQAVISSQALPGLLNLLKNTYKKSIKKEACWTISNITAGNTSQIQEVFQAGIIRPLINLLEIGEFEIKKEAVWAISNATSGGNHDQIKFLVSQGCIRPLCDLLPCPDPRVVTVTLEGLENILKVGEAEKNLGNTGNDNLYAQMIEDADGLDKIENLQSHDNNEIYEKAVKILESYWAADDEEEDIGGVDAPENVQSSGFQFGNQSGNAPTGGFNFG
Protein: Alpha-1,2-mannosyltransferase MNN2 (EC 2.4.1.-) (Calcium resistance and vanadate sensitivity protein 4) (Mannan synthesis protein MNN2) (P38069)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alpha-1,2-mannosyltransferase, responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:18410729, ECO:0000269|PubMed:20236934, ECO:0000269|PubMed:2082155, ECO:0000269|PubMed:9756928}; Single-pass type II membrane protein {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:18410729, ECO:0000269|PubMed:20236934, ECO:0000269|PubMed:2082155, ECO:0000269|PubMed:9756928}. Note=Golgi localization depends on SVP26.
Interaction partners:
- Mannan polymerase complexes subunit MNN9
- Putative glycosyltransferase HOC1
- Probable alpha-1,6-mannosyltransferase MNN10
- Probable alpha-1,6-mannosyltransferase MNN11
- Mannan polymerase II complex ANP1 subunit
- Alpha-1,3-mannosyltransferase MNN1
- Alpha-1,2-mannosyltransferase MNN5
- Glutamyl-tRNA
- Mannosyltransferase regulator 4
- Mannosyltransferase KTR6
Sequence:
MLLTKRFSKLFKLTFIVLILCGLFVITNKYMDENTSVKEYKEYLDRYVQSYSNKYSSSSDAASADDSTPLRDNDEAGNEKLKSFYNNVFNFLMVDSPKGSTAKQYNEACLLKGDIGDRPDHYKDLYKLSAKELSKCLELSPDEVASLTKSHKDYVEHIATLVSPKGTYKGSGIATVGGGKFSLMAFLIIKTLRNMGTTLPVEVLIPPGDEGETEFCNKILPKYNSKCIYVSDILPRETIEKFVFKGYQFKSLALIASSFENLLLLDADNFPIKPLDNIFNEEPYVSTGLVMWPDFWRRTTHPLYYDIAGIAVDKKKRVRNSRDDITPPAVYTKDLKDLSDVPLSDLDGTIPDVSTESGQLMINKTKHLATALLSLFYNVNGPTWYYPIFSQKAAGEGDKETFIAAANFYGLSFYQVRTRTGVEGYHDEDGFHGVAMLQHDFVQDYGRYLNAMESIGNKYGGTKSADAIKFDKNYSLEKYTEEFFDNEDLNAKNHVDVMFIHSNFPKFDPYDLSKSNFLTTNGKPARSYTALKKVKNYDIELENFKVLNEYVCVNKNPFKYLDDLLGQDKTEWKRVCGYITDRLAFLESTHDKAIAGK
Protein: Phytol kinase (EC 2.7.1.182) (P74653)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Catalyzes the CTP-dependent phosphorylation of phytol to phytylmonophosphate (PMP). Can also use UTP as an alternative phosphate donor, but not ATP or GTP. Is involved in tocopherol biosynthesis, via the utilization of phytol generated by chlorophyll degradation. Also plays a significant but not critical role in the recycling of phytol for the biosynthesis of new chlorophyll molecules.
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein slr0090
- Slr1648 protein
- Nucleoside triphosphate pyrophosphatase
- Prephenate dehydrogenase
- N-acyl-L-amino acid amidohydrolase
Sequence:
MGIEQNNPMALPLWIAVGLAATYLGAVVLTAELLNRLSLSPAEVTRKIVHIGAGQVVLIAWWLSIPGWVGAIAGVFAAGIAVLSYRLPILPSLESVGRHSYGTLFYALSIGLLVGGFFSLGLPIFAAIGILVMAWGDGLAALVGQRWGRHRYQVFGFRKSWEGTLTMVLASFLVTVVFLSYTFGFTVIVLVVAGTVAIASAGLESFSRWGIDNLTVPLGSALIAWAGSYLWLG
Protein: Metallothionein-1A (MT-1A) (Metallothionein-IA) (MT-IA) (P04731)
Organism: Homo sapiens (Human)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Interaction partners:
Sequence:
MDPNCSCATGGSCTCTGSCKCKECKCTSCKKSCCSCCPMSCAKCAQGCICKGASEKCSCCA
Protein: Cytotoxic T-lymphocyte protein 4 (Cytotoxic T-lymphocyte-associated antigen 4) (CTLA-4) (CD antigen CD152) (P09793)
Organism: Mus musculus (Mouse)
Function: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16410}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16410}. Note=Exists primarily an intracellular antigen whose surface expression is tightly regulated by restricted trafficking to the cell surface and rapid internalization. {ECO:0000250|UniProtKB:P16410}.
Interaction partners:
- T-lymphocyte activation antigen CD80
- Programmed cell death 1 ligand 1
- T-lymphocyte activation antigen CD86
- ICOS ligand
- Programmed cell death 1 ligand 2
- Tyrosine-protein phosphatase non-receptor type 11
- Programmed cell death protein 1
- Galectin-9
- Inducible T-cell costimulator
- Lymphocyte activation gene 3 protein
Sequence:
MACLGLRRYKAQLQLPSRTWPFVALLTLLFIPVFSEAIQVTQPSVVLASSHGVASFPCEYSPSHNTDEVRVTVLRQTNDQMTEVCATTFTEKNTVGFLDYPFCSGTFNESRVNLTIQGLRAVDTGLYLCKVELMYPPPYFVGMGNGTQIYVIDPEPCPDSDFLLWILVAVSLGLFFYSFLVSAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN
Protein: Dynein, axonemal, heavy chain 9 (B7FAT5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
NVSAAVMVLMAPGGKVPKDRSWKAAKITMAKVDSFLDSLIHFDKENIHENCLKAIRPYLQDPAFNPEFVATKSYAAAGLCSWVINIVRFYEVFCDVEPKRQALNKATSDLTTAQEKLAAIKAKITHLNENLAKLTTKFEKATAEKLKCQQEAELTAGTISLANRLVPIPTTPTLDPLRMLTDDAEVAAWQNEGLPADRMSMENATILINCERWPLMVDPQLQGIKWIKNKYGEELRVTQIGQKGCLQTIERALEAGDVVLIENLEESIDPVLGPLLGRE
Protein: Phosphoglycerate kinase 3, cytosolic (EC 2.7.2.3) (Q9SAJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00560}.
Interaction partners:
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP1, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1
- Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2
- Glyceraldehyde-3-phosphate dehydrogenase GAPB, chloroplastic
Sequence:
MATKRSVGTLKEADLKGKSVFVRVDLNVPLDDNSNITDDTRIRAAVPTIKYLMGNGSRVVLCSHLGRPKGVTPKYSLKPLVPRLSELLGVEVVMANDSIGEEVQKLVAGLPEGGVLLLENVRFYAEEEKNDPEFAKKLAALADVYVNDAFGTAHRAHASTEGVAKFLKPSVAGFLMQKELDYLVGAVANPKKPFAAIVGGSKVSTKIGVIESLLNTVDILLLGGGMIFTFYKAQGLSVGSSLVEEDKLDLAKSLMEKAKAKGVSLLLPTDVVIADKFAPDANSKIVPATAIPDGWMGLDIGPDSIKTFSEALDTTKTIIWNGPMGVFEFDKFAAGTEAVAKQLAELSGKGVTTIIGGGDSVAAVEKVGLADKMSHISTGGGASLELLEGKPLPGVLALDEA
Protein: PE-PGRS family protein PE_PGRS56 (Q6MWW7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
PQGADGNAGNGGDGGVGGNGGNGADNTTTAAAGTTGGAGGAGGAGGTGGTGGAAGTGTGGQQGNGGNGGNGGTGGKGGTGGDGALAGSSGGAGGKGGNGGDAGKAGTGSAPGTAGTGGDGGKGGNGGIGAAGTTGPVGTGASGGTGGSGGAGGTGGDGGAANGGTAGAGGAGGNGGKGGDGGAGVTSSTAGNSGGAGGSGGKGGDAGAGGAGATPGANGIAGNGGDGGDGAAGAVGISGATGAGDGGHGGTGAAGGNGGTGGAGGSGIDGVGGGTGGTGGNGGNGAIGGAGGDAGGSGNSGGNGGIGGKGGNAGAGGAAGSNGGTVGANGTGGDGGNGGAAGAATAGSNGGAGTGSAGGNGGTGGRGGSGGAGGDGIGGVGGGKGGNGADGEVGGAGGAGGSGPNTSPGGNGGQGGQGGSGGAGGAAGAGGAGGGANGTAGNGGQGGAGGTGGAGAASSATNGGSGGAGGTGGDGGSGGAGGTGGAGGTGGAAGDGGQGGQGGAGGGAGGQGGAGGAGGTGGNGGNITGGTAGTAGAAGNGGAAGKGGAGGQGGTGGGTGGQGGAGGDGGAGGTGGDRTVGGGTVPAGSGGQGGNAGGGGAGGQGGADGGSGGDGGDAGTGGNGGNGGNRNSGNGTGGAGGNGGGGANGGAGGAGGSGGGTGGNGGAGGDAGDAGNGGNGNGTGNGGNGGNGGIAGMGGNGGAGTGSGNGGNGGSGGNGGNAGMGGNSGTGSGDGGAGGNGGAAGTGGTGGDGGLTGTGGTGGSGGTGGDGGNGGNGADNTANMTAQAGGDGGNGGDGGFGGGAGAGGGGLTAGANGTGGQGGAGGDGGNGAIGGHGPLTDDPGGNGGTGGNGGTGGTGGAGIGSLGGGTGGDGGNGGNGGTGGEGGEVGGAGGTGGAAGNGGDGGTGGTGGGDGGAGGTGGTGGTGGLGDPRVGGSGGDGGTGGSGGAAGNGGNGGNAGAGGNGNGGTGGAGGIGGTGGNGGDAEPGVPPGAGGAGGAGTTGGKGGTGGNGSGTGSGGTGGDGGTGGGGGNGGTGWNGGKGDTGSGGGAGDGGKAPAGGTGGAGGDGGAGGKGGSGGV
Protein: PR domain zinc finger protein 15 (EC 2.1.1.-) (PR domain-containing protein 15) (Zinc finger protein 298) (P57071)
Organism: Homo sapiens (Human)
Function: Sequence-specific DNA-binding transcriptional regulator. Plays a role as a molecular node in a transcriptional network regulating embryonic development and cell fate decision. Stimulates the expression of upstream key transcriptional activators and repressors of the Wnt/beta-catenin and MAPK/ERK pathways, respectively, that are essential for naive pluripotency and self-renewal maintenance of embryonic stem cells (ESCs). Specifically promotes SPRY1 and RSPO1 transcription activation through recognition and direct binding of a specific DNA sequence in their promoter regions. Involved in early embryo development (By similarity). Also plays a role in induced pluripotent stem cells (iPSCs) reprogramming.
Subcellular location: Nucleus {ECO:0000269|PubMed:15904895}.
Interaction partners:
- Codanin-1
Sequence:
MAEDGSEEIMFIWCEDCSQYHDSECPELGPVVMVKDSFVLSRARSSLPPNLEIRRLEDGAEGVFAITQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKMDKPMLKQAGSGVHAAGTPENSAPVESEPSQWACKVCSATFLELQLLNEHLLGHLEQAKSLPPGSQSEAAAPEKEQDTPRGEPPAVPESENVATKEQKKKPRRGRKPKVSKAEQPLVIVEDKEPTEQVAEIITEVPPDEPVSATPDERIMELVLGKLATTTTDTSSVPKFTHHQNNTITLKRSLILSSRHGIRRKLIKQLGEHKRVYQCNICSKIFQNSSNLSRHVRSHGDKLFKCEECAKLFSRKESLKQHVSYKHSRNEVDGEYRYRCGTCEKTFRIESALEFHNCRTDDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMFYRKDVMLDHQRRHLEGVRRVKREDLEAGGENLVRYKKEPSGCPVCGKVFSCRSNMNKHLLTHGDKKYTCEICGRKFFRVDVLRDHIHVHFKDIALMDDHQREEFIGKIGISSEENDDNSDESADSEPHKYSCKRCQLTFGRGKEYLKHIMEVHKEKGYGCSICNRRFALKATYHAHMVIHRENLPDPNVQKYIHPCEICGRIFNSIGNLERHKLIHTGVKSHACEQCGKSFARKDMLKEHMRVHDNVREYLCAECGKGMKTKHALRHHMKLHKGIKEYECKECHRRFAQKVNMLKHCKRHTGIKDFMCELCGKTFSERNTMETHKLIHTVGKQWTCSVCDKKYVTEYMLQKHVQLTHDKVEAQSCQLCGTKVSTRASMSRHMRRKHPEVLAVRIDDLDHLPETTTIDASSIGIVQPELTLEQEDLAEGKHGKAAKRSHKRKQKPEEEAGAPVPEDATFSEYSEKETEFTGSVGDETNSAVQSIQQVVVTLGDPNVTTPSSSVGLTNITVTPITTAAATQFTNLQPVAVGHLTTPERQLQLDNSILTVTFDTVSGSAMLHNRQNDVQIHPQPEASNPQSVAHFINLTTLVNSITPLGSQLSDQHPLTWRAVPQTDVLPPSQPQAPPQQAAQPQVQAEQQQQQMYSY
Protein: biotin carboxylase (EC 6.3.4.14) (Q7KQ29)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVVNGQKPDIRTIVVSGNSLTNDAADQYESMEQFIHSHVADIEKRRPIKRLLVATNGIAAMRCLMTAKKFLHHTFRNDNLIHFVCMTTEDEIQSMSESLRMPNITLAESPSGTNKNNFANVDEILKHAIKYEVDAVWAGWGHASENPDLPRRLNDHNIAFIGPPASAMFSLGDKIASTIIAQTVGVPTVAWSGSGITMESIERSRGDFVVVPEDLLEQACVANYKEGLEALKTHNIGFPLMIKASEGGGGKGIRKCTKVEDFKSMFEEVAQEVQGSPIFLMKCVDGARHIEVQLLADRYENVISVYTRDCSIQRRCQKIIEEAPAIIASSHIRKSMQEDAVRLAKYVGYESAGTVEYLYLPASEGQEEHYYFLELNPRLQVEHPTTEMVSNISIPAIQLQIAMGLPLHKIKDIRKLYDLPIDGDSELPDEVLVDTKLHAIAARITCENPDDSFRPSTGKVYEINFPSSQDAWAYFSVGRGSSVHQFADSQFGHIFTRGTSRTEAMNTMCSTLKHMTIRSSFPTQVNYLVDLMHDADFINNAFNTQWLDKRIAMKIKQKCSLSMSVIIAVSAAVIGSSRVTGVFESFEESIDRGQVRPPNDLTETFIFDLVKDLNIYSLKVVRSAENTFVIILNGSKVTVGVKELQNGEFMVTHCEIVYRCAFEETKEAYKVTVNNEIITFEKDNDVSVLKSPYTGKLLQWKKEDGDWLNVGDVYATAESMKMVFQVEVAKAPGSYSSAPHTVKPCLATAMTWVETNLRSYVQPNSSMDEQYTQIEQYYETQFVDDLVIAINEDRKRYEQQLNTFMNKISSKRR