wanglab/gogpt-training-data huggingface dataset:
Protein: nicotinamidase (EC 3.5.1.19) (Nicotinamide deamidase) (O97284)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- nicotinate phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- indole-3-glycerol-phosphate synthase
- Arginase
- aminodeoxychorismate synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Glutamine-dependent NAD
- Apoptosis-inducing factor, putative
Sequence:
MKCLVIVDAQNDFLPNGSFNSKAEYLDVIDKINSVRLNLYKCTEESLLKLKDCKDIIEEKGGKKYEYMYEDKDIVEYSKCHNIIDDENNNEDIYLFPMNENIHNNINGYPHDCMNNIYDSSNINCYNNNNNEINNNCNNNYDNNVVNLTNHTEHADHIIDYNNIKTNSDDLKFGMCILTVDYHPAMHISFAETHRLLYEKICNNNLKCNNINNKSNMNCYDMNNSENSCINNNENEEMKKIDVNNNLIIEETEIESFLKNNNIHTLSDVLNNIDKIKSSQIIYKNIKSKNDIMEYHKINFLNENIDVWPVHCVKNTYGCKVHNKLIRHINDIIIKKAQKENKDSHTIFENEQVNGNIQKLLKQKNITSVYVCGFIFEYCVKETALSFLNLGYETYIVEDATAYLFDRQEDKLFLQNKGIKFINSSKLLS
Protein: Twinfilin (Q9VFM9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11724820}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11724820}.
Interaction partners:
- Adenylyl cyclase-associated protein
- F-actin-capping protein subunit beta
- Glia maturation factor
- WD repeat-containing protein 82
- Profilin
- Cofilin/actin-depolymerizing factor homolog
- Actin-5C
- F-actin-capping protein subunit alpha
- IP04855p
- Drebrin-like protein
Sequence:
MSHQTGIRANEQLAKVFGKAKNGKFRVIKVSIENEQLSCGATAETKKDWERDYDKLIGPLLEKDVPCYILYRLDAKIPLGYSWLLISWTPDTASIRQKMVYASTKATLKTEFGSAYITEELHATTLDECTLEGYRRHKQDFAAPAPLTSREEELKELRKTEVHTEINTNTRHQTLGGINCPLSEATVAAVQDLVRGKHDYLQFRIDLEEEQIHVSRAAKVELADLPKQVPEDHARYHLFLFRHTHEGDYFESYVFVYSMPGYSCSVRERMMYSSCKAPFLDELAALGVEVVKKLEIDSGSELTEAFLQDELHPKKILHRPAFAKPKGPPNRGAKRLTRPTAED
Protein: Matrix-remodeling-associated protein 7 (P84157)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEAPAELLAALPALATALALLLAWLLVRRGAAASPEPARAPPEPAPPAEATGAPAPSRPCAPEPAASPAGPEEPGEPAGLGELGEPAGPGEPEGPGDPAAAPAEAEEQAVEARQEEEQDLDGEKGPSSEGPEEEDGEGFSFKYSPGKLRGNQYKKMMTKEELEEEQRVQKEQLAAIFKLMKDNKETFGEMSDGDVQEQLRLYDM
Protein: Protein wntless homolog (Integral membrane protein GPR177) (Protein evenness interrupted homolog) (EVI) (Q6P689)
Organism: Rattus norvegicus (Rat)
Function: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Also plays an important role in establishment of the anterior-posterior body axis formation during development (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T9L3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T9L3}. Cell membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein Wnt
- Sorting nexin-3
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt-5a
- Protein Wnt-4
- Protein Wnt
- Vacuolar protein sorting-associated protein 35
- Protein Wnt
Sequence:
MAGAIIENMSTKKLCIVGGILLVFQIVAFLVGGLIAPAPTTAVSYVAAKCVDVRKNHHKTRWLMPWGPNKCNKINDFEEAIPREIEANDIVFSVHIPLPSMEMSPWFQFMLFILQIDIAFKLNNQIRENAEVSMDVSLGYRDDMFSEWTEMAHERVPRKLRCTFTSPKTPEHEGRHYECDVLPFMEIGSVAHKYYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDVGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWKWGGVTVQVSSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE
Protein: Actin-binding protein WASF2 (Protein WAVE-2) (Wiskott-Aldrich syndrome protein family member 2) (WASP family protein member 2) (Q8BH43)
Organism: Mus musculus (Mouse)
Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9Y6W5}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250}.
Interaction partners:
- BAR/IMD domain-containing adapter protein 2
- Abl interactor 1
- Abl interactor 2
- Nck-associated protein 1-like
- Cytoplasmic FMR1-interacting protein 1
- Nck-associated protein 1
- Cytoplasmic FMR1-interacting protein 2
- Protein BRICK1
- Actin-binding protein WASF1
- Actin-related protein 2
Sequence:
MPLVTRNIEPRHLCRQTLPSDTSELECRTNITLANVIRQLGSLSKYAEDIFGEICTQASAFASRVNSLAERVDRVQVKVTQLDPKEEEVSLQGINTRKAFRSSTTQDQKLFDRNSLPVPVLETYNSCDAPPPLNNLSPYRDDGKEALKFYTNPSYFFDLWKEKMLQDTKDIMKEKRKHRKEKKDNPNRGNVNPRKIKTRKEEWEKMKMGQEFVESKERLGPSGYSSTLVYQNGSIGSVENVDAASYPPPPQSDSASSPSPSFSEDNLPPPPAEFSYPADNQRGSVLAGPKRTSMVSPSHPPPAPPLSSPPGPKPGFAPPPAPPPPPPMSVPPPLPSMGFGSPGTPPPPSPPSFPPHPDFAAPPPPPPPPAADYPMPPPPLSQPSGGAPPPPPPPPPPGPPPLPFSGADGQPAAPPPPPPSEATKPKSSLPAVSDARSDLLSAIRQGFQLRRVEEQREQEKRDVVGNDVATILSRRIAVEYSDSEDDSSEFDEDDWSD
Protein: PHD finger protein 21A (BHC80a) (BRAF35-HDAC complex protein BHC80) (mBHC80) (Q6ZPK0)
Organism: Mus musculus (Mouse)
Function: Component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it may act as a scaffold. Inhibits KDM1A-mediated demethylation of 'Lys-4' of histone H3 in vitro, suggesting a role in demethylation regulation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15325272}.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related
- Lysine-specific histone demethylase 1A
- Histone deacetylase 1
- REST corepressor 2
- Histone deacetylase 2
- REST corepressor 1
- Zinc finger protein 217
- DNA excision repair protein ERCC-1
- C-terminal-binding protein 1
- High mobility group protein 20A
Sequence:
MELQTLQEALKVEIQVHQKLVAQMKQDPQNADLKKQLHELQAKITALSEKQKRVVEQLRKNLIVKQEQPDKFQIQPLSQSENKLQTAQQQPLQPLQQQQPQQPQQQQQQQQQHAQQSAAAPPSLTASQKTVTTASMITTKTLPLVLKAATATMPASVVGQRPTIAMVTAINSQKAVLSTDVQNTPVNLQTSSKVTGPGAEAVQIVAKNTVTLQVQATPPQPIKVPQFIPPPRLTPRPNFLPQVRPKPVAQNNIPIAPAPPPMLAAPQLIQRPVMLTKFTPTTLPTSQNSIHPVRVVNGQTATIAKTFPMAQLTSIVIATPGTRLAGPQTVQLSKPSLEKQTVKSHPEAEEKQAESRTVTPPAAPKPKREENPQKLAFMVSLGLVTHDHLEEIQSKRQERKRRTTANPVYSGAVFEPERKKSAVTYLNSTMHPGTRKRGRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTDGDIHEDFCSVCRKSGQLLMCDTCSRVYHLDCLEPPLKTIPKGMWICPRCQDQMLKKEEAIPWPGTLAIVHSYIAYKAAKEEEKQKLLKWSSDLKQEREQLEQKVKELSSSISKCMEMKSSILARQKEMRSSLDKVKRLIRLVHGVDLCRPVDSEATAGALSNGPDCTPPANAASTPAPSPSSQSCTANCNQGEETK
Protein: Urea transporter 2 (Solute carrier family 14 member 2) (Urea transporter, kidney) (Q62668)
Organism: Rattus norvegicus (Rat)
Function: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the kidney inner medullary collecting duct which is critical to the urinary concentrating mechanism.
Subcellular location: [Isoform 1]: Apical cell membrane {ECO:0000269|PubMed:16959825}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16959825}; Multi-pass membrane protein {ECO:0000255}. Note=Vasopressin increases expression in the cell membrane. {ECO:0000269|PubMed:16959825}.
Interaction partners:
Sequence:
MSDHPLKEMSDNNRSPPLPEPLSSRYKLYESELSSPTWPSSSQDTHPALPLLEMPEEKDLRSSDEDSHIVKIEKPNERSKRRESELPRRASAGRGAFSLFQAVSYLTGDMKECKNWLKDKPLVLQFLDWVLRGAAQVMFVNNPLSGLIIFIGLLIQNPWWTIAGALGTVVSTLAALALSQDRSAIASGLHGYNGMLVGLLVAVFSEKLDYYWWLLFPVTFASMACPVISSALSTVFAKWDLPVFTLPFNIALTLYLAATGHYNLFFPTTLVKPASSAPNITWSEIEMPLLLQTIPVGVGQVYGCDNPWTGGVILVALFISSPLICLHAAIGSIVGLLAALTVATPFETIYTGLWSYNCVLSCVAIGGMFYVLTWQTHLLALVCALFCAYTGAALSNMMAVVGVPPGTWAFCLSTLTFLLLTSNNPGIHKLPLSKVTYPEANRIYFLTAKRSDEQKPPNGGGGEQSHGGGQRKAEEGSETVFPRRKSVFHIEWSSIRRRSKVFGKSEHQERQTKEPLPYLYRKPTVELLDLNTMEESSEIKVETNTTRTTWIQSSMIAGGKRVSKALSYITGEMKECGEGLKDKSPVFQFLDWVLRGTSQVMFVNNPLSGILIVLGLFVQNPWWAISGCLGTIMSTLTALILSQDKSAIAAGLHGYNGVLVGLLMAVFSDKGNYYWWLLLPVIVMSMTCPILSSALSTVFSKWDLPVFTLPFNIAVTLYLAATGHYNLFFPTKLLQPAVTTPNITWSDVQVPLLLRAIPVGIGQVYGCDNPWTGGIFLVALFVSSPLICLHAAIGSTIGMLAALSIATPFDSIYFGLCGFNSTLACIAIGGMFYVITWQTHLLAIACALFAAYLGAALANMLSVFGLPPCTWPFCLSALTFLLLTTNNPGIYKLPLSKVTYPEANRIYFLSQEKNRRASMITKYQAYDVS
Protein: NACHT, LRR and PYD domains-containing protein 1a allele 1 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)] (D9I2F9)
Organism: Rattus norvegicus (Rat)
Function: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as B.anthracis lethal toxin (LT) or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}.
Interaction partners:
Sequence:
MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSNDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
Protein: Elongin-C (Q03071)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit RPO21 to trigger its proteolysis; plays a role in global genomic repair. Prevents degradation of interacting proteins like PCL6 by the proteasome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Elongin-A
- Cullin-3
- DNA repair protein RAD7
- RING-box protein HRT1
- DNA repair protein RAD16
- UV excision repair protein RAD23
- DNA repair protein RAD4
- COP9 signalosome complex subunit 5
- DNA repair protein RAD2
- ARS-binding factor 1
Sequence:
MSQDFVTLVSKDDKEYEISRSAAMISPTLKAMIEGPFRESKGRIELKQFDSHILEKAVEYLNYNLKYSGVSEDDDEIPEFEIPTEMSLELLLAADYLSI
Protein: GTPase-activating protein (Q6I7S1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MWAGGVGSPRRGMAPAPTDDLFARKLRQPARPPLTPHTFEPRPARGPLLRSGSDAGEVRPPTPASPRARAHSHEDTSRPAATPTRLFTDPLALLGLPAEEPEPTFPPVLEPRWFAHYDVQSLLFDWAPRPRATGSHTESNSGTLALAEDQTTTSDLLLGAPGFVSELGGEGELGLGGPISPPVPPALPNASVSVLEEPQTRTTAYSLEHADLGAGYYRKYFYGKEHQNFFGLDEALGPVAVSLRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPRGLSPRKLLEHVAPRLSPTCLRLGSASPKVPRTLLTLDEQVLSFQRKVGILYCRAGQGSEEEMYNNQEAGAAFMQFLTLLGDVVRLKGFENYRAQLDTKTDSTGAHSLYTTYQDHEIMFHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHAPCTPHTSYRVAVSRTQDTPAFGPALPEGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSLGGRRRATPRSPGAELQAAGALMWGVRAAPGARVSAGAETGGPDHAEVPCLLGISAETLVLVTPRDGRVVFNCACRDVLAWTFSDHQLDLYHGRGEAITLRLDGAPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFITHVERFTFAETTGLRPGARLLRVCGQTLPKLGPEAAAQMLRSASKVCVTVLPPDESGRPRRSFSELYTLSLKEPSRRAAPEPEQDETEKLVTLPAAKQLLHFCLKDGGSPPGPGDLTEERTEFLHSHNSLSPRSSMSDEAPVLPNTTPDLLLVTAVTTLAPGTDRETPPSQDQSGSSSSHEDTSDSAPELRASILPRTLSLRNSISKIMSEAGSETLEDEWQSISEIASTCNTILESLSREGQPILESGDPKETSKCNSEPEPGSLSEKVSHLESMLRKLQEDLQREKADRAALEEEVRSLRHNNQRLLAESESAATRLLLASKQLGSPTTDLA
Protein: Long-chain-fatty-acid--AMP ligase FadD28 (EC 6.2.1.49) (Acyl-AMP synthetase) (FAAL28) (Long-chain fatty acid adenylyltransferase FadD28) (P9WQ59)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of phthiocerol dimycocerosate (PDIM), a cell wall-associated lipid found only in pathogenic mycobacteria. Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase Mas for further chain extension. Probably plays a role in host phagosome maturation arrest (Probable).
Interaction partners:
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phthiocerol dimycocerosate exporter MmpL7
- Phenolphthiocerol/phthiocerol polyketide synthase subunit A
- Peptide synthetase MbtE
- Phenolphthiocerol/phthiocerol polyketide synthase subunit E
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Phthioceranic/hydroxyphthioceranic acid synthase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks15
- Polyketide synthase Pks13
- Polyketide synthetase MbtC
Sequence:
MSVRSLPAALRACARLQPHDPAFTFMDYEQDWDGVAITLTWSQLYRRTLNVAQELSRCGSTGDRVVISAPQGLEYVVAFLGALQAGRIAVPLSVPQGGVTDERSDSVLSDSSPVAILTTSSAVDDVVQHVARRPGESPPSIIEVDLLDLDAPNGYTFKEDEYPSTAYLQYTSGSTRTPAGVVMSHQNVRVNFEQLMSGYFADTDGIPPPNSALVSWLPFYHDMGLVIGICAPILGGYPAVLTSPVSFLQRPARWMHLMASDFHAFSAAPNFAFELAARRTTDDDMAGRDLGNILTILSGSERVQAATIKRFADRFARFNLQERVIRPSYGLAEATVYVATSKPGQPPETVDFDTESLSAGHAKPCAGGGATSLISYMLPRSPIVRIVDSDTCIECPDGTVGEIWVHGDNVANGYWQKPDESERTFGGKIVTPSPGTPEGPWLRTGDSGFVTDGKMFIIGRIKDLLIVYGRNHSPDDIEATIQEITRGRCAAISVPGDRSTEKLVAIIELKKRGDSDQDAMARLGAIKREVTSALSSSHGLSVADLVLVAPGSIPITTSGKVRRGACVEQYRQDQFARLDA
Protein: RNA polymerase sigma-54 factor rpoN (E0SE58)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Anti-sigma-E factor RseA
- Type III protein secretion system sensor kinase
- DNA-binding response regulator, LuxR family, near polyamine transporter
- Transmembrane anti-sigma factor
- Type III secretion protein
Sequence:
METITLKQMDACQIHTPANTVDWEQVFRLHGKRLQNFIRKRVSNREDVEDLQQMTYLEVLKNREKFAGASRPETWVFGIALNLVRNHFKQARYRAVDISDDALEVAEILSTDIDPSRITECDHSLNRALAASAHLPEETRKMLMMLLDADVSYQDIAEQLNIPIGTVRSRLSRARGYLRQAVDA
Protein: Ubiquitin-activating enzyme (EC 6.2.1.45) (Q8ID54)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ubiquitin-related modifier 1 homolog
- Rhodanese like protein, putative
- Cysteine desulfurase IscS
- Cytoplasmic tRNA 2-thiolation protein 1
- Small ubiquitin-related modifier
Sequence:
MYQVVKEYLNNYQRYIYYGVFIVVGYFLHDLINYAQREGVRIGRIRKIFDLFSKVLKKVYIFFNFYERRIITLENELFYKNYDKEVIDRHGKLLNIYDIPHDSLYKIFNTKILIIGLGGLGSPVCLYLSKFGFKEIGLVDGDKVEKSNLHRQIIHKEKYIGLNKCISAKLFLKDMDVHVSDCIKCYPFFLDKLNGINIIKEYDIIIDCTDNISTRFLINDLCILYKKKLIFASALGIYGQVNVYNLNNNTSSCYRCLKSFNNHSQNNDCDENGILSTVTGVIGLLQANEVIKLSIGLDQDVLTNFLTYNSFSNKLPFESLNINYKNKNCLCSMKNFKELYNFILSHNYDNINNTNNTNNTNNTYNTNNTYNTYNTNYNNNYNNNNNSSSNKINNANNIYCNNLICFNQTNETYIYQIDTFQFIDILNNNYSSLSFPVNQICILDVRKINNTNIYGLRNSVKWSFYEIIETFNKLQHNKHELLQIIIDKLNISKSKKNILIIVVCRRGIDSLKITKHFNNLFLYNDKLDSNKKEATYNNNDISLYNTKNKKFNKTLLNDAHIIAYNLKGGYLQLQKKIFKNLPFL
Protein: Growth arrest-specific protein 6 (GAS-6) (AXL receptor tyrosine kinase ligand) (Growth-potentiating factor) (GPF) (Q63772)
Organism: Rattus norvegicus (Rat)
Function: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:7559388}.
Interaction partners:
- Tyrosine-protein kinase Mer
- Tyrosine-protein kinase receptor UFO
- Tyrosine-protein kinase receptor TYRO3
- Vitamin K-dependent protein S
- Furin
- Galectin-3
- Tubby-like protein
Sequence:
MPPPPGPTAALGTALLLLLLASESSHTVLLRAREAAQFLRPRQRRAYQVFEEAKQGHLERECVEEVCSKEEAREVFENDPETDYFYPRYQECMRKYGRPEDKNPNFATCVKNLPDQCTPNPCDKKGTQLCQDLMGNFFCLCKDGWGGRLCDKDVNECSQKNGGCSQVCHNKPGSFQCACHSGFSLQSDNKSCQDIDECTDSDTCGDARCKNLPGSYSCLCDKGYTYSSKEKTCQDVDECQQDRCEQTCVNSPGSYTCHCNGRGGLKLSPDMDTCEDILPCVPFSMAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLLAEFDFRTFDPEGVLFFAGGRSDSTWIVLGLRAGRLELQLRYNGVGRITSSGPTINHGMWQTISVEELDRNLVIKVNKDAVMKIAVAGGLFQLERGLYHLNLTVGGIPFKESDLVQPINPRLDGCMRSWNWLNGEDSAIQETVKANTKMQCFSVTERGSFFPGNGFAFYSLNYTRTSLDVGTETTWEVEVVARIRPATDTGVLMALVGDKDVVLLSVALVDYHSTKKLKKQLVVLAVENVALALMEIKVCDSQEHTVTVSLRDGEATLEVDGTKGQSEVSTAQLQERLDLLKTRLQGSVLTFVGGLPDVQVTSTPVTAFYRGCMTLEVNGKTLDLDTASYKHSDITSHSCPPVEHVTA
Protein: DNA-binding transcriptional regulator NtrC (Nitrogen regulation protein NR(I)) (Nitrogen regulator I) (Q74EF9)
Organism: Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- histidine kinase
- histidine kinase
- DNA-binding transcriptional regulator NtrC)
- RNA polymerase sigma-54 factor RpoN
- Amidohydrolase, YcaC-related protein
- Glutamate dehydrogenase
- histidine kinase
Sequence:
MLLNRILVADDEESMRWVLSKALRKKGFTVDLARDGEEALRLIQSNEYDLAILDIKMPGFTGLELLDKVRELKHDLLMVIMTAEASMKNAVEAMKRGAYDYITKPFDLDVIDAIIEKVHKAREITSQMTILREELKERYHLEKNIIGNSPAMREVYKTIGKVAPSDVTVLVQGESGTGKELIARAIHFNSKRIGKPFIALNCAAIPKDLLESELFGFEKGAFTGAVERKLGKFEQANGGTIFLDEIGDMPLDLQAKILRVLQEKEVTRTGGSQNIAVDVRIVAATNQNLEELVRKKQFREDLFYRLNVVPIQLVPLRERKEDVPLLVDYFLQNACAELEVSPKKCSPEAMALLTTHSWPGNVRELENTIKRAVILSSDPLLTPSDFPGLRARQTGSEATAADDLSLEALVDMKLRASLTNLDKMESGDIYNLVLKQIERPLIRFVLEKTRGNQVKGAEILGINRNTLRKKIQELGIELRKD
Protein: Probable 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase (EC 3.1.1.91) (5-nitroanthranilic acid degradation protein C) (Lactone hydrolase NaaC) (F8QQ74)
Organism: Bradyrhizobium sp
Function: Involved in the 5-nitroanthranilic acid (5NAA) degradation. Catalyzes the hydrolysis of the lactone to produce maleylpyruvate biodegradation of 5-nitroanthranilate (Probable).
Interaction partners:
Sequence:
MATETIAMDWVDIGTNGESRLAYLARPVVTGRLPAVIVMPAIHGINTYIKDVAIDLAKAGFVALLIDIHSPEQEPDLSNAEKIQIAVETLDDRKVLKDVDAAVRYLEQHAAVRADRLGILGFCVGGTYALLAARTPAIRVSVGFYGLLEYQSRTDNKPVSPLDSVAQFTAPILFHVGDKDPWIDSKMLAEFTKRMQQHQKSYELCIYRGAGHAFHEHFRDAYRPIAAQSAWNNTLIYLRWHLCGKRTV
Protein: Ribosome assembly factor MRT4 (mRNA turnover protein 4) (P33201)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11583614, ECO:0000269|PubMed:19789271}. Cytoplasm {ECO:0000269|PubMed:19789271}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:19789271}.
Interaction partners:
- Nucleolar complex protein 2
- rRNA-processing protein EBP2
- 25S rRNA
- Pescadillo homolog
- Ribosome biogenesis protein 15
- ATP-dependent RNA helicase HAS1
- Ribosome biogenesis protein RPF2
- Ribosome biogenesis protein RLP7
- Regulator of ribosome biosynthesis
- Eukaryotic translation initiation factor 6
Sequence:
MPRSKRSKLVTLAQTDKKGRENKERIFDEVREALDTYRYVWVLHLDDVRTPVLQEIRTSWAGSKLIMGKRKVLQKALGEKREEEYKENLYQLSKLCSGVTGLLFTDEDVNTVKEYFKSYVRSDYSRPNTKAPLTFTIPEGIVYSRGGQIPAEEDVPMIHSLEPTMRNKFEIPTKIKAGKITIDSPYLVCTEGEKLDVRQALILKQFGIAASEFKVKVSAYYDNDSSTVESTNINME
Protein: DNA damage checkpoint protein LCD1 (DNA damage checkpoint protein 2) (Lethal, checkpoint-defective, DNA damage-sensitive protein 1) (Q04377)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a complex with the serine/threonine kinase MEC1 which activates checkpoint signaling upon genotoxic stresses. The MEC1-LCD1 complex is recruited by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Required for the recruitment of MEC1 to DNA lesions, the activation of CHK1 and RAD53 kinases and phosphorylation of RAD9 in response to DNA damage. Required for cell growth and meiotic recombination.
Subcellular location: Cytoplasm. Nucleus. Note=Localizes to nuclear DNA repair foci with other DNA repair proteins in response to DNA double strand breaks. The recruitment to DNA lesion sites requires the presence of the RPA complex on DNA.
Interaction partners:
- Serine/threonine-protein kinase MEC1
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase RAD53
- Serine/threonine-protein kinase CHK1
- DNA repair protein RAD9
- Replication factor A protein 1
- Mediator of replication checkpoint protein 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA damage checkpoint protein 1
- DNA damage checkpoint control protein MEC3
Sequence:
MRRETVGEFSSDDDDDILLELGTRPPRFTQIPPSSAALQTQIPTTLEVTTTTLNNKQSKNDNQLVNQLNKAQGEASMLRDKINFLNIEREKEKNIQAVKVNELQVKHLQELAKLKQELQKLEDEKKFLQMEARGKSKREVITNVKPPSTTLSTNTNTITPDSSSVAIEAKPQSPQSKKRKISDNLLKKNMVPLNPNRIIPDETSLFLESILLHQIIGADLSTIEILNRLKLDYITEFKFKNFVIAKGAPIGKSIVSLLLRCKKTLTLDRFIDTLLEDIAVLIKEISVHPNESKLAVPFLVALMYQIVQFRPSATHNLALKDCFLFICDLIRIYHHVLKVPIHESNMNLHVEPQIFQYELIDYLIISYSFDLLEGILRVLQSHPKQTYMEFFDENILKSFEFVYKLALTISYKPMVNVIFSAVEVVNIITSIILNMDNSSDLKSLISGSWWRDCITRLYALLEKEIKSGDVYNENVDTTTLHMSKYHDFFGLIRNIGDNELGGLISKLIYTDRLQSVPRVISKEDIGMDSDKFTAPIIGYKMEKWLLKLKDEVLNIFENLLMIYGDDATIVNGEMLIHSSKFLSREQALMIERYVGQDSPNLDLRCHLIEHTLTIIYRLWKDHFKQLREEQIKQVESQLIMSLWRFLVCQTETVTANEREMRDHRHLVDSLHDLTIKDQASYYEDAFEDLPEYIEEELKMQLNKRTGRIMQVKYDEKFQEMARTILESKSFDLTTLEEADSLYISMGL