wanglab/gogpt-training-data huggingface dataset:
Protein: DNA gyrase inhibitor YacG (P0A8H8)
Organism: Escherichia coli (strain K12)
Function: Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
Interaction partners:
- DNA gyrase subunit B
- DNA gyrase subunit A
- Dephospho-CoA kinase
- Cell division protein ZapD
Sequence:
MSETITVNCPTCGKTVVWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEEPKQ
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (A0A140VJE0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368116}.
Interaction partners:
Sequence:
MTSVRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH
Protein: DNA polymerase alpha subunit B (F4HTP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR018300}.
Interaction partners:
- Probable DNA primase large subunit
- DNA primase
- DNA polymerase alpha catalytic subunit
- DNA polymerase epsilon catalytic subunit B
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon subunit B
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta small subunit
- Replication factor C subunit 3
- Replication factor C subunit 2
Sequence:
MATDEEIKNEFKRSGFILVEEDEILKRCVTLCINYSLKPSDLVSSWELYHLNRQLLDQTVKKDDMDGFVLHLQNEQKESIMRVEEAGLHLYSNRDVDMLLDGVQEDTEEIVTTPTNKSQRLHPDPFDSISRSRDYGYSTGKSVGHVTPFGSRIEKFVVKFNVGNVAAHAENGNNNDVENSEDDIIKRVQTSQRCSLKVNGSGPEPGCRFMYDRTEDRFSALEYRIVRHADAFAASGLYEEQVDPAVASQRSIFAVGMICCDGEGHLNDKSILLQSSAERTSGQRVPVDLKRLDQFSIFPGQVVGIEGQNPSGHYLTASKLLDSVPLTLTVDVDLPPAKRQILDQEVLVPAEESCQKSEVSFIIASGPFTTSDNLLFEPLNELLAYAKRKPPQLLVLLGPFVDSEHPEIKKGAVDATFNEIFQVEVLRKLQDYVEFMGSEVRVVLVPSIRDANHDFIFPQPPFDIHIPDLEHQMTSLSNPGTFEANQVKVSCCTVDVLKQLSGEEMSKNPSGVPTDRMSRLASHLLRQRSFYPLYPPPESLPYDSSLAPKALQISSIPDILLLPSDMRYFVKILSLGEEEDAAKCVCVNPGRLAKGEGAGTFVELTYKGGPESMHASIISI
Protein: Epithelial splicing regulatory protein 1 (RNA-binding motif protein 35A) (RNA-binding protein 35A) (Q6NXG1)
Organism: Homo sapiens (Human)
Function: mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2. Regulates splicing and expression of genes involved in inner ear development, auditory hair cell differentiation, and cell fate specification in the cochlear epithelium (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19285943}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein M
- Protein enabled homolog
- Epithelial splicing regulatory protein 2
- Grainyhead-like protein 2 homolog
- KH domain-containing RNA-binding protein QKI
- Catenin delta-1
- Ribonucleoside-diphosphate reductase large subunit
- RNA binding protein fox-1 homolog 2
- Ras-related protein Rab-25
- Fibroblast growth factor receptor 2
Sequence:
MTASPDYLVVLFGITAGATGAKLGSDEKELILLFWKVVDLANKKVGQLHEVLVRPDQLELTEDCKEETKIDVESLSSASQLDQALRQFNQSVSNELNIGVGTSFCLCTDGQLHVRQILHPEASKKNVLLPECFYSFFDLRKEFKKCCPGSPDIDKLDVATMTEYLNFEKSSSVSRYGASQVEDMGNIILAMISEPYNHRFSDPERVNYKFESGTCSKMELIDDNTVVRARGLPWQSSDQDIARFFKGLNIAKGGAALCLNAQGRRNGEALVRFVSEEHRDLALQRHKHHMGTRYIEVYKATGEDFLKIAGGTSNEVAQFLSKENQVIVRMRGLPFTATAEEVVAFFGQHCPITGGKEGILFVTYPDGRPTGDAFVLFACEEYAQNALRKHKDLLGKRYIELFRSTAAEVQQVLNRFSSAPLIPLPTPPIIPVLPQQFVPPTNVRDCIRLRGLPYAATIEDILDFLGEFATDIRTHGVHMVLNHQGRPSGDAFIQMKSADRAFMAAQKCHKKNMKDRYVEVFQCSAEEMNFVLMGGTLNRNGLSPPPCKLPCLSPPSYTFPAPAAVIPTEAAIYQPSVILNPRALQPSTAYYPAGTQLFMNYTAYYPSPPGSPNSLGYFPTAANLSGVPPQPGTVVRMQGLAYNTGVKEILNFFQGYQYATEDGLIHTNDQARTLPKEWVCI
Protein: Small COPII coat GTPase SAR1A (EC 3.6.5.2) (P36536)
Organism: Mus musculus (Mouse)
Function: Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining endoplasmic reticulum exit sites (ERES) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NR31}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NR31}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9NR31}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NR31}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NR31}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NR31}. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII. Upon leucine deprivation, associates with lysosomal membranes to repress TORC1 signaling. {ECO:0000250|UniProtKB:Q9NR31}.
Interaction partners:
- Protein SEC13 homolog
- Guanine nucleotide-exchange factor SEC12
- Protein transport protein Sec31A
- Protein transport protein Sec31B
- SEC24 homolog B, COPII coat complex component)
- Protein transport protein Sec23A
- Protein transport protein Sec24A
- Protein transport protein Sec23B
- SEC24 homolog C, COPII coat complex component
- Small COPII coat GTPase SAR1B
Sequence:
MSFIFEWIYNGFSSVLQFLGLYKKSGKLVFLGLDNAGKTTLLQMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHEQARRVWKNYLPAINGIVFLVDCADHSRLMESKVELNALMTDETISNVPILILGNKIDRTDAISEEKLREIKGLYGQTTGKGNVTLKELNARPMEVFMCSVLKRQGYGEGFRWLSQYID
Protein: Heavy metal-associated isoprenylated plant protein 32 (AtHIP32) (Q9M8K5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein.
Interaction partners:
- DPP6 N-terminal domain-like protein
- Heavy metal-associated isoprenylated plant protein 31
- Heavy metal-associated isoprenylated plant protein 39
- RGG repeats nuclear RNA binding protein B
Sequence:
MSKEEFMKIQTCVLKVNIHCDGCKQKVKKILQKIEGVFTTKIDSEQGKVTVSGSVDPSVLIKKLAKSGKHAEIWGAPKGNNNPNQSQMANQFKGMQIDHGKAGGGGGGNNNNNKKGQKNGGGGGGGGGGGNSNAPKMGQQLNPQHLQQLQQLQKMKGFQDLKLPPQLKGSVPVNKNQNQKGVKFDVPEDDDDDDFSDEFDDEFTDDDDDEFDDEFDDLPLPSNKMKPNMTMMPNAQQMMMNAQKNANLAGGPAKNGGKGAPAAGGGGAGGGKGAGGGAKGGPGNQNQGGGKNGGGGHPQDGKNGGGGGGPNAGKKGNGGGGPMAGGVSGGFRPMGGGGPQNMSMPMGGQMGMGGPMGNMPAVQGLPATGPGGAPQGYFQGAGIDPMQMQQQQQQQQYLAAVMNQQRAMGNERFQPMMYARPPPAVNYMPPNPHQYPNPHPYPYPYPYPYPPPYGNDQYSHAFSDENTSSCDIM
Protein: GH04236p (Serine-arginine repetitive matrix 2/3/4, isoform B) (Q86BP9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGQGKTDLAKDEFGRVAARDTHQIAEAQQQKNARLREAFNISEYFVEGSSFDGDRKAKEDLAKSVALQKELDAQRESLAAAAAAAAAGKDKETGKRYALVRTPSRERDRDAGDAAANGDERDHVSKTDKKKRKKRARESSASPERKKKKKSKKHKKER
Protein: Crk-like protein (P46109)
Organism: Homo sapiens (Human)
Function: May mediate the transduction of intracellular signals.
Interaction partners:
- Breast cancer anti-estrogen resistance protein 1
- Rap guanine nucleotide exchange factor 1
- E3 ubiquitin-protein ligase CBL
- Tyrosine-protein kinase ABL1
- Dedicator of cytokinesis protein 1
- Epidermal growth factor receptor
- GRB2-associated-binding protein 1
- Signal transducer and activator of transcription 5A
- Signal transducer and activator of transcription 5B
- Adapter molecule crk
Sequence:
MSSARFDSSDRSAWYMGPVSRQEAQTRLQGQRHGMFLVRDSSTCPGDYVLSVSENSRVSHYIINSLPNRRFKIGDQEFDHLPALLEFYKIHYLDTTTLIEPAPRYPSPPMGSVSAPNLPTAEDNLEYVRTLYDFPGNDAEDLPFKKGEILVIIEKPEEQWWSARNKDGRVGMIPVPYVEKLVRSSPHGKHGNRNSNSYGIPEPAHAYAQPQTTTPLPAVSGSPGAAITPLPSTQNGPVFAKAIQKRVPCAYDKTALALEVGDIVKVTRMNINGQWEGEVNGRKGLFPFTHVKIFDPQNPDENE
Protein: Lysosomal enzyme trafficking factor (GNPTAB cleavage and activity factor) (GCAF) (Transmembrane protein 251) (Q8N6I4)
Organism: Homo sapiens (Human)
Function: Required for mannose-6-phosphate-dependent trafficking of lysosomal enzymes. LYSET bridges GlcNAc-1-phosphate transferase (GNPTAB), to the membrane-bound transcription factor site-1 protease (MBTPS1), thus allowing proteolytic activation of the GNPTAB. GNPTAB is involved in the regulation of M6P-dependent Golgi-to-lysosome trafficking of lysosomal enzymes. LYSET is thus an essential factor for maturation and delivery of lysosomal hydrolases.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:33252156, ECO:0000269|PubMed:36074821, ECO:0000269|PubMed:36096887}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with GNPTAB and GNPTG in Golgi apparatus cisternae. {ECO:0000269|PubMed:36074821}.
Interaction partners:
Sequence:
MPKPPDYSELSDSLTLAVGTGRFSGPLHRAWRMMNFRQRMGWIGVGLYLLASAAAFYYVFEISETYNRLALEHIQQHPEEPLEGTTWTHSLKAQLLSLPFWVWTVIFLVPYLQMFLFLYSCTRADPKTVGYCIIPICLAVICNRHQAFVKASNQISRLQLIDT
Protein: 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) (Q8MYR7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGFTNARLWPADWYQGVQQIAAKSPLLISQTAHKSDMRELNYTLAIKSDSVNELRSQILVLLEHSSDNVATAINKLSFAQCTYLLSVYWLEMLRVENADEPSLEPIMSYLCDTALQRDKTGIWQCVKCVADQVFEKFRNVLYAHDEIREKVLESQATLLLVYFNHIHKPIQMVADQYLSFLVDRFPHLLWNRRVLWCMLDILQLLAYSLSLDPNEETPTLRVVSTPYTLQLMDSLPARELRLKDFADRCQGIVNEAMKWAPRSTRSHLQEYPNQIPTPVLAHHSGLALAFDSVVSSSAQHTGTMSKRPSCVNSDTPRFVSVLCLRSKYAGEISGLLSVLSEKDKAGLADRLVSDVWEACAEKSDARHRGALWRATAYLIICSEISRKLLHAVASSQLELFTESAMETAVECWQWVLTARQDLELCFIQEMVSAWQTTFEKRMGLFAWETEVTHPLAAYEGCKLVSKPILIAPHLIWLQLLSEMVDTAKYCNRDKVEMFCLLLHRCLPVLKSSKQNRQVSTVGCRFKLLQCGLSLLQGNTIPKSLSRNILRERIYSNALDYFCGPPTCPNQSREQLLEDIMILLKFWQTMRSEKKHLVTSEVGDYDLTNASVSSTQMLAVRNNPETASLISGGGLVNDYTRSMSASGNAVGMGMGVAGGGSSSGWYNTIPHSTSTLSKRSNRSKRLQYQKDSYDKDYMKKRNLILELLAVELEFLITWYNPNSLPDLIVPGEEQITEWRNRPYKSTVWRDYARLAWCYNPALAVFLPQRIKNAEIIDEEVSRLVCSDPIAVCHIPEALKYLCTTKNLLQESPDLVYILSWSPVTPIQALAYFSRQYPSHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDTMGYVVEFIKNISRRSQIVAHQLIWNMQTNMYMDEDQQHKDPNLYEALDQLSQSIIASFSGAAKRFYEREFDFFGKITAVSGEIRSFAKGIERKNACLAALSRIKVQGGCYLPSNPEAMVLDIDYSSGTPMQSAAKAPYLARFRVYRCGITELETRAMEVSNNPNSQEDAKMTLGVESWQAAIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSGLSEYFQHQYGDESSKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPGGNIGFEPDMKLTDEMVMIMGGKMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRGQTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQYYQNQIPY
Protein: Nuclear distribution protein nudE homolog (Q9VT70)
Organism: Drosophila melanogaster (Fruit fly)
Function: Chaperone protein with functions in nuclear localization. Required for centrosome duplication and formation and function of the mitotic spindle (By similarity). In postmitotic neurons, acts with nudC downstream of dar1 to ensure correct positioning of the nuclei in primary dendrites and as a consequence, is required for determining multipolar neuron morphology.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the interphase centrosome and to the mitotic spindle. {ECO:0000250}.
Interaction partners:
- Lissencephaly-1 homolog
- Kinesin heavy chain 73, isoform E
- Nuclear migration protein nudC
- 14-3-3 protein epsilon
- Spindly
- Kinesin heavy chain
- Protein bicaudal D
- Dynein light intermediate chain
- Protein zwilch
Sequence:
MESPPMFNSVEDECRYWKERSKQYHKEWTDVKQEYDEFVEQSREMEIEMDATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEKGLLQEKLQRLMDETRDLKQELNVKSRFTPVVNGTSVPTANDTNTVNSSMNSSASLPNGIVANGELVKHDNAVATRATSVSVNALNGSLVNRNEYNQQHSLKSDGDETEDVPREWSANAAATPLLPAIHTSGAGRTALLLAGCRVVWILQFSVIHKPQIRNPIT
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4I2K0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative U-box domain-containing protein 53
- U-box domain-containing protein 52
- U-box domain-containing protein 34
- U-box domain-containing protein 51
- U-box domain-containing protein 35
- Probable E3 ubiquitin-protein ligase ARI3
Sequence:
MDSARSWFHKFQPRDKPRKKDMFSGSTYGGGVTETTVPDGGNDTETATKLPPLGGDGEALSNSTKQKVAAAKQYIENHYKEQMKNLNERKERRTTLEKKLADADVCEEDQTNLMKFLEKKETEYMRLQRHKMGADDFELLTMIGKGAFGEVRVVREINTGHVFAMKKLKKSEMLRRGQVEHVRAERNLLAEVDSNCIVKLYCSFQDNEYLYLIMEYLPGGDMMTLLMRKDTLSEDEAKFYIAESVLAIESIHNRNYIHRDIKPDNLLLDRYGHLRLSDFGLCKPLDCSVIDGEDFTVGNAGSGGGSESVSTTPKRSQQEQLEHWQKNRRMLAYSTVGTPDYIAPEVLLKKGYGMECDWWSLGAIMYEMLVGYPPFYADDPMSTCRKIVNWKTHLKFPEESRLSRGARDLIGKLLCSVNQRLGSTGASQIKAHPWFEGVQWEKIYQMEAAFIPEVNDDLDTQNFEKFDEEDNQTQAPSRTGPWRKMLSSKDINFVGYTYKNFEIVNDYQVPGIAELKKKESKSKRPSVKSLFESESDSSSSGSEQQTINRSYSNPTPRGMEPNLRRLDSE
Protein: Seminal fluid protein 24Bc (C4NAN9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQYFVILFAIISFLALAHGKKDPMCRNKPFAVGKCQQIVTGYTFAPKKKRCSRFSAEGCRVTGNFFNTRQQCEEKCWDEYQDLVEFQKNLLSLLAEIPEE
Protein: Hydroperoxide isomerase ALOXE3 (Epidermis-type lipoxygenase 3) (Epidermal LOX-3) (e-LOX-3) (eLOX-3) (Hydroperoxy dehydratase ALOXE3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Hydroperoxy icosatetraenoate isomerase) (EC 5.4.4.7) (D3ZKX9)
Organism: Rattus norvegicus (Rat)
Function: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (By similarity). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
Interaction partners:
- NIPA-like domain containing 4
- Protein-glutamine gamma-glutamyltransferase K
Sequence:
MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFCKDPWYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPGTARTICQDALPLLLDHRKRELQARQECYRWKIYAPGFPRMVDVSSFEEMESDKKFALTKTAPCADQDDNSGNRYLPGFPMKVDIPSLLHMEPNIRYSATKTASLIFNALPASLGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPIMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCLNGRQQYVTAPLCLLWLNPQGVLLPLAIQLSQIPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRRGLIYLMSTGLAHFTYTDFCLPDSLRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPNDACVQQDSELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGNTTMESYLETLPEVNTTCSNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQKCLAQISKDIRARNESLALPYAYLDPPLIENSVSI
Protein: Ribosomal protein L31 (Q1G3G5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ribosomal protein L18e/L15 superfamily protein
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- COX assembly mitochondrial protein
- Uncharacterized protein
- AT5g03660/F17C15_80)
- Defensin-like protein 196
- Uveal autoantigen with coiled-coil/ankyrin
- At3g05070
- Small ribosomal subunit protein uS17y
- Adenylyl cyclase
Sequence:
MKKGLHPQMQWISYVTQSGRLMHVMMTRIHHVGKVYHFGAKRQMAQSIGQIAKFKRRFNEQEAEAAEENNNENQNK
Protein: dITP/XTP pyrophosphatase (EC 3.6.1.66) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (Q9PMS6)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Interaction partners:
- GMP synthase
- Glutamate racemase
- Inosine-5'-monophosphate dehydrogenase
- GTP cyclohydrolase 1
- Adenylosuccinate synthetase
Sequence:
MKIILATSNKHKVLELKEILKDFEIYAFDEVLMPFEIEENGKTFKENALIKARAVFNALDEKQKKDFIALSDDSGICVDVLEGNPGIYSARFSGKGDDKSNRDKLVNEMIKKGFKQSKAYYVAAIAMVGLMGEFSTHGTMHGKVIDTEKGENGFGYDSLFIPKGFDKTLAQLSVDEKNNISHRFKALELAKIILKILNKG
Protein: V-type ATP synthase, subunit (VAPC-THERM) (Q5SIT5)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Interaction partners:
Sequence:
MTGGLVLNAISRAGGAMGGLGLIKSLAEKEKQLLERLEAAKKEAEERVKRAEAEAKALLEEAEAKAKALEAQYRERERAETEALLARYRERAEAEAKAVREKAMARLDEAVALVLKEVLP
Protein: Telomeric repeat-binding factor 2 (TTAGGG repeat-binding factor 2) (Telomeric DNA-binding protein) (Q9PU53)
Organism: Gallus gallus (Chicken)
Function: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. Chromosome, telomere {ECO:0000250|UniProtKB:Q15554}. Note=Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. {ECO:0000250|UniProtKB:Q15554}.
Interaction partners:
- Telomeric repeat-binding factor 2-interacting protein 1
- Protection of telomeres protein 1
- Uncharacterized protein.
- GOLD domain-containing protein.
- H/ACA ribonucleoprotein complex subunit DKC1
- Telomerase reverse transcriptase
- Telomere repeat binding bouquet formation protein 1.
- Zinc finger protein 276
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- Chromosome 10 open reading frame 88.
Sequence:
MAAKRSRAAMEEQEKTSTRSDDREQAVNRWVLQFYFHQAVAAYRAGRNRDFRQLRDVMQALLVRPLEREPAVAQMLRVMQFLSRIEEGENLDCTFDKETELTPLESAIGILQLIAKEFSVPEKKIELIHKVLKEAAVIVCIKNKEFSKALAVLKRHMEKDTGNQKKRTELQTIIREKNRAHPIIRDFSYVNFQQYMFQFLKTYVDTSEPLLVTMMKSLNSERAEEPKRSSVTPESPSRTEDQEEAYEPLRRVKHSVGTLRRAETAGGVAGAPSCPEMAKDPTGAPEHVGTVKDAVRAPCPAESTEDSQGTPRCAETARDVMGAPSPSEMTKDLLGAPKCTETARDVVRAPSPAESTKDPVGTPGHAETARDVARAPSPAETTKNLPGAPECADTVKNTVRAPSPAERRKDLVRAPKRAETARDVVRAPSPAERVKDTAGASEPMKSASYPTASQPRIAAVKSSKVFSVPVEISEQPAAAAPVHAGVSSRDLERTPFRTVTTYGISVLREAFKMLSNSPDSDALFNKLDETDLPSPQQMSPSVSHRTKRRKEEKNQGSETLDSPEIPHKSKRLFTISKMIMDQGSQCSKSSESPDSSQERVVSSAYRPVQELPDQPVSTKRSSQQRWNSSYGEERKDSWSDEDELFTDAALTETSSNNSTVYGSKKQKWTVQESEWIKDGVRKYGEGRWKTISEKYPFQNRTSVQIKDRYRTMKKLGIA
Protein: Threonine--tRNA ligase, chloroplastic/mitochondrial 2 (EC 6.1.1.3) (Protein EMBRYO DEFECTIVE 2761) (Threonyl-tRNA synthetase) (ThrRS) (F4IFC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16251277}. Mitochondrion {ECO:0000269|PubMed:16251277}.
Interaction partners:
- Valine--tRNA ligase, chloroplastic/mitochondrial 2
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Valine--tRNA ligase, mitochondrial 1
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase, chloroplastic/mitochondrial
- Cysteine--tRNA ligase 2, cytoplasmic
- Cysteine--tRNA ligase 1, cytoplasmic
- Lysine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MASSHSLLFSSSFLSKPSSFTSSLRRFVYLPTRQFWPRQRHGFSTVFAVATEPAISSSGPKKAEPSTVVLPSNESSDKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIDNGFYYDFDMEPLTDKDLKRIKKEMDRIISRNLPLLREEVSREEAKKRIMAINEPYKMEILDGIKEEPITVYHIGNEWWDLCAGPHVETTGKINKKAVELESVAGAYWRGDEKRQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRIGQDLDLFSIQDEAGGGLVFWHPKGAIVRNIIEESWKKMHVEHGYDLIYTPHVAKADLWKISGHLDFYRENMYDQMEIEDELYQLRPMNCPYHILLYQRKRQSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILSRFGFNKYEVNLSTRPEKSVGGDDIWEKATCALRDALDDKGWSYEVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPQRFDITYVDTNSDKKRPIMIHRAVLGSLERFFGVLIEHYAGDFPLWLSPVQVRVLPVTDNQLEFCKEVSKKLRACGVRAELCHGERLPKLIRNAETQKIPLMAVVGPKEVETGTVTVRSRFGGELGTIPVDDLINKINIAVETRTAL
Protein: WW domain-containing protein (Q2UMF2)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MNPSKARQGNHSDEELFIHTPGRSPVEPPIVGPLRINKRDTPSPVPQGAPLPYPDDRQNPQKMRSASTSRPTPTADGGRTGGSPTNPDNMPSIPANTGPSRSDYPAALRPRDGREPKPATLAERRGNVPKPLPESPAGDTPDKEGLFVTRYQRTPAPPALANGTQLDGTVHPNYRQQYYPPPQAATSSGPSARPPTAQSLQTPSSAINRISSTASTSTTRAQRGSPPPPETPIVEPGQPPASDIEARYAASGIAGTSALAGLQAQSSAAHRRAEQYVGQQATSQPPVQRPWTPTEQPGSQPHGPPTVYQGAEVVSTENLPGNPFPPQSAASSAQAGQALHHPRIPSNALEQDLERMRISSSPPPAYSSVSGPATSQGYPNEKQRAQTTPGQQAASAVHPATVAPINAATNSAALEVSAQDHPAFANDPRQEQPLEQSLQNGTQTGVLDGQQQIVQESQAAMLPTSTGIPPASPPPLPEGWIAHMDPNSGQYYYIHLPTQSTQWEFPKGPTPLNLNETPLSPVGSIYSSHPLASPGLSAFGKPLASPGIPLTPGYESLQSPVVAGFTGPPPSSGVDLYKVAPTNGVYFGPYLRYVNMNLERGIWLGSILLVTDAAQPPTIHIHQSVDLSPNPRQLKASAIAVHQRWTFYKYDVDLQMNESGPAKWTYAITSHLGCTRYEFLVAGRHETNWRFVTTSGNDFSLNVNANERSRLGGVSFMWKDIMQKHNEIGGFHAQLCLGGQIYADRMWKEIPSLKQWLVIRGKEARRTMPWTAAHEEDVSHAYFHYYTSHFDQPYLRESFAQIPYVCQVDDHDIFDGYGSYPEHMQFSNMFKNIGRVGTEMYLLFQHHTTLELLHNASTDVDLFTITGTGWHFVKFLGPAVVVVGLDCRSERNPHQVVAGPTYQGIFPKVAMLPPSVQHCLWMISVPVIYPRLETAEHIANTVASGKRAVTGAYNVLGKVTSSVAGVVGAKEVVGSGFDSVKRAVGKSGLMGGILSPFGEFDLMDELRDQWTHESKDLERTYLIRTLQGIAHQKFLRMTFLSGSVNVCGAGLVHDPAHPSDYKTMYQIISSAVVNNPPPSYVIKLLHSSNKPLYVPANGQRSSPSQPTDTKEDMMEIFQTDVTGQAREHRKLMGRRNYAAIVAYDPETVNAMYGQAPVVHGGRLNLAVDFMVQGDGSYGTVVKYGPVIIPSLGHGK
Protein: beta-fructofuranosidase (EC 3.2.1.26) (A2DMT0)
Organism: Trichomonas vaginalis (strain ATCC PRA-98 / G3)
Interaction partners:
- Ribokinase
- Kinase, pfkB family protein
- Kinase, pfkB family protein
- valine--tRNA ligase
- DNA topoisomerase 2
- Glucose-6-phosphate isomerase
- Aldehyde dehydrogenase
- Glucose-6-phosphate isomerase
- Aldose 1-epimerase
- nicotinamidase
Sequence:
MNFSSRLKFHFEPLKGWMNDPNGLIQFKGEYHAFFQHYPFDTKWGPMHWGHATSKDLIHWEHKPIALYPDQEYENNGGCFSGSAIEFNDKLHIFYTGVGKSNGQSQCHAVMQDENRFIKDPKNPIIKSPPIEYGINDFRDPKVVKIENTFYMVVGTGKDGIGRVLLYKSSNLENWTFLNLLVEGKEYGQCCECPDLIQIDNQFFLMFSQMTGQGIGTLFFHLKYENGTFTVDKKLNQPIIGPDFYAPQTFHDDKGRRIIIGWLYNWKRVPPKEVDYAGAFTIPCELKYKEGKIVVNPIDEISHELKSESKFVEIQENKLIINGKPSVIHEGKIENIKILEDVKTIEVWINNGEFYYSTWLF