wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase 1 regulatory subunit 14C (Kinase-enhanced PP1 inhibitor) (PKC-potentiated PP1 inhibitory protein) (Q8R4S0)
Organism: Mus musculus (Mouse)
Function: Inhibitor of the PP1 regulatory subunit PPP1CA.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:11812771}; Peripheral membrane protein {ECO:0000269|PubMed:11812771}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 14D
Sequence:
MSVVTGGGEAAGGGGGGGARVFFQSPRGGTGGSPGSSSSSGSSREDSAPVTTVAAAGQVQQQQRRHQQGKVTVKYDRKELRKRLVLEEWIVEQLGQLYGCEEEEMPDVEIDIDDLLDANSEEERASKLQEALVDCYKPTEEFIRELLSRIRGMRKLSPPQKKSV
Protein: C2H2-like zinc finger protein (Zinc finger-like protein) (Q8VZP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGRLWESLPVILLLLVLLLHQSVSQGFEESESTRLVNEEVEVSNAPEIHCSRERSRAAWQIIQDYLTPFVERERYEIPKNCRLHPDNDLYRDQEHHKVHVDVFEWKCGYCKKSFNDEKFLDKHFSTRHYNLLNTTDTKCLADLCGALHCDFVLSSKKPKSKCNPPAVAKNRHLCESVANSCFPVSQGPSASRLHEHFLRQFCDAHTCTGNDKPFPRGGKKKSGVFYLAISILTLMLLPLFYLLVFLHQREKRSGTQDLRRIIKSGKKTKPS
Protein: Autophagy-related protein 8A (Autophagy-related ubiquitin-like modifier ATG8A) (Protein autophagy 8) (OsAtg8) (Q2XPP5)
Organism: Oryza sativa subsp. indica (Rice)
Function: Ubiquitin-like modifier involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. May mediate the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton (By similarity).
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8LEM4}.
Interaction partners:
- Protein NBR1 homolog
- Uncharacterized protein
- Cysteine protease ATG4B
- Cysteine protease
- Ubiquitin-like modifier-activating enzyme ATG7
- Uncharacterized protein
- Uncharacterized protein
- Autophagy-related protein 3
- Cysteine protease ATG4A
- Uncharacterized protein
Sequence:
MARTSFKLEHPLERRQAESARIREKYSDRIPVIVEKADKTDVPEIDKKKYLVPADLTVGQFVYVVRKRIKLSPEKAIFVFVKNTLPPTASLMSAIYEENKDEDGFLYMTYSGENTFGSA
Protein: AP-1 complex subunit gamma-1 (Clathrin assembly protein complex 1 gamma-1 large chain) (Clathrin assembly protein large gamma-1 chain) (Gamma-adaptin) (Q9UU81)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-1 complex subunit sigma-1
- AP-1 complex subunit mu-1
- AP-1 complex subunit beta-1
- AP-3 complex subunit sigma
- Probable clathrin heavy chain
- AP-3 complex subunit beta
- AP-2 complex subunit beta
- AP-3 complex subunit mu
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
Sequence:
MQTTHPKNLHLTCSGVERGFTNSPKTHPKMSSLKSFIKAVRASKTTAEEHTTILKESAQIRKNIRQGSNDMRMRRKNVAKLLYLFLLGEPTHFGQIECLKLLSSSRFMDKRLGYLAAMLLLDENQEVLTLLTNSLQNDLKSRDKFIVGLALSAFGNVAGPELARDLSNDIAELCSNHHNYISKKAVLCALRVIQKEPDLESLYIEKTDELLHSKSHGVLMAALAFAISACKINPSLISRFESQADDLIYRIRQLSTSTYSSEHNIGNISDPFLQVKILQFLSILGQNNPKIYDKMSDLLAQVCTNTDSSRNAGNAILYQAVRTILDLNSDSSLRVLGVNILAKFLGNRDNNTRYVALNMLKLVVNSEENAVQRHRSTILACLNDVDSSIQSRALELSTFLVNEANVRFMVRELLSFLDNVSDELRGSTAQYITEVTNAFAPNKRWHFDTLLRVFKSAGNFVSESTLSTFLRLIASAPELHEYAVVKLYAALKEDVSQEALTLSAFWVIGEYGQMLLSPTMNFDDDQTLPHSVSESDIVDIIEEVFNSVEASRYIIVQYGLFALTKLSARLGSSSTASRIDKIIYSYKRNKNTEVQQRSVEFHLILNDSKLSKTILEPTPAPLPPPRTTPYQNAEQKLKANKHVEKRVQESNELLDLIGLTTPSVAEPLETPVDEMTQSPQSSLSRAPSTSKKSHFEDILGLFASPAPSAQPVDSLASSFASLDFNASASQPSNNLSLLSSIPSTSKSYPPIVVFDKHDVTLTLVPSKEESTKTAVIEAKFKNKNPMTRVEKIHLEVAVPKSQKLKIQPLRTTSMEPGGETSQTLRVHGPSGSQVKLRLRISVVRQGGSNTLDQVDFGKLPSDLLQ
Protein: B3 domain-containing transcription factor NGA1 (Protein NGATHA 1) (O82799)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates lateral organ growth. Functionally redundant with NGA2, NGA3 and NGA4.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- F23A5.30 protein
- B3 domain-containing protein At3g17010
Sequence:
MMTDLSLTRDEDEEEAKPLAEEEGAREVADREHMFDKVVTPSDVGKLNRLVIPKQHAERFFPLDSSSNEKGLLLNFEDLTGKSWRFRYSYWNSSQSYVMTKGWSRFVKDKKLDAGDIVSFQRCVGDSGRDSRLFIDWRRRPKVPDHPHFAAGAMFPRFYSFPSTNYSLYNHQQQRHHHSGGGYNYHQIPREFGYGYFVRSVDQRNNPAAAVADPLVIESVPVMMHGRANQELVGTAGKRLRLFGVDMECGESGMTNSTEEESSSSGGSLPRGGGGGASSSSFFQLRLGSSSEDDHFTKKGKSSLSFDLDQ
Protein: Dynein axonemal assembly factor 4 (Q381I1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}. Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- Telomerase-associated protein, putative
- FG-GAP repeat protein, putative
- FG-GAP repeat protein, putative
Sequence:
MLLFFFLPNSPPLLCGGLYKVMPVKPVYEWEQTNTEVLLRITIKGFKKEAIDIFVSDLLVKVNASPTYLLVLDLLHPIDEAKSTHFMDPEDRTCLRVRLRKRVPELWESLCINEGEIGAEAIRERRAGAIQRAEESYNRRLKERVGKREEEKRRMTEEQWEVDRAQRRLIEGRMKEEKDSAEAELYSWEEQQRAEQQAHEEKKRAPQCPGDIGAMQGSMEERKEEEMTPCVRHTETVVVPVQFTSKMAAIPTRSRGEDEYYRRSRYKPTRVEDSPMFWKERADKHYQRREWKAAADAYTESIKRDGAFLICVSNRAACFIQLFEYKRAIEDCTLALTMLSNTPASDLTQERYRYLMMKLHSRRGAAYCWGKCFERGIEDLRMAAAYCDAEEDADVIADYKLVESYMKKRGMLETRDPLAAKLHEASSMYYQGDYAAAADVYRQVLEEDPYEVRARNNLSAALLHQGCFKEALMESSHVLEFCREVAEALSCPGALSTNLVDSDDEDGGEDGVGGDGGGCGEDEVMRKRNAAARKVGEKSGHVYAILKACVRGAAAHCGLKDYRKALELLEQAMRITPYDNDLHDDYNRVVEKMRMETLLAASSGKLEKAPSKTAEAPPPAIAT
Protein: Non-classical export protein 2 homolog (O74333)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in membrane organization and might act as a sensor of sphingolipids that regulates plasma membrane function. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable sphingolipid long chain base-responsive protein pil1
- Eisosome protein sle1
- Meiotically up-regulated gene 33 protein
- Putative uncharacterized oxidoreductase C513.07
- SUR7 family protein pun1
- Probable sphingolipid long chain base-responsive protein pil2
Sequence:
MVGIRQYGVFTWVFRTFQLAIDTIVLALASALVNQQTSGGSPGKINFSVAVGSFAILTFFLTAVGRFLPTILGNPWLIAFYDFVNWVFALTGGCCIAVAIRVHACDNQKYLDRNHYTQGSMRRCQELKALCFFLWFMFGLYVASFIVQIFIAKNDTPNYTFRGRGRGKGSGPAVAPRPVMSAV
Protein: Target of EGR1 protein 1 (Target of EGR1, exonuclease) (B8A5U4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSSSMIIPVIDVQGNNFKELWAAMVIAIKTSSFIAIDTELSGLGSRKALLAESIEDRYNAICHAARTRSVLSLGFACYKELENKAETTYLVQVYNLTLLCSEEYIIEPQSVQFLVQHGFDFNKQYAEGIPYYKGNDKGGDAHGVNIRSLFVELLRANKPLVLHNGLIDLVFLYQCFYAHLPDRLGTFTADLSQMFPSGIYDTKYATEYELRFTASYLEYAYKKCKLENSKAIEAEGSGSNLFVEFCKYTGNMETYIDYRPCLDSQSQDDGALNICVQFSAYGWCPNGSQCPMSHNTDLIIQQDEKTREDKRKKRKRKNKKKGSQGPPETCSSPQGKRTHFEEAELDQAVPTSEHQEKTLNAEPTDEPGKTASNNGDEQSQPEASTEAQEKPKGKKVEGGTHRAGFDAFMTGYIFAYARNLMKNKEESSSTPVISTCLNKLFLSGKSVPLHVAKSTFSKSSKAHVQKMAYVWGKSIDVNMEKSA
Protein: RE10036p (Rad, Gem/Kir family member 2, isoform A) (Q6NN22)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQQQRSWDEGAVGGGSYGHPHSSHHKVPARAASNPLPCKGATPKLPRQYHGGPTSSYNYGGYDTPRSPKITTTFAQDSCDDVSSSTPSSYYQTPPSGSIDDSASLLSGRTTARSPKSQCQFVFDAVSPSHGRKFEYYEPISPDDGALYYDPPSSPRRQGSKKLMRTKTPLDPVPQLTTTGVDESMAVAMAMGGAGGGGYAQGGPNKRQRDEWELPVISKIEARNLSAAAGSSSAGGSYYGLKRDSCVTDCTQLSMESGETGTQHTNSTMVTHTTTSFSFTEPEMEQEAGQPQLRRQRRHAINITSNPGYQVLHSSHSTLDRTCSDSVVSLRYRKSTSDLTQDAEHELSGCKPNKPKAHVEHKPRRRGSSKGGLAYLASRRSSRESMKSACSNASIVSNDDVGPLAFQSSNRGRQRRTSNFLELPVPDHVRPRVCSLPERPYNPRASDDLYRLRHFSISKGNVVNCGDSIISRRSRSNTSVNSTNSRASERSPFEGSCCGAGYANVDSLPATPDDSENLDPPPPARYRVVMLGDAGVGKTALVNQFMTSEYMHTYDASLDDEFGEKTVSVLLDDEESDMVFIDHPSVEMSVENSLSTYEPHGCVVVFSVVDRSSFRVAEEIINYLWQENYTKDKAVILVGNKADLARARLITSQEGKALAASRDAKFIETSSGIQHNVDELLVGILKQMRLKEKREKKATASKMKTSRTHISLHLAKELLQKICLSDISKSKSCENLHVL
Protein: Hyaluronan synthase 2 (EC 2.4.1.212) (Hyaluronate synthase 2) (Hyaluronic acid synthase 2) (HA synthase 2) (P70312)
Organism: Mus musculus (Mouse)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction and it is particularly responsible for the synthesis of high molecular mass hyaluronan. Required for the transition of endocardial cushion cells into mesenchymal cells, a process crucial for heart development. May also play a role in vasculogenesis. High molecular mass hyaluronan also play a role in early contact inhibition a process which stops cell growth when cells come into contact with each other or the extracellular matrix.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Lysosome {ECO:0000250|UniProtKB:Q92819}. Note=Travels from endoplasmic reticulum (ER), Golgi to plasma membrane and either back to endosomes and lysosomes, or out into extracellular vesicles. Post-translational modifications control HAS2 trafficking. {ECO:0000250|UniProtKB:Q92819}.
Interaction partners:
- CD44 antigen
- Hyaluronidase-1
- Hyaluronidase-2
- Tumor necrosis factor-inducible gene 6 protein
- UDP-glucose 6-dehydrogenase
- Hyaluronan mediated motility receptor
- Pentraxin-related protein PTX3
- Hyaluronidase
- Aggrecan core protein
- Hyaluronan and proteoglycan link protein 1
Sequence:
MHCERFLCVLRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSDDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETEESHKESSQHVTQLVLSNKSICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNAMWFHKHHLWMTYEAVITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIKSSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIPVSVWFTILLGGVIFTIYKESKKPFSESKQTVLIVGTLIYACYWVMLLTLYVVLINKCGRRKKGQQYDMVLDV
Protein: Cyclin-dependent kinase D-1 (CDKD;1) (EC 2.7.11.22) (EC 2.7.11.23) (CDK-activating kinase 3-At) (CAK3-At) (Q9C9U2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000269|PubMed:15486101}.
Interaction partners:
- Cyclin-H1-1
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH subunit TFB4
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH subunit TFB2
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription and DNA repair factor IIH subunit TFB1-3
- General transcription and DNA repair factor IIH subunit TFB1-1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB2
Sequence:
MEQPKKVADRYLKREVLGQGTYGVVFKATDTKNGETVAIKKIRLGKEKEGVNVTALREIKLLKELKHPHIIELIDAFPHKENLHIVFEFMETDLEAVIRDRNLYLSPGDVKSYLQMILKGLEYCHGKWVLHRDMKPNNLLIGPNGQLKLADFGLARIFGSPGRKFTHQVFARWYRAPELLFGAKQYDGAVDVWAAGCIFAELLLRRPFLQGNSDIDQLSKIFAAFGTPKADQWPDMICLPDYVEYQFVPAPSLRSLLPTVSEDALDLLSKMFTYDPKSRISIQQALKHRYFTSAPSPTDPLKLPRPVSKQDAKSSDSKLEAIKVLSPAHKFRRVMPDRGKSGNGFKDQSVDVMRQASHDGQAPMSLDFTILAERPPNRPTITSADRSHLKRKLDLEFL
Protein: Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (TRAP/Mediator complex component TRAP25) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25) (Q96HR3)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 26
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 11
Sequence:
MSTPPLAASGMAPGPFAGPQAQQAAREVNTASLCRIGQETVQDIVYRTMEIFQLLRNMQLPNGVTYHTGTYQDRLTKLQDNLRQLSVLFRKLRLVYDKCNENCGGMDPIPVEQLIPYVEEDGSKNDDRAGPPRFASEERREIAEVNKKLKQKNQQLKQIMDQLRNLIWDINAMLAMRN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B9DFC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYKVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQNDGTVTYYLILDNRFRASSGYLGAEFQETMEGTPRMHPAESVASPVSHRLPGLMEYQGVGLRSQYPVERKWALGLQSRAHPREIMTEVLKALQDLNVCWKKIGHYNMKCRWVPNSSADGMLSNSMHDNNYFGDESSIIENEAAVKSPNVVKFEIQLYKTRDDKYLLDLQRVQGPQFLFLDLCAAFLAQLRVL
Protein: Arginine kinase (Q1DA50)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- TldD protein
- Peptidase, M12A
Sequence:
MLLHKHLTPELKSRLERLTTRNGWTLRKTIQSGLDHGDSQMGVYAGDSESYALFSPLLHPIIRDHSGHDLSGHTSDFSLDGLPQGDLDPTGEFILSTRVRVGRNLARYAFPPAIGARDRAALEAEVVQVLSGLRGHLAGKYHPLASLSEAERLELVHHHVLFQQSDRFLDSAGVNRDWPRNRGIFHSADMRFIVWVGEEDALRIISMQPGSGLAQTYLRLQTALEQFDGQLDFAQDSRLGFLTACPTNLGTAMRASVLIRLPHLSRRPDFRARCARLGLAVRGLHGEHSEARDGIHDVSNATRLGVTERDIYEQLRTGIHALMEMESAARKRGHPKVAPGN
Protein: Pumilio homology domain family member 6 (Q04373)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus.
Subcellular location: Bud tip. Nucleus, nucleolus.
Interaction partners:
- Nucleolar GTP-binding protein 1
- ATP-dependent RNA helicase HAS1
- 25S rRNA
- rRNA-processing protein EBP2
- Ribosome biogenesis protein BRX1
- Ribosome biogenesis protein SSF1
- Ribosome biogenesis protein RPF2
- Ribosome biogenesis protein 15
- Nucleolar complex protein 2
- Ribosome biogenesis protein MAK21
Sequence:
MAPLTKKTNGKRSAKEVSHSEKKLAKKPRISIDSSDEESELSKKEDAVSSSSDDDDLDDLSTSDSEAEEEADELDISDDSEEHENENEEKEGKDKSEGGENGNHTEQRKLLKERKMQRKSGTQVQQIKSVWERLRVKTPPLPKQIREKLSNEIWELSKDCISDLVLKHDASRIVQTLVKYSSKDRREQIVDALKGKFYVLATSAYGKYLLVKLLHYGSRSSRQTIINELHGSLRKLMRHREGAYVVEDLFVLYATHEQRQQMIKEFWGSEYAVFRETHKDLTIEKVCESSIEKRNIIARNLIGTITASVEKGSTGFQILHAAMREYVKIANEKEISEMIELLHEQFAELVHTPEGSDVACTLVARANAKERKLILKALKNHAEKLIKNEYGNIVFITILNCVDDTVLVFKTFSPTVKEHLQEFIIDKFGRRPWLYILLGLDGKYFSPIVKNELLRYIELSKATSKKDPLQRRHELLSKFAPMFLSTISKDYSSILTENLGCQFIAEVLINDELYAQLNEKDQEKYQQVLNNILTTFKGDITEEEHPIHRAFSTRLLKALIQGGKWNNKEKKVIPLKNVQGLGVPFAEKLYDEIIDSSNLLEWINNADSSFTIVALYETLKDQKEGKPFLKDLRGVQSKITTDESNKGSQLLAKLLK
Protein: L-xylulose reductase (XR) (EC 1.1.1.10) (Dicarbonyl/L-xylulose reductase) (Q91X52)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000269|PubMed:11882650}; Peripheral membrane protein {ECO:0000269|PubMed:11882650}. Note=Probably recruited to membranes via an interaction with phosphatidylinositol (By similarity). In kidney, it is localized in the brush border membranes of proximal tubular cells. {ECO:0000250}.
Interaction partners:
- Aldose reductase-related protein 2
- Aldo-keto reductase family 1 member B7
- aldose reductase
- Sorbitol dehydrogenase
- Aldo-keto reductase family 1 member B1
Sequence:
MDLGLAGRRALVTGAGKGIGRSTVLALKAAGAQVVAVSRTREDLDDLVRECPGVEPVCVDLADWEATEQALSNVGPVDLLVNNAAVALLQPFLEVTKEACDTSFNVNLRAVIQVSQIVAKGMIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKMMALELGPHKIRVNAVNPTVVMTPMGRTNWSDPHKAKAMLDRIPLGKFAEVENVVDTILFLLSNRSGMTTGSTLPVDGGFLAT
Protein: DNA topoisomerase 2-beta (EC 5.6.2.2) (DNA topoisomerase II, beta isozyme) (Q02880)
Organism: Homo sapiens (Human)
Function: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:8299728, ECO:0000269|PubMed:9155056}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9155056}. Nucleus {ECO:0000269|PubMed:19690332}.
Interaction partners:
- DNA topoisomerase 1
- DNA topoisomerase 2-alpha
- DNA topoisomerase I, mitochondrial
- DNA topoisomerase 2-binding protein 1
- Tyrosyl-DNA phosphodiesterase 2
- Structural maintenance of chromosomes protein 2
- Transcriptional repressor CTCF
- Androgen receptor
- SUMO-conjugating enzyme UBC9
- BTB/POZ domain-containing protein KCTD9
Sequence:
MAKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLAAFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKKKKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYFAESDEEEDDVDFAMFN
Protein: Nicotinamidase (EC 3.5.1.19) (Nicotinamide deamidase) (NAMase) (Pyrazinamidase) (PZAase) (EC 3.5.1.-) (P21369)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide.
Interaction partners:
- Nicotinate phosphoribosyltransferase
- NAD-dependent protein deacylase
- L-asparaginase 1
- Catalase-peroxidase
- NH
- Nicotinate-nucleotide adenylyltransferase
- Purine nucleoside phosphorylase DeoD-type
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Probable hydrolase YcaC
- DNA-directed RNA polymerase subunit beta
Sequence:
MPPRALLLVDLQNDFCAGGALAVPEGDSTVDVANRLIDWCQSRGEAVIASQDWHPANHGSFASQHGVEPYTPGQLDGLPQTFWPDHCVQNSEGAQLHPLLHQKAIAAVFHKGENPLVDSYSAFFDNGRRQKTSLDDWLRDHEIDELIVMGLATDYCVKFTVLDALQLGYKVNVITDGCRGVNIQPQDSAHAFMEMSAAGATLYTLADWEETQG
Protein: Ethylene-responsive transcription factor CRF4 (Protein CYTOKININ RESPONSE FACTOR 4) (Q9SUE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cytokinin signaling pathway involved in cotyledons, leaves, and embryos development. Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16832061}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:16832061}. Note=Relocalization from the cytoplasm into the nucleus is induced by cytokinins.
Interaction partners:
- Membrane magnesium transporter
- Defensin-like protein 95
Sequence:
MMMDEFMDLRPVKYTEHKTVIRKYTKKSSMERKTSVRDSARLVRVSMTDRDATDSSSDEEEFLFPRRRVKRLINEIRVEPSSSSTGDVSASPTKDRKRINVDSTVQKPSVSGQNQKKYRGVRQRPWGKWAAEIRDPEQRRRIWLGTFATAEEAAIVYDNAAIKLRGPDALTNFTVQPEPEPVQEQEQEPESNMSVSISESMDDSQHLSSPTSVLNYQTYVSEEPIDSLIKPVKQEFLEPEQEPISWHLGEGNTNTNDDSFPLDITFLDNYFNESLPDISIFDQPMSPIQPTENDFFNDLMLFDSNAEEYYSSEIKEIGSSFNDLDDSLISDLLLV
Protein: Vitamin B12-dependent ribonucleoside-diphosphate reductase (B12-dependent RNR) (EC 1.17.4.1) (Ribonucleotide reductase) (P9WH77)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Interaction partners:
- Ribonucleoside-diphosphate reductase subunit beta nrdF2
- Ribonucleoside-diphosphate reductase subunit beta nrdF1
- R2-like ligand binding oxidase
- UPF0301 protein Rv0038
- Thymidylate kinase
- Cytidylate kinase
- Ribonucleoside-diphosphate reductase subunit alpha
- Adenylate kinase
- Nucleoside diphosphate kinase
- Guanylate kinase
Sequence:
MPGERRRFAQATKSVGVSWPAKVRRRDGTLVPFDIARIEAAVTRAAREVACDDPDMPGTVAKAVADALGRGIAPVEDIQDCVEARLGEAGLDDVARVYIIYRQRRAELRTAKALLGVRDELKLSLAAVTVLRERYLLHDEQGRPAESTGELMDRSARCVAAAEDQYEPGSSRRWAERFATLLRNLEFLPNSPTLMNSGTDLGLLAGCFVLPIEDSLQSIFATLGQAAELQRAGGGTGYAFSHLRPAGDRVASTGGTASGPVSFLRLYDSAAGVVSMGGRRRGACMAVLDVSHPDICDFVTAKAESPSELPHFNLSVGVTDAFLRAVERNGLHRLVNPRTGKIVARMPAAELFDAICKAAHAGGDPGLVFLDTINRANPVPGRGRIEATNPCGEVPLLPYESCNLGSINLARMLADGRVDWDRLEEVAGVAVRFLDDVIDVSRYPFPELGEAARATRKIGLGVMGLAELLAALGIPYDSEEAVRLATRLMRRIQQAAHTASRRLAEERGAFPAFTDSRFARSGPRRNAQVTSVAPTGTISLIAGTTAGIEPMFAIAFTRAIVGRHLLEVNPCFDRLARDRGFYRDELIAEIAQRGGVRGYPRLPAEVRAAFPTAAEIAPQWHLRMQAAVQRHVEAAVSKTVNLPATATVDDVRAIYVAAWKAKVKGITVYRYGSREGQVLSYAAPKPLLAQADTEFSGGCAGRSCEF