wanglab/gogpt-training-data huggingface dataset:
Protein: Microfibrillar-associated protein 2 (MFAP-2) (Microfibril-associated glycoprotein 1) (MAGP) (MAGP-1) (Tropoelastin-binding protein) (P27424)
Organism: Bos taurus (Bovine)
Function: Component of the elastin-associated microfibrils.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Fibrillin-1
- Elastin
- Lysyl oxidase homolog 1
- Microfibrillar-associated protein 5
- Fibrillin-2
- Decorin
- Microfibril-associated glycoprotein 3
- Microfibril-associated glycoprotein 4
- Protein-lysine 6-oxidase
- Fibulin-5
Sequence:
MRAASLFLLFLPAGLLAQGQYDLDPLPPYPDHVQYTHYSEQIENPDYYDYPEMTPRPPEEQFQFQSQQQVQQEVIPAPTLEPGTVETEPTEPGPLDCREEQYPCTRLYSIHKPCKQCLNEVCFYSLRRVYVVNKEICVRTVCAQEELLRADLCRDKFSKCGVLASSGLCQSVAAACARSCGGC
Protein: Nucleoprotein (N protein) (Nucleocapsid protein) (p38) (p40) (P0C797)
Organism: Borna disease virus (strain V) (BDV)
Function: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Plays a critical role in the nucleocytoplasmic transport of viral RNP by interaction with other viral proteins. The nuclear export signal is masked by the interaction with the phosphoprotein P. Delays the host cell cycle progression by interacting with the host CDK1-cyclin B1 phase in late G2. Inhibits host NF-kappaB activation.
Subcellular location: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:11238866}. Host cytoplasm {ECO:0000269|PubMed:11238866}. Note=Shuttles between the host nucleus and cytoplasm. {ECO:0000269|PubMed:11238866}.
Interaction partners:
Sequence:
MPPKRRLVDDADAMEDQDLYEPPASLPKLPGKFLQYTVGGSDPHPGIGHEKDIRQNAVALLDQSRRDMFHTVTPSLVFLCLLIPGLHAAFVHGGVPRESYLSTPVTRGEQTVVKTAKFYGEKTTQRDLTELEISSIFSHCCSLLIGVVIGSSSKIKAGAEQIKKRFKTMMAALNRPSHGETATLLQMFNPHEAIDWINGQPWVGSFVLSLLTTDFESPGKEFMDQIKLVASYAQMTTYTTIKEYLAECMDATLTIPVVAYEIRDFLEVSAKLKEDHADLFPFLGAIRHPDAIKLAPRSFPNLASAAFYWSKKENPTMAGYRASTIQPGASVKETQLARYRRREISRGEDGAELSGEISAIMKMIGVTGLN
Protein: RNA editing 3' exouridylylase MP99 (Q38BP2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
- Protein artemis
- Small ubiquitin protein, putative
- RNA editing associated helicase 2
- REH2-associated factor 1
- MP18 RNA editing complex protein
- RNA-editing-associated protein 1
- RNA-editing ligase 1, mitochondrial
- RNA editing complex protein MP61
- RNA editing complex protein MP63
- RNA editing complex protein
Sequence:
MLRRSRLHLLADYRTSSKISDEFNNVLNRSGWGFDHVAVDVGSLSGAAGRLTRDLIGQERDAETVKIIHKQITNVILRRIQPKKSLAIFIDGSEPLWKVRHMRLYPGKKFEGKFYRSAASPMVYSLEDKLRCVGPDLRTPPKEFIVSGPAAPGPVEAKLSAWMLDLATRALPDGAVTTPTVTGAAAAASASAGPPEVTFNDTFCLIGGNDAFLSALGATPFHNITTVTLQQGEMKSLSLSEALEWFAMDHLLKGETSIGSGGNELQKRLASVRTDIVLLYLMANGISATDLPGLGVNFKDLMEAYTAEEANKLYLFGKTSEERCLRMCPLNLERVLTHATRRTSTPTRFCQQSADYLEILLQTHSMICDGGIKNFRWTPNDNDAVPEKQPKIPIERFIGHLKHLAAQGGETTAVADVGSTEPGLAASVDWTFALTGIETLLLSAPKAEMIDQIIPVFTKGHTLPDGVAQDIVDTKNVVEALHKVRRVLQVVVTSDNSGNDDGRIEHPAFNHYPTHYFVRTPGSRGPPPGWTYKSVNLGVRAVALGVRHRVASGMLTAASRVLDSGGVSSKNSLFVFHVKDGITTPSGGGNEDGWLETPCHELAGSSANPASKEISTLRVVTWNVQFSRHSGERTPLGRDGIDWCTSTRYVALAQTLEGLDADVIGMQEVEPAWCKYLSQQPWVREKYAMTCCEHSHAIQPWGVMLLVRRSLCVTSTHHANVPAFSGHTSVMPEVTVVVSEGVPVTVGSMHLLAPYNQNNISNRTTQLDNLTKRLRTRPPINGKQAGLIVMGDFNDCAKNYFTFPPEMGFKDAWLLLHPDEGVSSKSGHTIDGDRNPYAAQIIEKEFYGRADRVLFSSRNLQPIQTEIIGTTSVREMGITKQVDIDKDVPEYLYPSDHFGLLVEFQVV
Protein: Synaptonemal complex central element protein 3 (Testis-specific expressed protein 2) (TSEG-2) (B5KM66)
Organism: Mus musculus (Mouse)
Function: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility. May play a role in apoptosis of spermatogenic cells and pathogenesis of cryptorchidism.
Subcellular location: Nucleus {ECO:0000269|PubMed:21637789}. Chromosome {ECO:0000269|PubMed:21637789, ECO:0000269|PubMed:30949703}. Note=Colocalizes with SYCE1 in the central elements. {ECO:0000269|PubMed:21637789}.
Interaction partners:
- Synaptonemal complex central element protein 2
- Synaptonemal complex central element protein 1
- Testis-expressed protein 12
- Synaptonemal complex protein 1
- Synaptonemal complex protein 3
- Synaptonemal complex protein 2
- Protein SIX6OS1
- Cohesin subunit SA-3
- Structural maintenance of chromosomes protein 1B
- HORMA domain-containing protein 1
Sequence:
MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ
Protein: Activator of 90 kDa heat shock protein ATPase homolog 1 (AHA1) (Q8BK64)
Organism: Mus musculus (Mouse)
Function: Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O95433}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O95433}. Note=May transiently interact with the endoplasmic reticulum. {ECO:0000250|UniProtKB:O95433}.
Interaction partners:
- Stress-induced-phosphoprotein 1
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Prostaglandin E synthase 3
- Hsp90 co-chaperone Cdc37
- Heat shock 70 kDa protein 1B
- Peptidyl-prolyl cis-trans isomerase D
- Endoplasmin
- Cysteine and histidine-rich domain-containing protein 1
- Peptidyl-prolyl cis-trans isomerase FKBP4
Sequence:
MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTEKLKTLFLAVRVENEEGKCEVTEVNKLDGEASINNRKGKLIFFYEWTIKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEDGVKLLREAVGIYISTLKTEFTQGMILPTVNGESVDPVGQPALKTETCKAKSAPSKSQAKPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
Protein: Serine/threonine-protein kinase AFC3 (EC 2.7.12.1) (P51568)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g26610
- Protein FIP2
- Cytochrome P450, family 702, subfamily A, polypeptide 8
- DExH-box ATP-dependent RNA helicase DExH14
- At3g16760
- Protein phosphatase inhibitor 2
- Nuclear pore complex protein NUP35
- Protein C2-DOMAIN ABA-RELATED 11
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH1
- Insulin-degrading enzyme-like 1, peroxisomal
Sequence:
MIANGFESMDKERVRKRPRMTWDEAPAEPEAKRAVIKGHGSDGRILSPPLRDDDRDGHYVFSLRDNLTPRYKILSKMGEGTFGRVLECWDRDTKEYVAIKIIRSIKKYRDAAMIEIDVLQKLVKSDKGRTRCVQMKNWFDYRNHICIVFEKLGPSLFDFLKRNKYSAFPLALVRDFGCQLLESVAYMHELQLVHTDLKPENILLVSSENVKLPDNKRSAANETHFRCLPKSSAIKLIDFGSTVCDNRIHHSIVQTRHYRSPEVILGLGWSYQCDLWSIGCILFELCTGEALFQTHDNLEHLAMMERALGPLPEHMTRKASRGAEKYFRRGCRLNWPEGANSRESIRAVKRLDRLKDMVSKHVDNTRSRFADLLYGLLAYDPSERLTANEALDHPFFKSSS
Protein: Nuclear egress protein 1 (P10215)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04023, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
Interaction partners:
Sequence:
MYDTDPHRRGSRPGPYHGKERRRSRSSAAGGTLGVVRRASRKSLPPHARKQELCLHERQRYRGLFAALAQTPSEEIAIVRSLSVPLVKTTPVSLPFCLDQTVADNCLTLSGMGYYLGIGGCCPACNAGDGRFAATSREALILAFVQQINTIFEHRAFLASLVVLADRHNAPLQDLLAGILGQPELFFVHTILRGGGACDPRLLFYPDPTYGGHMLYVIFPGTSAHLHYRLIDRMLTACPGYRFVAHVWQSTFVLVVRRNAEKPTDAEIPTVSAADIYCKMRDISFDGGLMLEYQRLYATFDEFPPP
Protein: Anaerobic ribonucleoside-triphosphate reductase (EC 1.1.98.6) (Class III ribonucleoside-triphosphate reductase) (P28903)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Interaction partners:
- Anaerobic ribonucleoside-triphosphate reductase-activating protein
- Ribonucleoside-diphosphate reductase 1 subunit beta
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Adenylate cyclase
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- CTP synthase
- Nucleoside diphosphate kinase
- Pyruvate kinase I
- Nucleoside triphosphate pyrophosphohydrolase
- dCTP deaminase
Sequence:
MTPHVMKRDGCKVPFKSERIKEAILRAAKAAEVDDADYCATVAAVVSEQMQGRNQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIEREKRGRLNQEIRGLVEQTNASLLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTASYNKHRKTAEEWNIPDAEGYANSRTIKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQESILRNRIAGLGKNRKTAVFPKLVFAIRDGLNHKKGDPNYDIKQLALECASKRMYPDILNYDQVVKVTGSFKTPMGCRSFLGVWENENGEQIHDGRNNLGVISLNLPRIALEAKGDEATFWKLLDERLVLARKALMTRIARLEGVKARVAPILYMEGACGVRLNADDDVSEIFKNGRASISLGYIGIHETINALFGGEHVYDNEQLRAKGIAIVERLRQAVDQWKEETGYGFSLYSTPSENLCDRFCRLDTAEFGVVPGVTDKGYYTNSFHLDVEKKVNPYDKIDFEAPYPPLANGGFICYGEYPNIQHNLKALEDVWDYSYQHVPYYGTNTPIDECYECGFTGEFECTSKGFTCPKCGNHDASRVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHLGNGQIG
Protein: Corticoliberin (Corticotropin-releasing factor) (CRF) (Corticotropin-releasing hormone) (P06850)
Organism: Homo sapiens (Human)
Function: Hormone regulating the release of corticotropin from pituitary gland (By similarity). Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P06296}.
Interaction partners:
- Corticotropin-releasing factor-binding protein
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor receptor 2
- Urocortin
- Urocortin-3
- Urocortin-2
- Pro-opiomelanocortin
- Guanine nucleotide-binding protein G
- Pro-neuropeptide Y
- Somatoliberin
Sequence:
MRLPLLVSAGVLLVALLPCPPCRALLSRGPVPGARQAPQHPQPLDFFQPPPQSEQPQQPQARPVLLRMGEEYFLRLGNLNKSPAAPLSPASSLLAGGSGSRPSPEQATANFFRVLLQQLLLPRRSLDSPAALAERGARNALGGHQEAPERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK
Protein: Matrix protein (gp18) (p16) (P0C794)
Organism: Borna disease virus 1 (BoDV-1)
Function: Plays a crucial role in virion assembly and budding.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C795}. Host cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:11711600}. Note=During viral budding, associates with the inner side of the plasma membrane of infected cells (PubMed:11711600). Found in nuclear punctate structures that have been proposed to be the sites of viral replication and transcription, also termed viral speckles of transcripts (vSPOTs) (By similarity). {ECO:0000250|UniProtKB:P0C795, ECO:0000269|PubMed:11711600}.
Interaction partners:
Sequence:
MNSKHSYVELKDKVIVPGWPTLMLEIDFVGGTSRNQFLNIPFLSVKEPLQLPREKKLTDYFTIDVEPAGHSLVNIYFQIDDFLLLTLNSLSVYKDPIRKYMFLRLNKEQSKHAINAAFNVFSYRLRNIGVGPLGPDIRSSGP
Protein: Protein NRT1/ PTR FAMILY 6.2 (AtNPF6.2) (Nitrate transporter 1.4) (Q9SZY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- High affinity nitrate transporter 2.7
- Chloride channel protein CLC-a
- High-affinity nitrate transporter 2.1
- High-affinity nitrate transporter 2.2
- High affinity nitrate transporter 2.5
- High affinity nitrate transporter 2.4
Sequence:
MESKGSWTVADAVDYKGRPADKSKTGGWITAALILGIEVVERLSTMGIAVNLVTYLMETMHLPSSTSANIVTDFMGTSFLLCLLGGFLADSFLGRFKTIGIFSTIQALGTGALAVATKLPELRPPTCHHGEACIPATAFQMTILYVSLYLIALGTGGLKSSISGFGSDQFDDKDPKEKAHMAFFFNRFFFFISMGTLLAVTVLVYMQDEVGRSWAYGICTVSMAIAIVIFLCGTKRYRYKKSQGSPVVQIFQVIAAAFRKRKMELPQSIVYLYEDNPEGIRIEHTDQFHLLDKAAIVAEGDFEQTLDGVAIPNPWKLSSVTKVEEVKMMVRLLPIWATTIIFWTTYAQMITFSVEQASTMRRNIGSFKIPAGSLTVFFVAAILITLAVYDRAIMPFWKKWKGKPGFSSLQRIAIGLVLSTAGMAAAALVEQKRLSVAKSSSQKTLPISVFLLVPQFFLVGAGEAFIYTGQLDFFITQSPKGMKTMSTGLFLTTLSLGFFVSSFLVSIVKRVTSTSTDVGWLADNINHGRLDYFYWLLVILSGINFVVYIICALWFKPTKGKDSVEKENGKGFSVEDC
Protein: Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Protein lactyltransferase AARS1) (EC 6.-.-.-) (P50475)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03133}. Note=Translocates to the nucleus in response to increased levels of lactate; nuclear translocation is dependent on KPNA4. {ECO:0000255|HAMAP-Rule:MF_03133}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Glycine--tRNA ligase
- Alanine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MDSTLTAREIRERFINYFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTVDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPVERLYVTYFGGDEAAGLEPDLECRQIWQNLGLDEAKILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNRESDGVLKPLPKKSIDTGMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDTDGIDMAYRVLADHARTITVALADGGRPDNTGRGYVLRRILRRAVRYSHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDCQTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRAKGLEATDDSPKYNYHSDSSGSYVFECTVATVLALRREKMFVDEVVTGQECGVVLDKTCFYAEQGGQIFDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGNLRVGDQVRLFIDEPRRRPVMSNHTATHILNFALRSVLGDADQKGSLVAPDRLRFDFTAKGAMSTEQIKKTEEIVNGMIEAAKPVYTLDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKSETLKKSLSAMEVKVKAQSAPNKDVQKEIADLGEVLATAVIPQWQKDEQRETLKSLKKVMDDLDRASKADVQKRVLEKTKQLIDSNPNQPLVILEMESGASAKALNEALKLFKTHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDMSAQATGKNVGCLQEALQLATSFAQLRLGDVKN
Protein: NAD(P)H dehydrogenase [quinone] 1 isoform 2 (EC 1.6.5.2) (NAD(P)H dehydrogenase, quinone 1) (Q6P0H2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Gamma-glutamyl carboxylase.
- vitamin-K-epoxide reductase
- vitamin-K-epoxide reductase
- ornithine decarboxylase
- Crystallin, zeta
- Glutamate--cysteine ligase
- Nuclear factor
- Heme oxygenase
- Glutamate-cysteine ligase, modifier subunit.
- Transmembrane and coiled-coil domains 3.
Sequence:
MAQKTALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMKFKASATAEDIKGDLQNPEHFVYNNEMMVAWKEGRLSDDVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMQNMYDNGIFKNKRAMLSFTTGGMESMYKDDSLHGDINILLWPLQNGVLRFCGFQVLAPQIFWSPAYTPPEGRAAMLDGWRERLGGVFEEKPLSFAPSEYFDLSFQAGFCLRPEVKDKLASEPYGITTAHHLGKPLPPNNQTKPKQN
Protein: Regulatory protein AtoC (Acetoacetate metabolism regulatory protein) (DNA-binding transcriptional regulator AtoC) (Ornithine decarboxylase antizyme) (Q06065)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system AtoS/AtoC. In the presence of acetoacetate, AtoS/AtoC stimulates the expression of the atoDAEB operon, leading to short chain fatty acid catabolism and activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic pathway. Also induces the operon in response to spermidine. Involved in the regulation of motility and chemotaxis, via transcriptional induction of the flagellar regulon. AtoC acts by binding directly to the promoter region of the target genes. In addition to its role as a transcriptional regulator, functions as a post-translational regulator that inhibits polyamine biosynthesis via regulation of ornithine decarboxylase (ODC).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16153782}. Note=Membrane-associated in the presence of AtoS. {ECO:0000269|PubMed:16153782}.
Interaction partners:
- Signal transduction histidine-protein kinase AtoS
- Acetate CoA-transferase subunit alpha
- Acetate CoA-transferase subunit beta
- RNA polymerase sigma-54 factor
- Fatty acid metabolism regulator protein
Sequence:
MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEVKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGIDPADV
Protein: KH domain-containing protein SPIN1 (SPL11-interacting protein 1) (Q75GR5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in flowering time control. Binds DNA and RNA in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:18586868}.
Interaction partners:
- Os02g0732700 protein
- Mediator of RNA polymerase II transcription subunit 10
Sequence:
MSGLYSPGFSPARNLSPQIRSNPTDVDSQYLAELLAEHQKLGPFMQVLPICSKLLSQEIMRVSSIVHNHGFGDFDRHRFRSPSPMSSPNPRSNRSGNGFSPWNGLHQERLGFPQGTSMDWQGAPPSPSSHVVKKILRLDVPVDSYPNFNFVGRILGPRGNSLKRVEASTGCRVFIRGKGSIKDPGKEDKLRGKPGYEHLSDPLHILIEAEFPASIIDARLRHAQEVIEELLKPVDESQDFYKRQQLRELAMLNSTLREDSPHPGSVSPFSNGGMKRAKTGQ
Protein: Serine protease Rv3671c (EC 3.4.21.-) (P9WHR9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for M.tuberculosis resistance to oxidative stress in addition to its role in resistance to acid, which is essential for virulence. It protects M.tuberculosis against phagolysosomal concentrations of acid and maintains its intrabacterial pH when phagocytosed by IFN-gamma-activated macrophages.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nudix hydrolase domain-containing protein
- Proteasome-associated ATPase
- Endonuclease III lyase)
- Serine protease PepD
- Probable conserved Mce associated membrane protein
- Glycerol kinase
- Possible membrane protein
- Possible membrane-anchored thioredoxin-like protein
- CysO-cysteine peptidase
- Proteasome subunit beta
Sequence:
MTPSQWLDIAVLAVAFIAAISGWRAGALGSMLSFGGVLLGATAGVLLAPHIVSQISAPRAKLFAALFLILALVVVGEVAGVVLGRAVRGAIRNRPIRLIDSVIGVGVQLVVVLTAAWLLAMPLTQSKEQPELAAAVKGSRVLARVNEAAPTWLKTVPKRLSALLNTSGLPAVLEPFSRTPVIPVASPDPALVNNPVVAATEPSVVKIRSLAPRCQKVLEGTGFVISPDRVMTNAHVVAGSNNVTVYAGDKPFEATVVSYDPSVDVAILAVPHLPPPPLVFAAEPAKTGADVVVLGYPGGGNFTATPARIREAIRLSGPDIYGDPEPVTRDVYTIRADVEQGDSGGPLIDLNGQVLGVVFGAAIDDAETGFVLTAGEVAGQLAKIGATQPVGTGACVS
Protein: Cyclin-A1 (P78396)
Organism: Homo sapiens (Human)
Function: May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase inhibitor 1
- S-phase kinase-associated protein 2
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase 1
- Cyclin-dependent kinase inhibitor 1B
- Transcription factor E2F1
- Retinoblastoma-associated protein
- Cyclin-dependent kinase 6
- Cell division control protein 6 homolog
- Myb-related protein B
Sequence:
METGFPAIMYPGSFIGGWGEEYLSWEGPGLPDFVFQQQPVESEAMHCSNPKSGVVLATVARGPDACQILTRAPLGQDPPQRTVLGLLTANGQYRRTCGQGITRIRCYSGSENAFPPAGKKALPDCGVQEPPKQGFDIYMDELEQGDRDSCSVREGMAFEDVYEVDTGTLKSDLHFLLDFNTVSPMLVDSSLLSQSEDISSLGTDVINVTEYAEEIYQYLREAEIRHRPKAHYMKKQPDITEGMRTILVDWLVEVGEEYKLRAETLYLAVNFLDRFLSCMSVLRGKLQLVGTAAMLLASKYEEIYPPEVDEFVYITDDTYTKRQLLKMEHLLLKVLAFDLTVPTTNQFLLQYLRRQGVCVRTENLAKYVAELSLLEADPFLKYLPSLIAAAAFCLANYTVNKHFWPETLAAFTGYSLSEIVPCLSELHKAYLDIPHRPQQAIREKYKASKYLCVSLMEPPAVLLLQ
Protein: Adenylyl cyclase-associated protein (CAP) (P17555)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:8552082}. Note=Cortical actin patches.
Interaction partners:
- Actin-binding protein
- Adenylate cyclase
- Actin
- Cofilin
- Profilin
- Twinfilin-1
- Imidazole glycerol phosphate synthase hisHF
- Actin-interacting protein 1
- Centractin
- Fimbrin
Sequence:
MPDSKYTMQGYNLVKLLKRLEEATARLEDVTIYQEGYIQNKLEASKNNKPSDSGADANTTNEPSAENAPEVEQDPKCITAFQSYIGENIDPLVELSGKIDTVVLDALQLLKGGFQSQLTFLRAAVRSRKPDYSSQTFADSLRPINENIIKLGQLKESNRQSKYFAYLSALSEGAPLFSWVAVDTPVSMVTDFKDAAQFWTNRILKEYRESDPNAVEWVKKFLASFDNLKAYIKEYHTTGVSWKKDGMDFADAMAQSTKNTGATSSPSPASATAAPAPPPPPPAPPASVFEISNDTPATSSDANKGGIGAVFAELNQGENITKGLKKVDKSQQTHKNPELRQSSTVSSTGSKSGPPPRPKKPSTLKTKRPPRKELVGNKWFIENYENETESLVIDANKDESIFIGKCSQVLVQIKGKVNAISLSETESCSVVLDSSISGMDVIKSNKFGIQVNHSLPQISIDKSDGGNIYLSKESLNTEIYTSCSTAINVNLPIGEDDDYVEFPIPEQMKHSFADGKFKSAVFEHAG
Protein: 14-3-3 protein eta (P68510)
Organism: Mus musculus (Mouse)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Serine/threonine-protein kinase B-raf
- M-phase inducer phosphatase 2
- M-phase inducer phosphatase 3
- Serine/threonine-protein kinase A-Raf
- RAF proto-oncogene serine/threonine-protein kinase
- 14-3-3 protein zeta/delta
- Forkhead box protein O3
- 14-3-3 protein beta/alpha
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
Sequence:
MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN