wanglab/gogpt-training-data huggingface dataset:
Protein: Chitin-binding type-2 domain-containing protein (Q18529)
Organism: Caenorhabditis elegans
Interaction partners:
- Tyramine beta-hydroxylase
- Peptidase S1 domain-containing protein
- Chitinase-like protein C25A8.4
- FIP
- DUF19 domain-containing protein
- Uncharacterized protein
- DUF148 domain-containing protein
- DUF4362 domain-containing protein
- Uterine Lumin Expressed/locailized
- DUF1525 domain-containing protein
Sequence:
MRQLSIFAAAVILISADAKNVLNPKGPPCPDGDGLYAVGCSSKYLQCVNNVEYEQSCPEGLYFDRLLARCERRSSNHLCATGDRVTLNVRQKAVSINCVGRLSGDYALDKTVCNENYYQCANGISYMRKCPYQQVYVPILKRCDYHTNCNASGGVKDQAAAAYASPTYDSDNYIVTTKEFENGHNGLDCKVTGDMHFTDNVKCSPYFWQCSNGKLFRKTCPEKLIYVLDQNLCDFPESVKDCPEYNGSETSYRAPKTTTSSSSYGSIAEAPVDPTPYAPASAPVYSPPRTTYVPRSTSAAPPNPPPQNPTAAPYVPTEATPSPVFSSTVRYNPAVHGDCKNRDGIFGIKECHASFLSCDNGVGRVIQCADNLVFDTRVSACEFAAICLEPRKPEDVPVLYNHGGAYNERPAEVKVDFDCTGKPNGKYIKEACTKSFFTCHDGRAFANDCPGDLVFNKATGTCDFAENCEKNYMEPSQIYKGEDTPTTTIGYSSSVVYTTTEQPATKPYTQPPRDTERPSTIYGRPIYTKAPTTVGYEQPKATYTTQAPVTTTIALDDFSCKHLADGNHASGLCKSVFYICANGQVVATTCPANLIFNPYVGECDYSTNVRDCQGYQPTTTPSYSYPKTTSKPYEQPSTTQGYAPIEYTPVTPGYAPQYTSTIFTTTLSPKYAAMCAKRDDGNYGFDCEKYLIKCYNRKTFKFPCPSGLYYSRLQDKCDVKENVEGCPEYKPTTDATPAAEQPVISYQNYGYSQSTTKAYNPSVTTPSPQHAAFCERLENGNYGLDCEDYYISCNNFETTINRCPAGLFYSKLNNRCDYKEHVEDCPEYKPTPSTTPAAEQPGTTKYTTYNYPNIDYTSTTPGPVDTTPLAKAFSCSGRPDGIYALPYCSQDYVQCMQGRSLISSCAPGLFYNEKNGMCAYKHTVDTCKIGKGSDIIDSNACFGKSDGYYSAGCSSYYFSCIDEQIRKMSCPNSLKFSKESEKCVFPIDAKECSIATTLDRTPPAVPSDFCTIRSNGLHHLKMCSPHYIVCDNGRAFSGTCIAPLVYNGDTQTCNYKSTNKDCGNDYIPPVAEVTSSYTTYTTKRFEQPAPTTTAAPYQPQTTTTGKVLYKAAYTTTATQYEEPATTPSRDVETPTTTTHKPYETTTEAQDATTTTTASYVAPTTSSAYKSY
Protein: AT08432p (Q8T499)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLLGQQLQAFDYCDPTLCPGPERHIACNNFGALADICSPDAHIVRITTARRTMILNELNEYRDRIARGDLMGFSPATRMATLQWDQELASFAELNVKRCALVNDHCRNSEQFRNVAQVVAEGGWQGDPLPPSSPSDPPNPEAPIPVEYHTEDEVIKATLEQMFAEYKECSMRDIIAFSPPNNSKCIAYFTQLVRDSTTHVGCGILRQTKNTTNEAGQSLSSVHQYMTCNFVRTNDVNAPVYQSGDRPATECRSGRNSVFINLCSVNEIYDSSNLAGLF
Protein: Disintegrin and metalloproteinase domain-containing protein unc-71 (Uncoordinated protein 71) (G5EFD5)
Organism: Caenorhabditis elegans
Function: Involved in the migration of sex myoblasts (progenitors of egg-laying muscles), Q neuroblasts and BDU interneurons during development. Involved in axon branching and guidance of neurons including GABAergic type D motor neurons. Promotes sex myoblast migration and positioning independently of gonad attraction cues. May act downstream of mig-13 in order to promote the guidance, migration and positioning of Q neuroblasts and their descendants along the anteroposterior body axis. Required for coordinated movements.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12783787, ECO:0000305|PubMed:8970152}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MICASKITMLGLLVMCTLGGVLGKVDIRQTTANKAFMETMRADGYEVVHPFQIRDKNERIGIDTRNYFLKAQEHYSHVTIVIRSNQLGRLKLVLERNNFIFLNQTAFHKLDADGERVIQNRVENCYYQGTVGGEESSFVALSSCNGLRGVISFANGTTFGIWPLDGGDRNSRRHPHILYKSEWSQEAKCGSSMAHAVGQRRMKKHVHKHRSHHHEHNKKRDVSKRTKYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSMLSRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDYASGHIYHIQKDASILFTAGSFANQEVSNAAIRSICTARSAVIVKGVEQFATHWNGELLAQSIGHLLGLEHDTTACSCEPSPECVMRQQPGRVGGGGGSPFSWQFSKCSVARMHGIWQDGNIQCLLNKPFQVSELRECGNGVVDGSEECDCGSRENCQDPCCDPLTCTLRPHAQCAAHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPDGHLIDGTVCGTDGQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQNTKGAEYANCGQRQADGTYHPCQIEDTRCGTLHCHSGSITPIDSSLKAFTFHFTENSHQIQCKSIASAAVGLTSDGTNCASGRVCVAGSCVEMSSVSSATACPTNNLALLCSGHGHCTTTARCVCFNGWSGVACDIRSNSSTYQGSMGFGEEGSGGSSQKSSERKTIMIPHLNIGTTLETATLFAILLGFGVFLLLCLVCLMLCYRRRSVVEIPKPSDEKDEESPDRQIKFGNMPSYREEKRKRKSNKKIYGALNRITEADERDSTSLRSRDSAGGSQQLVDRRNGAPVVVGGIRDPYAGEHIYAESSSNHLTRQFRGINSDGSYPLRSFGSWRSSAPISPASSSGQLTDVSTATTPLRLNKIGKFLKTLQSDDESPSPFSDHQSFTTGIGIGARLEQMQFGGGGDEELSAVEADHDVGSNTESSRGCEEPMDPGSWDSPTLVNGASSSSTSNNYNFRQSPSLFSDPFKLEMTNSMHN
Protein: Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme (ATP:glutamine synthetase adenylyltransferase) (ATase) [Includes: Glutamine synthetase adenylyl-L-tyrosine phosphorylase (EC 2.7.7.89) (Adenylyl removase) (AR) (AT-N) (AT-N440) (P-I); Glutamine synthetase adenylyl transferase (EC 2.7.7.42) (Adenylyl transferase) (AT) (AT-C)] (P30870)
Organism: Escherichia coli (strain K12)
Function: Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Interaction partners:
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Glutamine synthetase
- Nitrogen regulatory protein P-II 1
- Inorganic triphosphatase
- Nitrogen regulatory protein GlnK
- Ammonium transporter AmtB
- Sensory histidine kinase/phosphatase NtrB)
- Glutamate decarboxylase alpha
- Glutamate/gamma-aminobutyrate antiporter
- DNA-binding transcriptional regulator NtrC)
Sequence:
MKPLSSPLQQYWQTVVERLPEPLAEESLSAQAKSVLTFSDFVQDSVIAHPEWLTELESQPPQADEWQHYAAWLQEALCNVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLSYLAETLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAWPEHGCTQGGRRELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFAALEDYYQEQGRDWERYAMVKARIMGDSEGVYANELRAMLRPFVFRRYIDFSVIQSLRNMKGMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRSLLPTLSAIAELHLLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPSDELNRARLAWAMDFADWPQLTGALTAHMTNVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQVLTLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLSRITALLVGIVTRTTYLELLSEFPAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQYLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQAWVQMVARYGKPNHLNEREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGEREIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSAEAFADYQKNEAWTWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHRDRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMALTRAYTTLRDELHHLALQELPGHVSEDCFTAERELVRASWQKWLVEE
Protein: D-ribitol-5-phosphate phosphatase (EC 3.1.3.-) (5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase) (EC 3.1.3.104) (Q8A947)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Function: Catalyzes the dephosphorylation of D-ribitol-5-phosphate and D-ribitol-1-phosphate. Is also able to dephosphorylate 5-amino-6-(5-phospho-D-ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- Riboflavin biosynthesis protein RibD
- Riboflavin synthase
Sequence:
MIKNIVFDFGGVIVDIDRDKAVQAFIKLGLADADTRLDKYHQTGIFQELEEGKLSADEFRKQLGDLCGRELTMEETKQAWLGFFNEVDLRKLDYILGLRKSYHVYLLSNTNPFVMSWACSPEFSSEGKPLNDYCDKLYLSYQLGHTKPAPEIFDFMIKDSHVIPSETLFVDDGSSNIHIGKELGFETFQPENGADWRQELTVILNS
Protein: Cold-regulated 413 plasma membrane protein 1 (AtCOR413-PM1) (WCOR413-like protein) (Q9XIM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein COLD-REGULATED 15B, chloroplastic
- Protein EARLY-RESPONSIVE TO DEHYDRATION 7
- At3g20340
Sequence:
MPMKSLRNDHGTLKAMIGSDFNELTIAAKNLATHAFTLTGLGFGTSVLEWVASIAAIYLLVLDRTNWKTNMLTSLLIPYIFFSLPSLIFGIFRGEIGKWIAFVAVVVQLFFPKHAREYLELPVALVLLAVVAPNLIAGTFRDSWIGLAICLGIGCYLLQEHIRASGGFRNAFTKANGISNTVGIICLVVFPVWALIF
Protein: Tribbles homolog 1 (TRB-1) (Q8K4K4)
Organism: Mus musculus (Mouse)
Function: Adapter protein involved in protein degradation by interacting with COP1 ubiquitin ligase. Promotes CEBPA degradation and inhibits its function. Controls macrophage, eosinophil and neutrophil differentiation via the COP1-binding domain. Regulates myeloid cell differentiation by altering the expression of CEBPA in a COP1-dependent manner. Interacts with MAPK kinases and regulates activation of MAP kinases, but has no kinase activity (By similarity).
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 1
- CCAAT/enhancer-binding protein alpha
- RIB43A-like with coiled-coils protein 2
- E3 ubiquitin-protein ligase COP1
Sequence:
MRVGPVRFALSGASQPRGPGLLFPAARGTPAKRLLDTDDAGAVAAKCPRLSECSSPPDYLSPPGSPCSPQPPPSTQGTGGSCVSSPGPSRIADYLLLPLAEREHVSRALCIHTGRELRCKEFPIKHYQDKIRPYIQLPSHSNITGIVEVLLGESKAYVFFEKDFGDMHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIIKGEDDALSDKHGCPAYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHVSPKARCLIRSLLRREPSERLTAPQILLHPWFEYVLEPGYVDSEIGTSDQIVPEYQEDSDISSFFC
Protein: Dynactin subunit 5 (Q9VJQ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Dynactin subunit 4
- Dynactin subunit 6
- Actin-related protein 10, isoform A
- Dynactin subunit 2
- Actin-related protein 1
- CG9893 protein
- F-actin-capping protein subunit beta
- Dynactin subunit 1
- Dynactin subunit 1
- F-actin-capping protein subunit alpha
Sequence:
MEIPDTYYSKDEYVETASGNKVSRHTVLCGSQNIILNGKVIVQSGAIIRGDLANVRTGRYCVIGKNSVIRPPYKQFSKGIAFFPMHVGEHVFVGEGAVVSAATIGSYVYIGKNAIIGRRCVLKDCCVIEDGAVLPPETTVSSYMRYTARGTIEGGQGNPYFVPAAMQDEMINYTKSFYEHFVRAPAPAS
Protein: Embryonal Fyn-associated substrate (SRC-interacting protein) (Signal-integrating protein) (Q64355)
Organism: Mus musculus (Mouse)
Function: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES.
Interaction partners:
Sequence:
MAIATSAQLARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPANRVKLLPAGPAPKPSLCPASPTQPGSSCPTPERGCEEQEVYVIPPPARPCSASGLPARSCSPSSDSIYKVPRGNGMQLTASRDVAEVYDVPPNILRAPSSCPYDSPASFSCPVAPVVPQPPREDEAPYDVPLALKPPAELERDPEWEGGREPGPPLYAAPSNLKRASALLNLYEAPEELLANGESRDADEGIYDVPLLGPEPPSPEPPVASSSTDLDTVAQLPTRSSPPQHRPRLPSTESLSRRPLPALPVSEAPAPSPAPSPAPGRKGSIQDRPLPPPPPCLPGYGGLKPEGDPECREVANDPAGPHNEYEGIPMAEEYDYVHLKGVDTAQGSRPLDKAFPVDPELLERGLAERKEALSPEEPLVLSTGDLQLLHFYAGQCQSHYSALQAAVAALVASTQANQPPCLFVPHGKRVVVAAHRLVFVGDTLGRLAASAALRAQVGAAGTMLAQTLRATVLAVKGAALGYPSDTAVQEMARCVAELAGQALRFTTLLDGLLP
Protein: S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase (EC 4.1.3.44) (tRNA wybutosine-synthesizing protein 1) (O59761)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Interaction partners:
- tRNA wybutosine-synthesizing protein 3
- tRNA wybutosine-synthesizing protein 4
- tRNA wybutosine-synthesizing protein 2
- Translation initiation factor rli1
- Monothiol glutaredoxin-4
- Iron-sulfur assembly protein 1
- tRNA
- tRNA
- Porphobilinogen deaminase
- tRNA
Sequence:
MGYSLGYIGEHWEEYRAVLYIVLLLPVLIHFLIRRKTQLSNSDKSSEKKDEVKKQREVKRFKRVGKRGKIGSPSSSIRKQNDTIDWKNSPLCVFYSTLGGTAERYAKQVHEELSSLLQRDDIQLLNLDYVDLSEYFVSCPENAIYLVVLPSYEIESSIDYYLSSLQESFSDFRVPKDPLHGLSGYAVFGLGDMENYPGDKFCYQAIQADKWIKKLGARRLAPLGVVNTQLAPTAQIDALLQWTRSVAECLKNGTLLKIGNTDSLSSDVMDVEDMGSMMAKAKAEAALPVGTKEMVSTESPTYKALTKQGYSVVGSHSGVKICRWTKSAMRGRGFCYKYSFYGIRSHLCMEATPSLACANKCTFCWRHGTNPVGTSWRWKVDPPEMILQGILKAHYAKLKLMKGVPGVLPDRYEEASRVRHCALSLVGEPIFYPYINEFVSMLHEREISSFLVTNAQHPEALRNMGMVTQLYVSVDASTKQSLKSVDRPLFKDFWERMLTCLEILREKRQRTVYRMTLVKGFNMEQIKEYTELIRLGVPCFIEVKGVTYSGNSDQSPLTMKNVPYYEEVIDFVKKLIEYIDIHLQDLGVRYEIAAEHAHSCSILVAQTAFKKDGHWHTHIDYPKFFELIRTKKDFGPFDYMASTPDFAMFGNGGFSPEDTRFHRKKKTQTSKPISATISETATISEAAA
Protein: Alpha-adducin (Erythrocyte adducin subunit alpha) (Q9QYC0)
Organism: Mus musculus (Mouse)
Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.
Subcellular location: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Beta-adducin
- Protein 4.1
- Ankyrin-2
- Ankyrin-1
- Dematin
- Ankyrin-3
- Gamma-adducin
- Tropomodulin-4
- Tropomodulin-1
- Tropomodulin-3
Sequence:
MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTASVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTNLGVNQAGFTLHSAVYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGDVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLDPGKYKAKSRSPGTPAGEGSGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALRERSKKYSDVEVPASVTGHSFASDGDSGTCSPLRHSFQKQQREKTRWLHSGRGDDASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVMMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEEDLPQEPTSRDDSDATTFKPTPPDLSPDEPSEALAFPAVEEEAHASPDPTQPPAEADPEPASAPTPGAEEVASPATEEGSPMDPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS
Protein: Lamin-B1 (P70615)
Organism: Rattus norvegicus (Rat)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Subcellular location: Nucleus lamina {ECO:0000250|UniProtKB:P14733}.
Interaction partners:
- Delta
- Prelamin-A/C
- Lamin B2
- Emerin
- Barrier-to-autointegration factor
- Caspase-6
- Granzyme B
- Barrier-to-autointegration factor-like protein
- Lamina-associated polypeptide 2, isoform beta
- Actin, cytoplasmic 1
Sequence:
MATATPVQQRAGSRASAPATPFSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSARGGMMESRMRIESLSSQLSNLQKDSRACLERIQELEDMLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVVLKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVPLEEERFHQQGTPRASNKSCAIM
Protein: Oxygen-insensitive NAD(P)H nitroreductase (EC 1.-.-.-) (Dihydropteridine reductase) (EC 1.5.1.34) (FMN-dependent nitroreductase) (P38489)
Organism: Escherichia coli (strain K12)
Function: Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.
Interaction partners:
- Oxygen-insensitive NADPH nitroreductase
- N-ethylmaleimide reductase
- FMN-dependent NADH:quinone oxidoreductase
- Uncharacterized protein YbdF
- Thymidine kinase
- Uncharacterized NAD
- NADPH:quinone oxidoreductase MdaB
- Protein RecA
Sequence:
MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV
Protein: Growth-regulating factor 4 (AtGRF4) (Transcription activator GRF4) (Q8L8A7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU01002}.
Interaction partners:
- GRF1-interacting factor 1
- GRF1-interacting factor 2
- Transmembrane protein
- Calcium-binding EF-hand family protein
- Pathogenesis-related thaumatin superfamily protein
- Ribonucleoside-diphosphate reductase small chain C
- Ribonucleoside-diphosphate reductase small chain A
- Putative ribonucleoside-diphosphate reductase small chain B
Sequence:
MDLQLKQWRSQQQNESEEQGSAATKISNFFFDQIQSQTATSAAAAPLPLFVPEPTSSSSFSCFSPDSSNSSSSSRFLKMGNFFSWAQWQELELQALIYRYMLAGASVPQELLLPIKKSLLHQSPMHFLHHPLQHSFPHHQPSWYWGRGAMDPEPGRCKRTDGKKWRCSRDVVAGHKYCDRHIHRGRNRSRKPVETATTTITTTATTTASSFVLGEELGHGPNNNHFFSSGSSQPLHLSHQQSCSSEMKQESNNNKRPYEANSGFSNGRSDDGHILRHFFDDWPRSSDSTSSPMSSSTCHLSISMPGNNTSSDVSLKLSTGNEEEEENMRNNNNEREQMNWWSNGGNHHNNMGGPLAEALRSASSTSSVLHQMGISTQVFH
Protein: ATP synthase peripheral stalk subunit b, mitochondrial (ATP synthase F(0) complex subunit B1, mitochondrial) (ATP synthase peripheral stalk-membrane subunit b) (ATP synthase subunit b) (ATPase subunit b) (P13619)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MLSRVVLSAAAAAAPSLKNAALLGPGVLQATRIFHTGQPSLAPVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSAISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKRVVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM
Protein: 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5) (Q7ZU69)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 3
- Proteasome 26S subunit, ATPase 3
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 12
- Proteasome 26S subunit, non-ATPase 6.
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome 26S subunit, non-ATPase 14.
Sequence:
MKDVLGFLKQQQSQSPTPEIAAEWHSLEDFYNRKLWHQLTLKLTVFVQDPYFAKGDGLIQLYENFLCDFEHRINPLSLVEIILHVARQMQDPNTAITFLEKTKEKVKASDEAVILCKTSIGSLKLDISDLPATKKLIEEVEEMLNNLPGVTSVHGRFYDLSSKYYRIIGNHALYYKDALRYLGCVEAKDLPEAEQQERAFTLGLAGLLGEGVYNFGELLMHPVLESLRNTDKQWLIDTLFAFNAGNVEKFQALKTAWGQQPDLAAQEAKLMQKIQLLCVMEMTFTRPANNRQLSFQEIAQSAKIQVNEVELLVMKALSVGLIKGSIDEVEKKVHMTWVQPRVLDVQQIKGMKDRLDFWCGDVKNMAVLVEQRAQDILT
Protein: ORF4 polyprotein (Q27YG7)
Organism: Nora virus
Function: ORF4 polyprotein codes for VP4a, VP4b, and VP4c, three of the four proteins that self-assemble to form the icosahedral capsid. The capsid is made of VP3 (coded by ORF3), VP4a, VP4b and VP4c.
Subcellular location: Virion {ECO:0000305|PubMed:27298753}.
Interaction partners:
Sequence:
MQNPTQTMHIYDMPLRVIAGLSTLAKTTEEDDNTSTGIVVSEVGEPQVVNHPAWIDPFVAYQLRAPRKNITPDFIFGRADIGNAFSAFLPRRFSAPAVGTRLVVDPVFTYQQRTVLGLYNYFHADFYYIVHVPAPLGTGIYLKIYAPEFDTTTVTRGIRFKPSASPTIALSVPWSNDLSTVETSVGRVGQSGGSIVIETIEDNSNETVNTPLSITVWCCMANIKATGYRHADTSAYNEKGMNFISVPVPKPPVPPTKPITGEEQADNEVTAEGGKLVQELVYDHSAIPVAPVVETQAEQPEVPVSLVATRKNDTGHLATKWYDFAKISLSNPANMNWTTLTIDPYNNVTLSRDGESMVLPWRRNVWTTGSKSIGYIRTMVAQINIPRPPQISGVLEVKDSINNSSISLVEFGGKVEIPIIPKVMNGLATTASLPRHRLNPWMRTAESKVELQYRIIAFNRTSDIADLNVSVLLRPGDSQFQLPMKPDNNVDTRHFELVEALMYHYDSLRIRGEEQSLPENAPNAVSNPQQFITPATALSAEEYNVHEALGETEELELDEFPVLVFKGNVPVDSVTSIPLDLATIYDFAWDGEQNAISQKFQRFAHLIPKSAGGFGPVIGNYTITANLPTGVAGRILHNCLPGDCVDLAVSRIFGLKSLLGVAGTAVSAIGGPLLNGLVNTAAPILSGAAHAIGGNVVGGLADAVIDIGSNLLTPKEKEQPSANSSAISGDIPISRFVEMLKYVKENYQDNPVFPTLLVEPQNFISNAMTALKTIPIEVFANMRNVKVERNLFDRTVVPTVKEATLADIVIPNHMYGYILRDFLQNKRAFQSGTKQNVYFQQFLTVLSQRNIRTHITLNDITSCSIDSESIANKIERVKHYLSTNSSGETTEEFSRTDTGLLPTTTRKIVLGESKRRTERYVAETVFPSVRQ
Protein: Nudix hydrolase DR_0079 (EC 3.6.1.-) (Q9RY71)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: Hydrolase that converts various nucleotide triphosphates (NTPs) to the corresponding nucleotide monophosphates and diphosphate, and nucleotide diphosphates to nucleotide monophosphates and inorganic phosphate. Has a marked preference for cytosine ribonucleoside 5'-diphosphate (CDP) and cytosine ribonucleoside 5'-triphosphate (CTP). Has lower activity towards the deoxyribose nucleotides dCDP and dCTP, and towards dGDP, TDP and UDP.
Interaction partners:
- N-acetyl-gamma-glutamyl-phosphate reductase
- Shikimate 5-dehydrogenase, putative
- Ornithine carbamoyltransferase
- MutT/nudix family protein
Sequence:
MGGVSDERLDLVNERDEVVGQILRTDPALRWERVRVVNAFLRNSQGQLWIPRRSPSKSLFPNALDVSVGGAVQSGETYEEAFRREAREELNVEIDALSWRPLASFSPFQTTLSSFMCVYELRSDATPIFNPNDISGGEWLTPEHLLARIAAGEAAKGDLAELVRRCYREEE
Protein: DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (C82) (DNA-directed III 74 kDa polypeptide) (C74) (P32349)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC7
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I and III subunit RPAC2
Sequence:
MDELLGEALSAENQTGESTVESEKLVTPEDVMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVALGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQETAISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEEEHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSLFVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNSPLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTSLRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQVYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAELVEEKTPGLTFNAIDLARHLPAELDLRGSLLSRKPSDNKKRSGSNAAASLPSKKLKTEDGFVIPALPAAVSKSLQESGDTQEEDEEEEDLDADTEDPHSASLINSHLKILASSNFPFLNETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRLSRCIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVEIQEVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMANLLFKKEKLKQENSTLLKKANRDDVKGRENELLLPSELNQLKMVNERELNVFARLSRLLSLWEVFQMA