wanglab/gogpt-training-data huggingface dataset:
Protein: Thyroid hormone receptor interactor 11 (E9Q512)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
- Intraflagellar transport protein 20 homolog
- ADP-ribosylation factor 1
- Golgin subfamily A member 5
- Aryl hydrocarbon receptor nuclear translocator
- Golgin B1
- Golgin subfamily A member 3
- GRIP and coiled-coil domain-containing protein 2
Sequence:
MSSWLGGLGSGLGQSLGQVGGSLASLTGQISNFTKDMLLEGTEDVPADFPNSGREENEATHSVLRSENERLKKLYTDLEEKHEASELQIKQQSSSYRSQLQQKEEEINHLKARQLALQDELLRLQSAAQSAHLGSGSAPAASASSSFSYGVSHRVSAFHEDDMDFGDVISSQQEINRLSNEVSRLESELGHWRHIAQTKVQGAQSSDQTEICKLQNIIKELKQNRSQDLDDHQHELSALQNAHQQKLTEISRRHREELSDYEERIEELENLLQQGGSGVTVTDHSKVYEMQNTIQILQMEKVESTKQIEDLENKIKEIHKRLSSAEHDQEVWKKEQERLEVEKREMTEQCERLKLELSEAQQSALRQSDAAVEEETILPHSSSVAEVLRLQQALTDAENEIMRLRSLNQDISLAEDNQKLQMCVQTLEKEKSLLSQEKEELQISLSKLSSEYEVIKSTATRDLDLFSQVHDLKHNLEAKEQELNQSIHENEILMAELEELDKQNQEATKHVILIKDQLSKQQSEGDSVIKKLKEELAGEKQRTHQLEDDKMNIIKELTVQKEKLTHSEQALSDLQLTKQKLEDKVEDLVDQLSKSEKNNFDIQKENHELREHIRQNEEELSTVRSELTQSQTQGSSRNVKDDLLKERETQVQNLKQNLSEVEQLNEHLEQVAFDLRTENEELLEAYEEVRNQLEESVAGNKQISLEKTAMLEWEKAPLETELCRAEKRVLEEERKYEQTVQELSSACSPDTSALQLEQERLIQLNQEKDFEIAELKKSIEQMDTDHKRTKETLSSSLEEQKQLTQLINEKEICIVKLKEKSSELQKELDKCAQTLRKNETLRQTIEEKDRSLGSMKEENNHLQEELERLREQQSRVVPAPEPRTLDSTTELESELSQLHRIKGHLEEEIKHHQKMIEDQNQSKLQLLQSLQEQKKELDEFKYQHEQMSISHTRLFLEKDEEIKNLQKTIEQIKAQLHEERQDSQTENSDIFQETKVQSLSIEHGSEKHDLSKAETERLVKGIKERELEIKLLNEKNTSLTKQIDQLSKDEVGKLTQIIQQKDLEIQALHARISSASYSQDVVYLQQQLHAYAMEREKVMVILNEKTRENSQLKTEYHKVIDIISAKEAALIKLQDENKKMSTRFESSGQDMFKETIQNLSRIIREKDIEIDALSQKCQTLLTVLQTSGTGSEAGGVNSNQFEELLQERDKLKQQVKKMEEWKQQVMTTVQNMQHESAQLQEELHQLQAQVSVDSDNNSKLQVDYTGLIQSYEQNETKLKNFGQELAQVQHSIGQLCNTKDLLLGKLDIMSPQLSSGSSLTSQAAEPLRASQSSEPHESSQLLQQEVDDLRKSLQEKDATIRTLQENNHRLSDSVAASSEVERKEHEQADSEIKQLKEKQEVLQNLLKEKDLLIKAKSDQLHSSNENLANKVNENELLRQAVTNLKERILILEMDISKLKGENEKIVDASKGKETEYQALQETNMKFSMMLREKEFECHSMREKALAFEQLLKEKEQGKAGELNQLLNAVKSMQEKTVTFQQERDQVMLALKQKQMETSTLQNEVQRLRDKESRLNQELQRLRDHLLESEDSHTREALAAEDREAKLRKKVSVLEEKLVSSSNAMENASHQASVQVESLQEQLNMVSKQRDETALQLSVSQEQVKQYALSLANLQMVLEHFQQEEKAMYSAELEKQNHLLAEWKKKAESLEGKVLSLQERLDEANAALDSASRLTEQLDLKEEQIEELKKQNELHQEMLDDAQKKLMSLVNSTEGKVDKVLMRNLFIGHFHTPKHQRHEVLRLMGSILGVKREEMEQLFAEDQGGVTRWMAGWLGGGSKSVPNTPLRPNQQSVFNSSFSELFVKFLETESHPSVPPPKLSVHGLKPLDSPGRRKADTGIPESFRDTAESRAGRRTDVNPFLAPRSAAVPLINPAGHGPGGPGHLLLKPISDVLPTFTPLPVSPDNSAGVVLKDLLKQ
Protein: Nitrogen regulatory protein P-II (Q53044)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Interaction partners:
- Ammonium transporter
- Rh-like protein/ammonium transporter
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- histidine kinase
- Glutamine synthetase
- Acetylglutamate kinase
- Nitrogenase iron protein
- L-glutamine synthetase
- L-glutamine synthetase
- ADP-ribosyl-
Sequence:
MKKIEAIIKPFKLDEVKEALHEIGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKIELVIEDALVERAIEAIQQAAQTGRIGDGKIFVYAIEEAIRIRTGERGGDAI
Protein: Phthioceranic/hydroxyphthioceranic acid synthase (EC 2.3.1.287) (Polyketide synthase pks2) (P9WQE9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in sulfolipid-1 biosynthesis. Catalyzes the synthesis of the hepta- and octamethyl phthioceranic and hydroxyphthioceranic acids, the methyl-branched acyl constituents of sulfolipids.
Interaction partners:
- Probable fatty acid synthase Fas
- 2'-acyl-2-O-sulfo-trehalose
- Phenyloxazoline synthase MbtB
- Malonyl CoA-acyl carrier protein transacylase
- Mycoketide-CoA synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Mycocerosic acid synthase-like polyketide synthase
- Isonitrile lipopeptide synthase
- NADH-quinone oxidoreductase subunit I
Sequence:
MGLGSAASGTGADRGAWTLAEPRVTPVAVIGMACRLPGGIDSPELLWKALLRGDDLITEVPPDRWDCDEFYDPQPGVPGRTVCKWGGFLDNPADFDCEFFGIGEREAIAIDPQQRLLLETSWEAMEHAGLTQQTLAGSATGVFAGVTHGDYTMVAADAKQLEEPYGYLGNSFSMASGRVAYAMRLHGPAITVDTACSSGLTAVHMACRSLHEGESDVALAGGVALMLEPRKAAAGSALGMLSPTGRCRAFDVAADGFVSGEGCAVVVLKRLPDALADGDRILAVIRGTSANQDGHTVNIATPSQPAQVAAYRAALAAGGVDAATVGMVEAHGPGTPIGDPIEYASVSEVYGVDGPCALASVKTNFGHTQSTAGVLGLIKVVLALKHGVVPRNLHFTRLPDEIAGITTNLFVPEVTTPWPTNGRQVPRRAAVSSYGFSGTNVHAVVEQAPQTEAQPHAASTPPTGTPALFTLSASSADALRQTAQRLTDWIQQHADSLVLSDLAYTLARRRTHRSVRTAVIASSVDELIAGLGEVADGDTVYQPAVGQDDRGPVWLFSGQGSQWAAMGADLLTNESVFAATVAELEPLIAAESGFSVTEAMTAPETVTGIDRVQPTIFAMQVALAATMAAYGVRPGAVIGHSMGESAAAVVAGVLSAEDGVRVICRRSKLMATIAGSAAMASVELPALAVQSELTALGIDDVVVAVVTAPQSTVIAGGTESVRKLVDIWERRDVLARAVAVDVASHSPQVDPILDELIAALADLNPKAPEIPYYSATLFDPREAPACDARYWADNLRHTVRFSAAVRSALDDGYRVFAELSPHPLLTHAVDQIAGSVGMPVAALAGMRREQPLPLGLRRLLTDLHNAGAAVDFSVLCPQGRLVDAPLPAWSHRFLFYDREGVDNRSPGGSTVAVHPLLGAHVRLPEEPERHAWQADVGTATLPWLGDHRIHNVAALPGAAYCEMALSAARAVLGEQSEVRDMRFEAMLLLDDQTPVSTVATVTSPGVVDFAVEALQEGVGHHLRRASAVLQQVSGECEPPAYDMASLLEAHPCRVDGEDLRRQFDKHGVQYGPAFTGLAVAYVAEDATATMLAEVALPGSIRSQQGLYAIHPALLDACFQSVGAHPDSQSVGSGLLVPLGVRRVRAYAPVRTARYCYTRVTKVELVGVEADIDVLDAHGTVLLAVCGLRIGTGVSERDKHNRVLNERLLTIEWHQRELPEMDPSGAGKWLLISDCAASDVTATRLADAFREHSAACTTMRWPLHDDQLAAADQLRDQVGSDEFSGVVVLTGSNTGTPHQGSADRGAEYVRRLVGIARELSDLPGAVPRMYVVTRGAQRVLADDCVNLEQGGLRGLLRTIGAEHPHLRATQIDVDEQTGVEQLARQLLATSEEDETAWRDNEWYVARLCPTPLRPQERRTIVADHQQSGMRLQIRTPGDMQTIELAAFHRVPPGPGQIEVAVRASSVNFADVLIAFGRYPSFEGHLPQLGTDFAGVVTAVGPGVTDHKVGDHVGGMSPNGCWGTFVTCDARLAATLPPGLGDAQAAAVTTAHATAWYGLHELARIRAGDTVLIHSGTGGVGQAAIAIARAAGAEIFATAGTPQRRELLRNMGIEHVYDSRSIEFAEQIRRDTNGRGVDVVLNSVTGAAQLAGLKLLAFRGRFVEIGKRDIYGDTKLGLFPFRRNLSFYAVDLGLLSATHPEELRDLLGTVYRLTAAGELPMPQSTHYPLVEAATAIRVMGNAEHTGKLVLHIPQTGKSLVTLPPEQAQVFRPDGSYIITGGLGGLGLFLAEKMAAAGCGRIVLNSRTQPTQKMRETIEAIAAMGSEVVVECGDIAQPGTAERLVATAVATGLPVRGVLHAAAVVEDATLANITDELLARDWAPKVHGAWELHEATSGQPLDWFCLFSSAAALTGSPGQSAYSAANSWLDAFAHWRQAQGLPATAIAWGAWSDIGQLGWWSASPARASALEESNYTAITPDEGAYAFEALLRHNRVYTGYAPVIGAPWLVAFAERSRFFEVFSSSNGSGTSKFRVELNELPRDEWPARLRQLVAEQVSLILRRTVDPDRPLPEYGLDSLGALELRTRIETETGIRLAPKNVSATVRGLADHLYEQLAPDDAPAAALSSQ
Protein: Serine/threonine-protein kinase shk2 (EC 2.7.11.1) (Q10056)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Forms an activated complex with GTP-bound Ras-like cdc42. Participates in Ras-dependent morphological control and mating response pathways.
Interaction partners:
- Cell division control protein 42 homolog
- Serine/threonine-protein kinase shk1/pak1
- Mitogen-activated protein kinase spm1
- Probable Rho-type GTPase-activating protein 4
- Probable Rho-type GTPase-activating protein 3
- GTP-binding protein rho2
- GTP-binding protein rho5
Sequence:
MLLSVRGVPVEIPSLKDTKKSKGIIRSGWVMLKEDKMKYLPWTKKWLVLSSNSLSIYKGSKSESAQVTLLLKDIQKVERSKSRTFCFKLRFKSSTKNFEIQACELSVADNMECYEWMDLISSRALASKVSSPMNPKHQVHVGIDNEGNYVGLPKEWILLLQSSSITKQECMEEPKAVIQALDFYSKQLDTTSETKDSFSFCKETLPRSSTTSYSIRDADKHHKLTTSGVTKMNITERCKPKTTIQTDKKHIIRPFIEDKSHVESIMTGKVTKVPVKADSKNTLSRRMTDRQALAMLKDSVTSHDPVEYFNVKHKLGQGASGSVYLAKVVGGKQLGIFDSVAIKSIDLQCQTRKELILNEITVMRESIHPNIVTYLDSFLVRERHLWVVMEYMNAGSLTDIIEKSKLTEAQIARICLETCKGIQHLHARNIIHRDIKSDNVLLDNSGNIKITDFGFCARLSNRTNKRVTMVGTPYWMAPEVVKQNEYGTKVDIWSLGIMIIEMIENEPPYLREDPIRALYLIAKNGTPTLKKPNLVSKNLKSFLNSCLTIDTIFRATAAELLTHSFLNQACPTEDLKSIIFSRKANTHIN
Protein: LD45290p (Q86NY7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
STTNCDHSVHAVCSMLDSNNSSPIGSPNPDAGKRLGFRRQAIQEIISSEKSYLEQLELLMNFFVRPLKEQAIIDCSNHTLLFGQIEMIHNLNGEFLRELEANMENVAHAFLKMAPFFKLYSVYAFDYRGALFIIQDLISKNPVFRKFLEQTESRPEVQRKLNSLMIVPIQRVPRYKLLLEQVLLYTSPADADYKLLKESVKEIEATASHINTCVEEQEITQYLIHLQNSLVNRTPNIVKPSRRVIKEGVLQKITHKGTEIKRYCVLMSDIFMYCKMIKERAPNTVVENSLECCCIFPLKKCKVYEMLPGNFKLTCQSDGIIFGSGDVQLSRTWVGFIRDAIDLHVQCRKTLRKDSSKRTPIRKKDMKKFGADYVLSPNKRKCEYDTVFRNKNRSTDSEEETEDSACFSRKRKVASGILRAPNGNPMGKASSSSSSSVSMKRVAPPPPAPPPPPAVQMRHQPGRPGELATASKENRISKLYKKIAAGDKVANVRGILKRSNVPAPNNDHDPSYGFASRYSDSKSYFRAHNVDNTIPTFVKREDLFNGDNMFPVHLKSHEEICTPPQKKRVKFDDTLDAVSPVLVEKPFAFSSESSSALKPTSLRERIYDFFANLF
Protein: DNA-directed RNA polymerase III subunit rpc3 (RNA polymerase III subunit C3) (RNA polymerase III subunit C82) (Q9C106)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-directed RNA polymerase III subunit rpc4
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit rpc5
- Probable DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerase III subunit rpc8
- DNA-directed RNA polymerase III subunit rpc31
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MSQYAVELCEILVEEFFGDCCSAVASALLRHGRLTIPMLQKRTSLPGPKIRQALVSLMQHHMVLYVTVIENVREVTYYETQWKEIYNILRKGKDVYLISQKLNQEAASVVKYLSTQGRARVLEVFNAFDKKVDGSDEESRMMQKNLTELIYQKFLLVVQPRHLIPVGDQEMQLRIKHLDRRKSENVSEIKKNREVDDSVALEMLELRAADMSELQGLTRKPKESIPHPTKRRKRAVGSAPSVSTDLNNILDDDNSILVPDLSAHVRINSGKLSVLSKNARLTHWVERRIGKSTSLVYSHVLSMLEPRLFSISNQSPVFTLTTMELTRNFPNDIDVESSIVDKQYSVNSASNELRVMEKLNELDELAEEDNYEESVDENANRKSKVLAQHLELLADCSLKFISKIGNRGMGEWAVNFTHLTDMLRAIEYENFIEQKFGERAIRLLRIIKDKGKIEEKQLANIALLRQRDLRTVLQAMAEIGALELQEVPRSSDRAPSKTFFLWFHRPDRAYSLLLDELYHVIARLYMRLRDARAQRAQLIEKAERIDIKGNEEQYLQKFEQAELKKLYSYEEKLLLQASRLDDMVLVFRDNL
Protein: F-box protein FBW2 (SKP1-interacting partner 18) (Q9ZPE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP40
- C3H4 type zinc finger protein
- Putative E3 ubiquitin-protein ligase XBAT31
- Protein argonaute 1
Sequence:
MEEDCEFRHWDELIPDALGLIFSHLPLQEVLTVVPRVCKAWNRAVTGPYCWQEIDIELWSNRFHQSDHLDRMLEMLIPRSAGSLRKLSVTGLRNDSIFSFIAQHAGSLKTLKVPRSGLTNSGVVNVAEKLSSLTFLDLSYCCKIGPEAIQAIGKHCKSLREFCRNMHPLDVASVVSHDDEAYAIANTMPKLKRLEIAYHRVSTEGVLKILSCCVFLEFLELRGCWDVQLDNKFFKEKFPDMKVLGPRVIGFYDMINDWEDCCSDYFSDGSDYLAWEFFEDGVMGEFYEDEFEHGWDDNFYAENAVLDMEPHIWPPSP
Protein: Replication-associated protein G2P (Rep) (EC 3.1.21.-) (EC 6.5.1.1) (G2P) (Gene 2 protein) (P69545)
Organism: Enterobacteria phage fd (Bacteriophage fd)
Function: Isoform G2P plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates at the 3'-OH of the cleavage site. After one round of rolling circle synthesis, protein G2P is linked to the newly synthesized ssDNA and joins the ends of the displaced strand to generate a circular single-stranded molecule ready to be packed into a virion.
Interaction partners:
Sequence:
MIDMLVLRLPFIDSLVCSRLSGNDLIAFVDLSKIATLSGMNLSARTVEYHIDGDLTVSGLSHPFESLPTHYSGIAFKIYEGSKNFYPCVEIKASPAKVLQGHNVFGTTDLALCSEALLLNFANSLPCLYDLLDVNATTISRIDATFSARAPNENIAKQVIDHLRNVSNGQTKSTRSQNWESTVTWNETSRHRTLVAYLKHVELQHQIQQLSSKPSAKMTSYQKEQLKVLSNPDLLEFASGLVRFEARIETRYLKSFGLPLNLFDAIRFASDYNRQGKDLIFDLWSFSFSELFKAFEGDSMNIYDDSAVLDAIQSKHFTITPSGKTSFAKASRYFGFYRRLVNEGYDSVALTMPRNSFWRYVSALVECGIPKSQLMNLSTCNNVVPLVRFINVDFSSQRPDWYNEPVLKIA
Protein: Homeobox-leucine zipper protein ATHB-12 (HD-ZIP protein ATHB-12) (Homeodomain transcription factor ATHB-12) (Q9M276)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription activator that may act as growth regulators in response to water deficit.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:15369784}.
Interaction partners:
- NAC domain-containing protein 72
- Homeobox-leucine zipper protein ATHB-8
Sequence:
MEEGDFFNCCFSEISSGMTMNKKKMKKSNNQKRFSEEQIKSLELIFESETRLEPRKKVQVARELGLQPRQVAIWFQNKRARWKTKQLEKEYNTLRANYNNLASQFEIMKKEKQSLVSELQRLNEEMQRPKEEKHHECCGDQGLALSSSTESHNGKSEPEGRLDQGSVLCNDGDYNNNIKTEYFGFEEETDHELMNIVEKADDSCLTSSENWGGFNSDSLLDQSSSNYPNWWEFWS
Protein: Uncharacterized protein C17H9.07 (O13804)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit srp68
- Signal recognition particle subunit srp14
- Signal recognition particle sec65 subunit
- Signal recognition particle subunit srp72
- Signal recognition particle receptor subunit alpha homolog
- Large ribosomal subunit protein eL31
- Signal recognition particle receptor subunit beta
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein eL14
Sequence:
MVYLQTVNEFFTQSKSLTEAYPKTTKLSIKYRTNEQSQNYLIAKAFESASGICLKYRTDKAAELGRLLLIANKLSYVSTGNEIPPEPEQEVVASPVTEQKKAEPSAPPKGSKKKKRGKKK
Protein: Kinesin light chain 3 (Kinesin light chain KLCt) (Q68G30)
Organism: Rattus norvegicus (Rat)
Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Plays a role during spermiogenesis in the development of the sperm tail midpiece and in the normal function of spermatozoa (By similarity). May play a role in the formation of the mitochondrial sheath formation in the developing spermatid midpiece (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:11319135, ECO:0000305|PubMed:12594206, ECO:0000305|PubMed:15464570}. Mitochondrion {ECO:0000269|PubMed:12594206, ECO:0000269|PubMed:15464570}. Note=In elongating spermatid tail midpiece, localized in outer dense fibers (ODFs) and associates with mitochondria (PubMed:12594206, PubMed:15464570). Also localizes to the manchette in elongating spermatids (By similarity). {ECO:0000250|UniProtKB:Q91W40, ECO:0000269|PubMed:12594206, ECO:0000269|PubMed:15464570}.
Interaction partners:
- Kinesin-1 heavy chain
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Kinesin light chain
- Kinesin light chain 1
- Kinesin light chain 4
- C-Jun-amino-terminal kinase-interacting protein 3
- Glycogen synthase kinase-3 beta
- Neurofilament light polypeptide
- Alpha-synuclein
Sequence:
MSVQVAAPGSTGLGPERLNPEELVRQTRQVVQGLEALRAEHHSLAGHLAEALAGPGPVAGVELLEEKQQVVNHSLEAIELGLGEAQVLLALSAHVGVLEAEKQRLRAQARRLAQENTWLREELEETQRRLRASEEAVAQLEEEKSHLQFLGQLRQYDPPEESQRPDSPPRRDSLASLFPSEEEEKKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFQDVERHYARALSIYEALGGPQDPNVAKTKNNLASAYLKQNKYQQAEELYKEILSQEALPAPLGAPQGGTAGEAQQQVLRRSSSFSKLRESIRRGSEKLVSRLRGESMAGAAGMKRAMSLNMLNVDGPRAARMQLSTQHLNEASRTLSASTQDLSPR
Protein: Guanylate cyclase soluble subunit alpha-1 (EC 4.6.1.2) (Soluble guanylate cyclase large subunit) (E7EZW5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Guanylate cyclase soluble subunit beta-1
- guanylate cyclase
- cGMP-dependent protein kinase
- cGMP-dependent protein kinase
- Si:dkey-121j17.5.
- cGMP-dependent protein kinase
- Inosine triphosphate pyrophosphatase
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- Bis
- Molybdenum cofactor biosynthesis protein 1
Sequence:
MFCAKLKDLKIAGECPFSMVLGNEEPADFEGSNAVNVVPVSREVQGNITNILPRRKISRSKVNLHSLGESVRKLVCPEFEKLRNALIRVIKQQIDTSCPVACSSDVSHTLDNAEQLSDVMKNYSLKTGIPMDALKISLGLEVFRDCYEEDGHILRVVGGALHDFLNSFNVLLKQSTPPTPEIQRYIHQASILCLDKDPGLLTVYFFNPLPSTELFFSGIIQAAACLLYCTRVEVRMDVGGKDSGALQADHQPHLLYSVVVRDGRSLTPSPMRTHTSGDIPLSLLYSTFPFHILLDQEMGLLQIGDGLRRRLGRCRDGQRRPAFNEHFAIVSPEIRASFQDILTMLNTQFLLRVKQHGASSADSPGKHMDLKGQMIFMSEMSALLFLGSPCVDKLEELTGRGLYLSDIPIHNALRDVVLVGEQTKAQDGLKKRLGKAKAALEQAHQALEEEKRRTVELLFTIFPGNVAQRLWQGLPVQAKKFDHVTVLFSDIVGFTAICSRCTPMQVVNMLSELYTRFDHHCGELDVYKVETIGDAYCVAGGLHKESPTHAVQIALMALKMMELSDEVTTPMGEVIRMRIGIHSGSVLAGVVGVKMPRYCLFGNNVTLANKFESCSLPRKINVSPTTYRLLKDCPEFTLIPRTREDLPPNFPTDIPGVCYFLQAHDQKTNAAPEETQPSG
Protein: Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase 1) (CANP 1) (Calpain mu-type) (Calpain-1 large subunit) (Cell proliferation-inducing gene 30 protein) (Micromolar-calpain) (muCANP) (P07384)
Organism: Homo sapiens (Human)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409'. Cleaves and activates caspase-7 (CASP7).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:8769305}. Cell membrane {ECO:0000269|PubMed:8769305}. Note=Translocates to the plasma membrane upon Ca(2+) binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719). {ECO:0000269|PubMed:21531719}.
Interaction partners:
- Calpain small subunit 1
- Calpastatin
- Calpain-2 catalytic subunit
- Cyclin-dependent kinase 5 activator 1
- Bcl-2 homologous antagonist/killer
- Cellular tumor antigen p53
- Calpain small subunit 2
- BH3-interacting domain death agonist
- Interleukin-1 alpha
- Apoptosis regulator BAX
Sequence:
MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
Protein: Mediator of RNA polymerase II transcription subunit 27 (Cofactor required for Sp1 transcriptional activation subunit 8) (Mediator complex subunit 27) (A0A8I6A9B1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADVLSVGVNLEAFSQAISAIQALRSSVSRVFDCLKDGMRNKETLEGREKAFIAHFQDNLHSVNRDLNELERLSNLVGKPSENHPLHNSGLLSLDPVQDKTPLYSQLLQAYKWSNKLQYHAGLASGLLNQQSLKRSANQMGVSAKRRPKAQPTTLVLPPQ
Protein: L-lysine N6-monooxygenase (EC 1.14.13.59) (Lysine 6-N-hydroxylase) (Lysine N6-hydroxylase) (Lysine-N-oxygenase) (P11295)
Organism: Escherichia coli
Function: Flavoprotein monooxygenase required for N-hydroxylation of lysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced by the organism under iron-stressed conditions.
Subcellular location: Cytoplasm. Cell membrane {ECO:0000305}.
Interaction partners:
Sequence:
MKKSVDFIGVGTGPFNLSIAALSHQIEELDCLFFDEHPHFSWHPGMLVPDCHMQTVFLKDLVSAVAPTNPYSFVNYLVKHKKFYRFLTSRLRTVSREEFSDYLRWAAEDMNNLYFSHTVENIDFDKKRRLFLVQTSQGEYFARNICLGTGKQPYLPPCVKHMTQSCFHASEMNLRRPDLSGKRITVVGGGQSGADLFLNALRGEWGEAAEINWVSRRNNFNALDEAAFADEYFTPEYISGFSGLEEDIRHQLLDEQKMTSDGITADSLLTIYRELYHRFEVLRKPRNIRLLPSRSVTTLESSGPGWKLLMEHHLDQGRESLESDVVIFATGYRSALPQILPSLMPLITMHDKNTFKVRDDFTLEWSGPKENNIFVVNASMQTHGIAEPQLSLMAWRSARILNRVMGRDLFDLSMPPALIQWRSGT
Protein: ABC-type antigen peptide transporter (EC 7.4.2.14) (O02086)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ankyrin repeat and KH domain-containing protein mask-1
- Conserved oligomeric Golgi complex subunit 3
- CTCHY-type domain-containing protein
- Pre-mRNA-splicing factor 38
Sequence:
MHRWINTSLYLYMLIDAAITNVSFGYFAPGWKFNYDSFLGIITFSLPYHFTTTPYEFQIFSFIRQSFCAIAVLLIILNKREKVKVLFPVVICNAVVVYSLSLIKFLAFSEDSNQLYFPGLWFSVIWSILSGFIQVLVWYFVFTSNPFDYHRLLNTTAENAGTSVTETAAETVRDTETASNVESGSSTAPRAPLHKVLLRLLSYCGHQWPWFASGFVFLTVYALARVFIPNYTAQVISDIVNKRGIQALIHSIIVLTCLTATSSLFGGLRGGCFDYATALVTLRIRLDLFTSLIRQDIAFYDTAKTGDTMSRLTSDCQTISSTVSTNVNVFMRNGVMLIGALAFMILMSWRLAMVTFIAVPLVGFITKAYSSFYDKISEKLQQTIAETNQMAEEVVSTMRTVRSFACEKKELKRFEDRLSSTLSVNRKKSIAYLFYTWNNEFCDNAILVAVLFYGGHLVMTGKMEKEQLITFLLYQMQLGENLYYLSYVMSGLMEAVGASRKVFDLMNRKPQFELDGMQRPFVNGNITFSHVGFTYPSRPNNPVLKDLTLSIKSGETVALVGPSGGGKSSIVSLIEHFYEPDEGSVTLDGVPIKDINHVYYHQKVALVAQEPVLYNGSVRHNILYGCDFATEDDMLNASKMANVHDFVMELEKGYDTNCGEKGVQMSGGQKQRIAIARALVRNPAVLILDEATSALDTESEALVQQALSRCAQERTVIIVAHRLSTIEKANKIAVIVKGCLVQMGTHTELMTDTDGMYYSLVSRQMLSAKVGED
Protein: Chromosomal passenger complex protein BIR1 (P47134)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Seems to act in the pleiotropic control of cell division. May participate in chromosome segregation events.
Interaction partners:
- N-terminal-borealin-like protein
- Inner centromere protein SLI15
- Aurora kinase
- Centromere DNA-binding protein complex CBF3 subunit A
- ATP synthase subunit beta, mitochondrial
- Pro-apoptotic serine protease NMA111
- Centromere DNA-binding protein complex CBF3 subunit B
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Metacaspase-1
- Protein ECM5
Sequence:
MDGQIDKMEKRYSMTKLENRLRTFQDGVALEKKKLKWSFKVIPYQAMAKLGFYFDPVIDPKTSKLKKDSVRCCYCHRQTYNVRDCRSKRKDVLETLSNIMRQHLTVTDNKQVCLLIYLRNKLLTDYSFHMGVSDWKNDKYFSNPDDENVINLRKFTFQDNWPHSGSQNEHPLGIEKMVNAGLMRYDSSIEGLGDPSMDKTLMNDTCYCIYCKQLLQGWSINDDPMSRHYKVSQNGNCYFFQTRNRFERIKNDNDSITKNCEVSPTLGENGKREVINTKTASQRQCPLFESPPSSTGPQLDDYNEKTDISVIQHNISVLDGAQGENVKRNSVEEKEQINMENGSTTLEEGNINRDVLADKKEVISTPTAKEIKRPNVQLTQSSSPIKKKRKFKRISPRKIFDEEDSEHSLNNNSANGDNKDKDLVIDFTSHIIKNRDVGRKNAILDDSTDEFSFSNQGHNTFDIPIPTSSHLLKGIDSDNDNVIREDDTGINTDTKGASSKHEKFSVNSEEDLNFSEVKLTGRDSSTNILIRTQIVDQNLGDIDRDKVPNGGSPEVPKTHELIRDNSEKREAQNGEFRHQKDSTVRQSPDILHSNKSGDNSSNITAIPKEEQRRGNSKTSSIPADIHPKPRKNLQEPRSLSISGKVVPTERKLDNINIDLNFSASDFSPSSQSEQSSKSSSVISTPVASPKINLTRSLHAVKELSGLKKETDDGKYFTNKQETIKILEDVSVKNETPNNEMLLFETGTPIASQENKSRKLFDEEFSGKELDIPIDSSTVEIKKVIKPEFEPVPSVARNLVSGTSSYPRNSRLEEQRKETSTSLADNSKKGSSFNEGNNEKEPNAAEWFKIDENRHLVKNYFHDLLKYINNNDATLANDKDGDLAFLIKQMPAEELDMTFNNWVNLKVQSIKREFIDDCDKKLDILRRDYYTATNFIETLEDDNQLIDIAKKMGIL
Protein: DNA replication licensing factor MCM7 (EC 3.6.4.12) (O16297)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365012}.
Interaction partners:
- DNA replication licensing factor mcm-6
- DNA replication licensing factor mcm-4
- DNA replication complex GINS protein SLD5
- DNA replication licensing factor mcm-5
- DNA replication licensing factor MCM2
- CDT1 Geminin-binding domain-containing protein
- Cell division control protein
- DNA replication licensing factor MCM3
- Protein MCM10 homolog
- DNA replication complex GINS protein PSF3
Sequence:
MKTTTYNTDWAAEKTKIRSFFDEYYVDNEDGSGKAFPYRDQVFEIARRDKQAIVVNVDHIKESDIPDALELSEAITSNTKRYEVLFKDTISDMIQDYLGDKQAPVIDALDAYMFQRLHMDRNEGAANEEVSLQDKRKKYPPQLLQRFEVYFTTDDAAHETCVRNIKATEIGHLVSMKGVVIRATEVKPCVEVMTYTCDTCAAEVYQPVKGMQFTPPVNCPNKECVEAKANGRLHMQLRGSKFVKFQELKIQELSEQVPVGSIPRTMTVHVYGEMTRKCNTGNVVHVSGVFLPIMQSGFRPTGGLVADTYLEAHYINNLDDNPTFNGVQSAELEVLRRKGDNYETLAASIAPEIFGHVDVKKCLLMALVGGNDNSSNGMKIRGCINVLMMGDPGVAKSQLLGYVNRLAPRSQYTTGRGSSGVGLTAAVMKDPVTGEMSLEGGALVLADGGICCIDEFDKMMDHDRTAIHEVMEQQTISIAKAGIMTTLNARTAIIAAANPAYGRYNPNRSIEQNVDLPAALLSRFDLILLMQDKADRENDKILAEHITYVHQHGCHPNREKKDLISLETLREYISLCKTYTPTVDPALRERIVEAYVEMRRDARYSSDPTFVSPRMILGIVRMATARAKLRLSTIVDESDVEEALRLMQFAKDSLRPEQNKIEKRMAPVDAAFAVLRELYHADNAPIAISNAIQRCARKGISEVALKKCLDQYTANGLLVMDRQNIVFAMN