wanglab/gogpt-training-data huggingface dataset:
Protein: NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK) (P9WHV7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates as well as inorganic polyphosphate (poly(P)) as a source of phosphorus.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
Interaction partners:
- 16S/23S rRNA
- Tetratrico peptide repeat group 5 domain-containing protein
- Uncharacterized protein
- D-glycerol 3-phosphate phosphatase
- DNA repair protein RecN
- Glutamine-dependent NAD
- Probable nicotinate-nucleotide adenylyltransferase
- Possible transcriptional regulatory protein NadR
- NAD-dependent protein deacylase
- proton-translocating NAD
Sequence:
MTAHRSVLLVVHTGRDEATETARRVEKVLGDNKIALRVLSAEAVDRGSLHLAPDDMRAMGVEIEVVDADQHAADGCELVLVLGGDGTFLRAAELARNASIPVLGVNLGRIGFLAEAEAEAIDAVLEHVVAQDYRVEDRLTLDVVVRQGGRIVNRGWALNEVSLEKGPRLGVLGVVVEIDGRPVSAFGCDGVLVSTPTGSTAYAFSAGGPVLWPDLEAILVVPNNAHALFGRPMVTSPEATIAIEIEADGHDALVFCDGRREMLIPAGSRLEVTRCVTSVKWARLDSAPFTDRLVRKFRLPVTGWRGK
Protein: Myosin heavy chain 7 (Myosin-7) (F1QZW1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Myosin-binding protein C, cardiac-type
- Troponin T type 2a
- Myosin light chain 2 Mlc2a
- Tropomyosin 1
- Actin alpha cardiac muscle 1a
- Tropomyosin alpha-1 chain
- Myosin regulatory light chain 2b
- Myosin, light chain 1, alkali; skeletal, fast
- Myosin, light chain 4, alkali
- Cardiac myosin light chain-1.
Sequence:
MGDAQMAEFGAAASYLRKSDRERLEAQTRPFDMKKECFVPDPDEEYVKASIVSREGDKVTVQTEKRKTVTVKEADIHPQNPPKFDKIEDMAMFTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGQLEEMRDDRLSLIISGIQARSRGLLARVEFQKIVERRDALLVIQWNVRAFMGVKNWPWMKLFFKIKPLLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKSRDVSSKKGHDQE
Protein: T-box protein H15 (Q94890)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- Uncharacterized protein
Sequence:
MLLSNQPANTKPQQTPSPSQTQNFKSKLQQQIVSAAAAAAANIANGSSHHHHHQNHHHHHPLNNHHNHNHNQHNISFATDFSIAAIMARGGNAPSSREPSERSLSPASVERYSGQDADDDVDVDVVDCSDSEMPSATAAAAAAATTAAAAAAALQAQQQARQALRVAQQQQQQQQQQRQQTHHHATTGKQQRQHHNHHSSNTNNSSNSGNSNTNSKSSSQRGRSAAAVGAAATPSPPPPPPSQSPEELERLSPEESPAQQPTPKIVGSCNCDDLTPVQCHLETKELWDKFHELGTEMIITKSGRRMFPTVRVSFSGPLRQIQPADRYAVLLDVVPLDSRRYRYAYHRSSWLVAGKADPPPPSRIYAHPDCPLSPEALRKQVVSFEKVKLTNNEMDKSGQVVLNSMHRYQPRIHLVRLSHGQSIPGSPKELQDMDHKTFVFPETVFTAVTAYQNQLITKLKIDSNPFAKGFRDSSRLSDFDRDPMDAFFFDQHMRTAPLRFFPDPLMSQLTPQEADAASMALLEKARQHLQMFGRSPYTEMLLPHLYQRSAAPPPPPPAPHLSAFQLGMWQQQWPQLTAGFLASANQQAALALAAAGANRTPPPSMAVAPPAPATPTSSCGSASPDLRARPQLNHYPQRFSPYQVPQHQASPPASNRAESP
Protein: Cofilin-2 (Cofilin, muscle isoform) (Q9Y281)
Organism: Homo sapiens (Human)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity).
Subcellular location: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with CSPR3 in the Z line of sarcomeres. {ECO:0000269|PubMed:19752190}.
Interaction partners:
- LIM domain kinase 1
- Actin nucleation-promoting factor WASL
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Src substrate cortactin
- Protein phosphatase Slingshot homolog 1
- Hematopoietic lineage cell-specific protein
- WD repeat-containing protein 1
- LIM domain kinase 2
- Protein phosphatase Slingshot homolog 3
Sequence:
MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (E7F048)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
- Tumor necrosis factor receptor superfamily, member 1a.
- TNF receptor-associated factor 6
Sequence:
MELNEQRYFIVLRRNKKGLSRGTIGRAEGETAEEELIGMVCEGGGSIRSSRTVKKHDTYPLSRHQAGLLMLVCPASRRLELLGNLQLFSAICELARDDLVMVKHKKIFQPCLVKNLVQIGKQDKQGDLQVLGFELELVETENEISLKKTAPLPFFSAADILQVAPSDLNTRVPLRDAIDLGLKRKAVSLLNSLPSLNSRNAKKGSVLFKKDVSESIQALSHYSLEVGSMAEVLSLNGLTVYGVIRWIGVPEGKKNCWAGLELDTEATTCSDGTLGTKRYFTCEANKALFVPLTNCKPDSRFLLIPDEMLKPLNPPSATLVEDLDEDVPPVAEQDVLSHLVGRMKGIQGHFNSCYLDATLFSLFTSSVAFDRIFNRSADSKKGISHILRRDIVNCLRRSGFVPAENVMKFREQLGCKSFASEEKDPEEFITLLLQHVLHIEPLLKIRSQGEFPQEAYTHQIIVEKNQVAAVPSVQQLLEMSFVTSNLKFEEIPSCLIVQMPRFGKKFKMFPKIIPSTELDITDVLHCSPRECFLCGHLAKYECVQCLMDRKLQPGKIKQYCSTCNTQVHNHPTRQEHTPQKLTLPDCPAEDAPVQRHPMQLFAVLCINTSHYVSFVKYGPDPRSWIFFDSMADRCGDDNKGYSIPVIRSCPEVGDFLSQSEEEISSADLSQCSEAVRRLMVDSYMCLYQTTDCQQ
Protein: 2,5-diketo-D-gluconic acid reductase A (2,5-DKG reductase A) (2,5-DKGR A) (25DKGR-A) (EC 1.1.1.274) (AKR5C) (Q46857)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- NADPH-dependent aldehyde reductase YqhD
- HTH-type transcriptional regulator YqhC
- Serine/threonine kinase YeaG
- Lactaldehyde reductase
- Uncharacterized protein YqjD
- Peroxiredoxin OsmC
- Uncharacterized protein YdiZ
- Transketolase 2
- Uncharacterized oxidoreductase YghA
- Transaldolase A
Sequence:
MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIQKALEVGYRSIDTAAAYKNEEGVGKALKNASVNREELFITTKLWNDDHKRPREALLDSLKKLQLDYIDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVWDFRLDKDELGEIAKLDQGKRLGPDPDQFGG
Protein: Rho GTPase-activating protein 44 (NPC-A-10) (Rho-type GTPase-activating protein RICH2) (RhoGAP interacting with CIP4 homologs protein 2) (RICH-2) (Q17R89)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. Acts as a GAP at least for CDC42 and RAC1. In neurons, is involved in dendritic spine formation and synaptic plasticity in a specific RAC1-GAP activity (By similarity). Limits the initiation of exploratory dendritic filopodia. Recruited to actin-patches that seed filopodia, binds specifically to plasma membrane sections that are deformed inward by acto-myosin mediated contractile forces. Acts through GAP activity on RAC1 to reduce actin polymerization necessary for filopodia formation (By similarity). In association with SHANK3, promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation (By similarity).
Subcellular location: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5SSM3}. Recycling endosome {ECO:0000250|UniProtKB:Q5SSM3}. Presynapse {ECO:0000250|UniProtKB:Q5SSM3}. Cell projection, dendrite {ECO:0000250|UniProtKB:F1LQX4}. Note=In CA1 hippocampal synapses, detected at both presynaptic and postsynaptic sites (By similarity). Located in convoluted dendritic plasma membrane sections enriched in polymerized actin and myosin (patches) along dendrites where often emerge filopodia (By similarity). {ECO:0000250|UniProtKB:F1LQX4, ECO:0000250|UniProtKB:Q5SSM3}.
Interaction partners:
- Cdc42-interacting protein 4
- Rho GTPase-activating protein 17
- SH3 domain-binding protein 1
- Ras-related C3 botulinum toxin substrate 1
- Cell division control protein 42 homolog
Sequence:
MKKQFNRMRQLANQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEIEFNITGNYGSPVHVNHNANYSSMPSPDMDPADRRQPEQARRPLSVATDNMMLEFYKKDGLRKIQSMGVRVMDTNWVARRGSSAGRKVSCAPPSMQPPAPPAELAAPLPSPLPEQPLDSPAAPALSPSGLGLQPGPERTSTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQPGASPSPSQPPADQSPHTLRKVSKKLAPIPPKVPFGQPGAMADQSAGQPSPVSLSPTPPSTPSPYGLSYPQGYSLASGQLSPAAAPPLASPSVFTSTLSKSRPTPKPRQRPTLPPPQPPTVNLSASSPQSTEAPMLDGMSPGESMSTDLVHFDIPSIHIELGSTLRLSPLEHMRRHSVTDKRDSEEESESTAL
Protein: Packaging enzyme P4 (EC 3.6.1.15) (P11125)
Organism: Pseudomonas phage phi6 (Bacteriophage phi-6)
Function: Packaging motor with helicase and translocase activities. Part of the packaging complex that packages the viral RNA segments, replicate them into a double-stranded form and transcribe them. is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.
Subcellular location: Virion. Note=Capsid protein found in 72 copies. Prior to RNA packaging, localizes on the outer procapsid surface at the 12 potential RNA portal sites.
Interaction partners:
Sequence:
MPIVVTQAHIDRVGIAADLLDASPVSLQVLGRPTAINTVVIKTYIAAVMELASKQGGSLAGVDIRPSVLLKDTAIFTKPKAKSADVESDVDVLDTGIYSVPGLARKPVTHRWPSEGIYSGVTALMGATGSGKSITLNEKLRPDVLIRWGEVAEAYDELDTAVHISTLDEMLIVCIGLGALGFNVAVDSVRPLLFRLKGAASAGGIVAVFYSLLTDISNLFTQYDCSVVMVVNPMVDAEKIEYVFGQVMASTVGAILCADGNVSRTMFRTNKGRIFNGAAPLAADTHMPSMDRPTSMKALDHTSIASVAPLERGSVDTDDRNSAPRRGANFSL
Protein: Mitochondrial ribosome and complex I assembly factor AltMIEF1 (Alternative MIEF1 protein) (AltMIEF1) (MIEF1 microprotein) (MIEF1-MP) (alternative transcript upstream of MiD51) (AltMiD51) (L0R8F8)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of mitochondrial fission mediated by DNM1L. Positively regulates mitochondrial translation. May play a role in ribosome biogenesis by preventing premature association of the 28S and 39S ribosomal subunits (Probable).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:28892042, ECO:0000269|PubMed:29083303, ECO:0000269|PubMed:30215512}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- Mitochondrial assembly of ribosomal large subunit protein 1
- GTP-binding protein 10
- rRNA methyltransferase 3, mitochondrial
- Probable ATP-dependent RNA helicase DDX28
- Transcription termination factor 4, mitochondrial
- Mitochondrial ribosome-associated GTPase 1
- 5-cytosine rRNA methyltransferase NSUN4
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL21m
Sequence:
MAPWSREAVLSLYRALLRQGRQLRYTDRDFYFASIRREFRKNQKLEDAEARERQLEKGLVFLNGKLGRII
Protein: Glutamate dehydrogenase, mitochondrial (GDH) (EC 1.4.1.3) (P54385)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Glutamate synthase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- Glutamine synthetase 2 cytoplasmic
- Glutamine synthetase 1, mitochondrial
- Multifunctional fusion protein
- alanine transaminase
- Delta-1-pyrroline-5-carboxylate synthase
- omega-amidase
- Glutamate decarboxylase
Sequence:
MYHLKSLARQGARRQQELATLAKALPTAVMQSSRGYATEHQIPDRLKDVPTAKDPRFFDMVEYFFHRGCQIAEESLVDDMKGKLTRDEKKQKVKGILMLMQPCDHIIEIAFPLRRDAGNYEMITGYRAQHSTHKTPTKGGIRFSLDVSRDEVKALSALMTFKCACVDVPFGGAKAGLKINPKEYSEHELEKITRRFTLELAKKGFIGPGVDVPAPDMGTGEREMSWIADTYAKTIGHLDINAHACVTGKPINQGGIHGRVSATGRGVFHGLENFINEANYMSQIGTTPGWGGKTFIVQGFGNVGLHTTRYLTRAGATCIGVIEHDGTLYNPEGIDPKLLEDYKNEHGTIVGYQNAKPYEGENLMFEKCDIFIPAAVEKVITSENANRIQAKIIAEAANGPTTPAADKILIDRNILVIPDLYINAGGVTVSFFEWLKNLNHVSYGRLTFKYERESNYHLLASVQQSIERIINDESVQESLERRFGRVGGRIPVTPSESFQKRISGASEKDIVHSGLDYTMERSARAIMKTAMKYNLGLDLRTAAYVNSIEKIFTTYRDAGLAF
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (P39749)
Organism: Mus musculus (Mouse)
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. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Proliferating cell nuclear antigen
- DNA ligase 1
- DNA polymerase beta
- DNA polymerase delta catalytic subunit
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA repair nuclease/redox regulator APEX1
- Double-strand break repair protein MRE11
- DNA polymerase delta subunit 2
- DNA polymerase epsilon catalytic subunit A
Sequence:
MGIHGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSLMGMFYRTIRMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQEAGMEEEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALAKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRVLQELGLNQEQFVDLCILLGSDYCESIRGIGAKRAVDLIQKHKSIEEIVRRLDPSKYPVPENWLHKEAQQLFLEPEVVDPESVELKWSEPNEEELVKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGPAKKKAKTGGAGKFRRGK
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (A0A8J8YLI4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
Interaction partners:
Sequence:
MIGQKTLYSFFSPTPTGKRTTRSPQPAPGSGVTAENSSDAAASPAKKARVEQDEPATPPSSPLSAEQLVRIQRNKAAALLRLAARNVPAGLGESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISWKEL
Protein: Armadillo repeat-containing protein 5 (Q96C12)
Organism: Homo sapiens (Human)
Function: Involved in fetal development, T-cell function and adrenal gland growth homeostasis (By similarity). Negatively regulates adrenal cells survival. Plays a role in steroidogenesis, modulates steroidogenic enzymes expression and cortisol production.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24283224}.
Interaction partners:
- Decapping and exoribonuclease protein
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
- High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
Sequence:
MAAAKPTLTDSLSFCLAQLAAAAGEALGGEKDPATNETPLSRALLALRTRHIKAAGGIERFRARGGLRPLLALLRRAAAAGSAPSQAGPGSAPSSAASGASSPAPASGPAPSAVSSSSPTPPVRLRKTLDLALSILADCCTEGACRTEVRRLGGILPLVTILQCMKTDSIQNRTARALGNLAMEPESCGDIHCAGAVPLLVESLTACQDSQCLQSVVRALRNLADSPQHRLALAQQGAVRPLAELLATAPDAALTLALVRALLELSRGCSRACAEQLSLGGGLGPLVSLASHPKRAVREGTILILANLCAQGLIRPALGNAGGVEVLVDELRQRRDPNGASPTSQQPLVRAVCLLCREAINRARLRDAGGLDLLMGLLRDPRASAWHPRIVAALVGFLYDTGALGRLQALGLVPLLAGQLCGEAGEEEEEGREAASWDFPEERTPERAQGGSFRSLRSWLISEGYATGPDDISPDWSPEQCPPEPMEPASPAPTPTSLRAPRTQRTPGRSPAAAIEEPWGREGPALLLLSRFSQAPDPSGALVTGPALYGLLTYVTGAPGPPSPRALRILSRLTCNPACLEAFVRSYGAALLRAWLVLGVAPDDWPAPRARPTLHSRHRELGERLLQNLTVQAESPFGVGALTHLLLSGSPEDRVACALTLPFICRKPSLWRRLLLEQGGLRLLLAALTRPAPHPLFLFFAADSLSCLQDLVSPTVSPAVPQAVPMDLDSPSPCLYEPLLGPAPVPAPDLHFLLDSGLQLPAQRAASATASPFFRALLSGSFAEAQMDLVPLRGLSPGAAWPVLHHLHGCRGCGAALGPVPPPGQPLLGSEAEEALEAAGRFLLPGLEEELEEAVGRIHLGPQGGPESVGEVFRLGRPRLAAHCARWTLGSEQCPRKRGLALVGLVEAAGEEAGPLTEALLAVVMGIELGARVPA
Protein: Bromodomain PHD finger transcription factor splice variant (E5D6T0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVSEEDEEEEEDGDAEETQDSEDEEEDDMEEDDDDSDYPEEMEDDDDDASYCTESSFRSHSTYSSTPGRRKPRVHRPRSPILEEKDIPPLEFPKSSEDLMVPNEHIMNVIAIYEVVRNFGNVLRLSPFCFEDFCAALVSQEQCTLMAEMHVALLKAVLREEDTSNTTFGPADLKDSVNSTLYFIDGMTWPEVLRVYCESDKEYHHVLPYQEAEDYPYGPVENKIKVLQFLVDQFLXTNIAREELMSEGVIQYDDHCRVCHKLGDLLCCETCSAVYHLECVKPPLEEVPEDEWQCEVCVAHKVPGVTDCVAEVQKNKPYVRHEPIGYDRSRRKYWFLNRRLIIEEDTDNENEKKVWYYSTKVQLAELIDCLDKGYWEAELCRVLEDIREEMQQHMDVTEDLTNKARGSNKSFLAAANEEILDSLRIKRGEDIDCDQSPEDPEKDKHEGENNSSKDAEKSREEAEDPSADKDADSKGLEEEPGHGKPEGDFRLEKSNGEVSESPGAGKGTSGSTRIITRLRNPESKLSQLKSQQVAAAAHEANKLFKEGKEVLVVNSQGEVSRLSTKKEVVMKGNINNYFKLGQEGKYRVYHNQYSTNSFALNKHQHREDHDKRRHLAHKFCLTPAGEFKWNGSVHGSKVLTISTLRLTITQLESNIPSSFLHPNWASHRANWIKAVQMCSKPREFALALAILECAVKPVVMLPIWRESLGHTRLHRMTSIEREEKEKVKKKEKKQEEEETMQQATWVKYTFPVKHQVWKQKGEEYRVTGYGGWSWISKTHVYRFLPKLPGNTNVNYRKPLDGAKNNTDENKDESEKRKSPRSPKKMKTECDSEQGETRDADATAGAAAGAMELSKEPEKKDQDVKELLDSDNDKSFKEEPMEIDDTIKTESHVSSLESTEVDVVNVSEGFHLRTSYKKKTKSSKLDGLLERRIRQFTLEEKQRLEKLKLESGVKGAGKPPMGALKSSSESPGSTKASEGHQGDSLRQEQSPSSSQASTVDLGLGGSQSDPLVLGISPPSLSTHKPDPKDQVLDDVSIQSPGPNCQRQNSVESDLDARISEPAGKGLELSQTKTEVTDSSSDDSKPTSADDVGILICKSRKLHSQDDSSTVVSSSKSTLPASVPKSPRDRDARAFSKAVDFDGRLGGDSEYSSTLENSSDNMCIRDSAEEDMVVQNSSEATSKRFIAPEQGGESVESTKCQVVSKSTENCEDKLQGKVTEANGKKLGQHPPKPEERAVNRCTDQVSLRHSVDRKNSEPRESEKKGQKANKFQINGKDSKAKGYLKGPGTKDGSDGKVVSSAVEPKVNNINKVIPGNTKSLAGKESAAKPFINGDIIMEELSEQNTSETNSYSLSSSDAKGNHQDGLHTLPSTKESASTQVITPRAPCPDRNSLSQVEDMETESPEVKRVIPSPVRTGEGSNLSKGFMDDNGLPSSKDENVNGESQRKTVITEVTTMTSTVATESKTVIKVAKGDKQTVVSSTENCARSTVTTTTTTVTKLSTPSPDTGVDTISVKEQSKTVVTTTVTDSLTTAGSTLVTSMTVSKEYSTRDRVKLMKFSRPKKTRSGTALPSYRKFVTKSSKKSIFVLPNDDLKKLARKGGIREVPYFNYNAKPALDIWPYPSPRPTFGITWRYRLQTVKSLAGVSLMLRLLWASLRWDDMAAKAPPGGGSTRTETSETEITTTEIIKRRDVGPYGIRSEYCIRKIICPIGVPEAPKETPTPQRKGLRSSALRPKRPETPKQTGPVIIESWVAEEELELWEIRAFAERVEKEKAQAAEQQTKKRLEQQKPAVIAASTTSPANNTSSTVSPAQKVMVAPLSGSVTPGTKMVLATKVGSPATVTFQQNKNFHQTFATWVKQGQSNSGMVQVQQKVLGIIPSTTGPSQQTFTSFQPRTATVTIRPNTSASAGTTTTSQVITGPQIRPGMTVIRTPLQQPALGKAIIRTPVVVQPGTPQQVVTQIIRGQPVSTAISAPSTASSAPVQKGLTPGAAAGPLQPSAPHSPRPQQGQVKLTMAQLTQLTQGHGGNQGLTVVIQGQGQTTGQLQLIPQGMTVLPGPGQQLMQAAMPNGTVQRFLFTPLSTSATAASSSSNSSSTTTNATAAGSGEQKQSKILPQTQVQPATTLAPTQSSSVSPAEAQPQPAQPAAQPQPQPQPPAQPEVQTQPAVSSHVPSETQPSQAQTSKPLVATQCQPRSSVQGQSPVRVQSPPLTRIRPSTPSQVTPGQQPQVQTTASQPIPIPPPTSLQAPSQGQPQSQPQVVMKHNAVIEHLKQKKTMTPAEREENQRMIVCNQVMKYILDKIDKEEKQAAKKRKREESVEQKRSKQNASKLSALLFKHKEQLKAEILRKRALLDKELQIQVQEELKRDLKMKREREMAQAVQANAASVPTPSVPAPVPAPAPAAPPAPPRSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEADLIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPRDTPFYQCAEVLESFFVQKLKGFKASRSHNNKLQSTAPD
Protein: V-type proton ATPase subunit E1 (V-ATPase subunit E1) (Protein EMBRYO DEFECTIVE 2448) (Vacuolar H(+)-ATPase subunit E isoform 1) (Vacuolar proton pump subunit E1) (Q39258)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Required for Golgi organization and vacuole function in embryogenesis.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15610355}; Peripheral membrane protein {ECO:0000269|PubMed:15610355}.
Interaction partners:
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit D
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit H
- Vacuolar ATP synthase catalytic subunit-related / V-ATPase-related / vacuolar proton pump-like protein
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit d2
Sequence:
MNDGDVSRQIQQMVRFIRQEAEEKANEISVSAEEEFNIEKLQLVEAEKKKIRQDYEKKEKQADVRKKIDYSMQLNASRIKVLQAQDDIVNAMKDQAAKDLLNVSRDEYAYKQLLKDLIVQCLLRLKEPSVLLRCREEDLGLVEAVLDDAKEEYAGKAKVHAPEVAVDTKIFLPPPPKSNDPHGLHCSGGVVLASRDGKIVCENTLDARLDVAFRMKLPVIRKSLFGQVTA
Protein: Metal regulatory transcription factor 1 (MRE-binding transcription factor) (Transcription factor MTF-1) (Q07243)
Organism: Mus musculus (Mouse)
Function: Zinc-dependent transcriptional regulator of cellular adaption to conditions of exposure to heavy metals. Binds to metal responsive elements (MRE) in promoters and activates the transcription of metallothionein genes like metallothionein-2/MT2A (By similarity). Also regulates the expression of metalloproteases in response to intracellular zinc and functions as a catabolic regulator of cartilages.
Subcellular location: Nucleus {ECO:0000269|PubMed:24529376}. Cytoplasm {ECO:0000269|PubMed:24529376}. Note=Translocation to the nucleus is induced by metals. {ECO:0000269|PubMed:24529376}.
Interaction partners:
- Proton-coupled zinc antiporter SLC30A1
- Cysteine and glycine-rich protein 1
- Metallothionein-1
Sequence:
MGEHSPDDNIIFFKGEEDDLTPHDKMLRFVDDNGLVPSSSGTVYDRTTVLIEQDPGTLEDDEDDGQCGEPLPFLVEGEEGFLIDQEAMSQGYVQHIISPDQIHLTINPGSTPMPRNIEGATLTLQSECPETKRKEVKRYQCTFEGCPRTYSTAGNLRTHQKTHRGEYTFVCNQEGCGKAFLTSYSLRIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESQGCSKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGERPFFCPSNGCEKTFSTQYSLKSHMKGHDNKGTAYSALPQHNGSEDTNHSLYLSELGLLSTDSELQENSSSTQDQDLSTISPAIIFESMFQNSDDPGIQDDPLQTAALIDSFNGDAESVIDVPPPAGNSASLSLPLVLQSGISEPPQPLLPATAPSAPPPAPSLGPGSQPAAFGSPPALLQPPEVPVPHSTQFAANHQEFLPHPQAPPQTIVPGLSVVAGAPASAATVASAVAAPAPPQSTTEPLPAMVQTLPLGANSVLTNNPTITITPTPNTAILQSSLVMGEQNLQWILNGATSSPQNQEQIQQASKVEQVYFATAVPVASGTGSSVQQIGLSVPVIIIKQEEACQCQCACRDSAKERAAGRRKGCSSPPPPEPNPQPPDGPSLQLPP