wanglab/gogpt-training-data huggingface dataset:
Protein: Fatty acyl-CoA reductase (EC 1.2.1.84) (Q8S7T9)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Fatty acyl-CoA reductase
- Fatty acyl-CoA reductase
- Os05g0556300 protein
Sequence:
MGMSSCVNLSRVAAAAAGRRPGFAGELGGRRGHGRSVLPVVAALPVRRKGSGCGVACCVSSSSSSSVHGKNSAAAAEGHAGGIGIAEFLGGKNFLITGGTGFLAKVLIEKILRTNPDVGKIYVLIKAKDGDAALKRLHNEVVDTELFSRLQEIHGKDYHSFAARKLVPVVGDVREANVGIAPELAGVIADEVDIIVNSAANTTFDERYDVAMDINTVGPFRIMSFAQRFRRLKLFLQVSTAYVNGQRQGVVLEKPFRLGDTIAKELGSPDSSQHKNTMLDIEAEIKLAFDHRRHGDDSASFSEEMKELGLERAKLHGWQDTYVFTKAMGEMVINSMRGDIPVVTIRPSVIESTWRDPFPGWMEGNRMMDPVVLYYGKGQLSGFLADPEGVLDVVPADMVVNATLASMAKHGRGGAAAAAAAAEGMHVYHVASSTVNPLAFGDLSRFLFQHFTGSPYSDAAGRPIHVPPMRLFDTMEQFASYVETDALLRAGRLAGAGAGAGDERVSQRLRELCAKSVEQTIYLGSIYQPYTFYGGRFDNGNTEALIGEMSEEEKARFHFDVRSIEWTDYITNVHIPGLRKHVMKGRGVGGGSGASSSSNASLLAGASV
Protein: Large T antigen (LT) (LT-AG) (EC 5.6.2.4) (DNA 3'-5' helicase large T antigen) (P03070)
Organism: Simian virus 40 (SV40)
Function: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. May inactivate the growth-suppressing properties of the E3 ubiquitin ligase CUL7.
Subcellular location: Host nucleus {ECO:0000269|PubMed:3027978, ECO:0000269|PubMed:6096007}.
Interaction partners:
Sequence:
MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEIPTYGTDEWEQWWNAFNEENLFCSEEMPSSDDEATADSQHSTPPKKKRKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLDRMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDSGKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQGINNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPKDYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLSVYQKMKFNVAMGIGVLDWLRNSDDDDEDSQENADKNEDGGEKNMEDSGHETGIDSQSQGSFQAPQSSQSVHDHNQPYHICRGFTCFKKPPTPPPEPET
Protein: Interferon-induced transmembrane protein 2 (Dispanin subfamily A member 2c) (DSPA2c) (Fragilis protein 3) (Q99J93)
Organism: Mus musculus (Mouse)
Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q01629}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01629}. Lysosome membrane {ECO:0000250|UniProtKB:Q01629}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01629}. Late endosome membrane {ECO:0000250|UniProtKB:Q01629}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01629}.
Interaction partners:
- Interferon-induced transmembrane protein 3
- CD81 antigen
Sequence:
MSHNSQAFLSTNAGLPPSYETIKEEYGVTELGEPSNSAVVRTTVINMPREVSVPDHVVWSLFNTLFFNACCLGFVAYAYSVKSRDRKMVGDVVGAQAYASTAKCLNISSLIFSILMVIICIIIFSTTSVVVFQSFAQRTPHSGF
Protein: Fidgetin-like protein 1 (EC 3.6.4.-) (Q9VQN8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
Sequence:
MSDEQSSWRSKLLLICQQTRSSSESIHFAALKDHHARLQACESMEKAMKERCQKKITMSRRTKRGITHAGYLFEMPHNSVFEPECRGFYESCQQTEMASSDLQAPALEVSSTYPVQQAVKSRPEGQFPESRNNSTKKIDAQQYSSESSSQSGFGFRTAREQLIMDELKKKNRQATSEVDAVPTGMMNFRKKTLGGKRTVSSNFVSPVAQNDNSTSSRSSSIPPALAHLDSKMVDHILGESMHDFKPVAWEDIAGLESAKSTFLEAIIMPLRRPDLFTGVRCPPRGVLLFGPPGTGKTLIAKSIASQAKAKFFSINPSSLTSKWVGDAEKLVKTLFAVAAAHQPAIIFIDEVDSLLSKRSANENESTLRLKNEFLIHLDGAASNEEIRVLVIGATNRPQELDEAVRRRFVRRLYVPLPTREARQKIIEKLIHQVKHNLDVRQVIELAELTDGYSGADVDTLCRYASMAPLRSLTPDQMEVIETHQLPAVTMDDFKQALRVISKSVSSEDCKQFEAWNEIYGVRH
Protein: Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase) (Q16667)
Organism: Homo sapiens (Human)
Function: May play a role in cell cycle regulation. Dual specificity CC phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10669749}.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase 1
- Disks large-associated protein 5
- Cyclin-A2
- Cyclin-dependent kinase inhibitor 1
- G2/mitotic-specific cyclin-B1
- Cyclin-dependent kinase 6
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- G2/mitotic-specific cyclin-B2
- Baculoviral IAP repeat-containing protein 5
Sequence:
MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRDSQSRSVSR
Protein: Dye-decolorizing peroxidase AauDyP1 (EC 1.11.1.19) (EC 1.11.1.7) (AjP I) (Manganese-independent peroxidase I) [Cleaved into: Dye-decolorizing peroxidase AauDyP2 (EC 1.11.1.19) (EC 1.11.1.7) (AjP II) (Manganese-independent peroxidase II)] (I2DBY1)
Organism: Auricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae)
Function: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5.
Subcellular location: Secreted {ECO:0000305|PubMed:23111597}.
Interaction partners:
Sequence:
MRLSPVFVALLSGLLAADLGLARSVAPRVADSPAAVTGTRKTSLLKNVAGLPPVPSAAQVAATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A590UJW8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDSGSQLGSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPVSKLHFRVWSHQTLKSDVLLGTAALDIYETLKSNNMKLEEVVVTLQLGGDKEPTETIGDLSICLDGLQLESEVVTNGETTCSESASQNDDGSRSKDETRVSTNGSDDPEDAGAGENRRVSGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSATSESDGSSTGSLPPTNTNTNTSEGATSGLIIPLTISGGSGPRPLNPVTQAPLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATSQSKEFDPLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQGQLNEKPLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPRTGKSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE
Protein: MKIAA0079 protein (Q80U83)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
Sequence:
DQIGDALIMNVNQSAPPVPPYGQNQPIYPGYHQSSYGGQPGPAAPATPYGAYNGPVPGYQQAPPQGVPRAPPSSGAPPASAAQVPCGQTTYGQFGQGDIQNGPSSTAQMQRVPGSQQFGPPLAPVVSQPAVLQPYGPPPTSTQGFGSLPVNQANHVSSPPAPALPPGTQMTGPPVPPPPPMHSPQQPGYQLQQNGSFGPARGPQPNYESPYPGAPTFGSQPGPPQPLPPKRLDPDAIPSPQLNELPPQQKTRHRIDPDAIPSPIQVIEDDRNNRGSEPFVTGVRGQVPPLVTTNFLVKDQGNASPRYIRCTSYNIPCTSDMAKQAQVPLAAVIKPLARLPPEEASPYVVDHGESGPLRCNRCKAYMCPLMTFIEGGRRFQCSFCSCVNDVPPQYFQHLDHTGKRVDAYDRPELSLGSYEFLATVDYCKNNKFPSPPAFIFMIDVSYNAIRTGLVRLLCEELKSLLDYLPREGGAEESAIRVGFVTYNKVLHFYNVKSSLAQPQMMVVSDVADMFVPLLDGFLVNVSESRAVITSLLDQIPEMFADTRETETVFAPVIQAGMEALKAAECAGKLFLFHTSLPIAEAPGKLKNRDDRKLINTDKEKTLFQPQTGTYQTLAKECVAQGCCVDLFLFPNQYVDVATLSVVPQLTGGSVYKYACFQVENDQERFLSDLRRDVQKVVGFDAVMRVRTSTGIRAVDFFGAFYMSNTTDVELAGLDGDKTVTVEFKHDDRLNEENGALLQCALLYTSCAGQRRLRIHNLALNCCTQLADLYRNCETDTLINYMAKFAYRAVLNSPVKTVRDTLITQCAQILACYRKNCASPSSAGQLILPECMKLLPVYLNCVLKSDVLQPGAEVTTDDRAYVRQLVSSMDVAETNVFFYPRLLPLTKSPLDSTAEPPAVRASEERLSSGDIYLLENGLNLFVWVGASVQQGVVQSLFNVSSFSQITSGLSVLPVLDNPLSKKVRGLIDSLRAQRMRYMKLIVVKQEDKLEMLFKHFLVEDKSLSGGASYVDFLCHMHKEIRQLLS
Protein: Granulocyte-macrophage colony-stimulating factor (GM-CSF) (Colony-stimulating factor) (CSF) (P01587)
Organism: Mus musculus (Mouse)
Function: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Subcellular location: Secreted.
Interaction partners:
- Granulocyte-macrophage colony-stimulating factor receptor subunit alpha
- Cytokine receptor common subunit beta
- Granulocyte colony-stimulating factor
- Interleukin-1 beta
- Interleukin-3
- Interleukin-2
- Interleukin-3 receptor class 2 subunit beta
- Eotaxin
- Interleukin-1 alpha
- Interferon gamma
Sequence:
MWLQNLLFLGIVVYSLSAPTRSPITVTRPWKHVEAIKEALNLLDDMPVTLNEEVEVVSNEFSFKKLTCVQTRLKIFEQGLRGNFTKLKGALNMTASYYQTYCPPTPETDCETQVTTYADFIDSLKTFLTDIPFECKKPGQK
Protein: Heme-binding protein 1 (p22HBP) (Q9NRV9)
Organism: Homo sapiens (Human)
Function: May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12413491}.
Interaction partners:
- N-formyl peptide receptor 3
- N-formyl peptide receptor 2
Sequence:
MLGMIKNSLFGSVETWPWQVLSKGDKEEVAYEERACEGGKFATVEVTDKPVDEALREAMPKVAKYAGGTNDKGIGMGMTVPISFAVFPNEDGSLQKKLKVWFRIPNQFQSDPPAPSDKSVKIEEREGITVYSMQFGGYAKEADYVAQATRLRAALEGTATYRGDIYFCTGYDPPMKPYGRRNEIWLLKT
Protein: Carboxypeptidase Y (CPY) (EC 3.4.16.5) (O13849)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.
Subcellular location: Vacuole {ECO:0000269|PubMed:9209031}. Note=Lysosome-like vacuoles.
Interaction partners:
- Vacuolar protein sorting/targeting protein 10
- Uncharacterized carboxypeptidase C24C9.08
- Protein OS-9 homolog
- Uncharacterized derlin-like protein C365.08c
- Syntaxin pep12
- Alkaline phosphatase
- Invertase
- t-SNARE affecting a late Golgi compartment protein 1
- Vacuolar protein sorting-associated protein 27
- Cell division cycle protein 48
Sequence:
MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPFKHHELEEHEGPEHHRGPEDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHQGPKEKHNERPEQNMQSSHELLVIEAFADLINSVPVEEIAEEFSRFLDTLGIEYYGNIPVHIQENAPKDSSIPPLFEFDDDLELSDLTPEQFAYLEMLKAEGIDPMTAFRDQSHPAKPSNAQPADSSRPYAVFSQEENGEHVNLKAFPDHTLRVKDSKPESLGIDTVKQYTGYLDVEDDRHLFFWFFESRNDPENDPVVLWLNGGPGCSSLTGLFMELGPSSINIETLKPEYNPHSWNSNASVIFLDQPINTGFSNGDDSVLDTVTAGKDVYAFLNLFFAKFPQYAHLDFHIAGESYAGHYIPQFAKEIMEHNQGANFFVASGYEMEKQYINLKSVLIGNGLTDPLVQYYFYGKMACESPYGPIMSQEECDRITGAYDTCAKLITGCYQTGFTPVCIGASLYCNNAMIGPFTKTGLNIYDIREECRDQEHLCYPETGAIESYLNQEFVQEALGVEYDYKGCNTEVNIGFLFKGDWMRKTFRDDVTAILEAGLPVLIYAGDADYICNYMGNEAWTDALEWAGQREFYEAELKPWSPNGKEAGRGKSFKNFGYLRLYEAGHMVPFNQPEASLEMLNSWIDGSLFA
Protein: Zinc finger protein 219 (Q9P2Y4)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator. Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3'. Binds to the HMGN1 promoter and may repress HMGN1 expression. Regulates SNCA expression in primary cortical neurons. Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with SOX9 (By similarity). Plays a role in chondrocyte differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10819330, ECO:0000269|PubMed:14621294}.
Interaction partners:
- Non-histone chromosomal protein HMG-14
- Chromodomain-helicase-DNA-binding protein 5
- Transcriptional repressor p66-alpha
- Zinc finger protein 521
- Chromodomain-helicase-DNA-binding protein 3
- Cyclin-dependent kinase 2-associated protein 1
- Methyl-CpG-binding domain protein 3-like 1
- Transcriptional repressor p66-beta
- Zinc finger protein 423
- Methyl-CpG-binding domain protein 2
Sequence:
MEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFRTSAERERHLHILHRPWKCGLCSFGSSQEEELLHHSLTAHGAPERPLAATSAAPPPQPQPQPPPQPEPRSVPQPEPEPEPEREATPTPAPAAPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEEPEEEEEVVEAEEETWARGRSLGSLASLHPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGPPPEPPPPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER
Protein: Phosphatase and actin regulator 1 (Q2M3X8)
Organism: Mus musculus (Mouse)
Function: Binds actin monomers (G actin) and plays a role in multiple processes including the regulation of actin cytoskeleton dynamics, actin stress fibers formation, cell motility and survival, formation of tubules by endothelial cells, and regulation of PPP1CA activity. Involved in the regulation of cortical neuron migration and dendrite arborization.
Subcellular location: Cytoplasm. Synapse {ECO:0000250}. Nucleus. Note=Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import. {ECO:0000250}.
Interaction partners:
Sequence:
MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQARRATLLLPPTLMAASSEDDIDRRPIRRVRSKSDTPYLAEARISFNLGAAEEVERLAAMRSDSLVPGTHTPPIRRRSKFANLGRIFKPWKWRKKKSEKFKHTSAALERKISMRQSREELIKRGVLKEIYDKDGELSISNEDDSLENGQSLSSSQLSLPALSEMEPVPMPRDPCSYEVLQASDIMDGPDPGAPVKLPCLPVKLSPPLPPKKVLICMPVGGPELTLASYAAQKSSQQAVAQHHHTVLPSQMQHQLQYGSHGQHLPSSTGTLPMHPSGCRMIDELNKTLAMTMQRLESSEQRVPCSTSYHSSGLHSSDGITKAGPMGLPEIRQVPTVVIECDDNKENVPHEPDYEDSPCLYGREEEEEEEDEDDDASLYTSSLAMKVCRKDSLAIKLSNRPSKRELEEKNILPRQTDEERLELRQQIGTKLTRRLSQRPTAEELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELRERKILIRFSDYVEVADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRFHRP
Protein: PX domain-containing protein (D9PTP6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNSDEAICVDISDALSEREKVKYTVHTRTRLQEMKPETAVVREHEEFLWLHGTLEDNENYAGFIIPPAPPKPNFDSSREKLQKLGEGEATMTKEEFLKMKHDLEQDYLAQFKKTVAMHEVFLQRIAAHPVFKNDQNFRIFLQYENELSVRGKNKKEQVESFWKRFTQSADEVLLSGQKDVDEFFEKEKNYMVEYNIHIKEAAAKSEKLIAARKNVVASFSKIGDSFERIARGEPNKSLARTFAQGADAMFKLKKVESRSSNDEELKLGDTLHYFARDTQAAKDLLYRRMRCLANYEAANKNLERARAKNREIPKAEAEQSEACKKFEEITGLSKNELKELKTRRVQAFKKNLTDLAELEIKHSKAEISLLRDVVERLKSSQ
Protein: F-box protein SKIP24 (SKP1-interacting partner 24) (Q9CAZ0)
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.
Interaction partners:
- F-box protein SKIP22
- V-type proton ATPase subunit c''1
- F-box/kelch-repeat protein At5g49000
- F-box protein SKIP31
- Casein kinase II subunit alpha-4, chloroplastic
- SKP1-like protein 1A
- Transcriptional adapter ADA2b
Sequence:
MSANEIPDELWRKILEIGVKSSTFSYKDLCCISISSRRLFRLSCDDSLWDLLLVHDFPNHIVSASSSSESPTKFIYMTRFEREKERKLAAHRRALLRKESEISEWGRRIRELEARLSDEAERLQSSSLQFSDLLKVRQASVALNVWQPEVVRGRQKQMVEQNAVPVEGRLRALEMEMKLCKQQIMGLNRALREVKHRYDIAIKELESMKYHPLRDYKSIRNGDQGSNGKTKKLKTSINYSGDQVSNGKRRKLKTSIDCKFMNISHFSSCSSVTEKFYSYSPKIIHEYIPENLLVL
Protein: Large ribosomal subunit protein uL22 (50S ribosomal protein L22) (P61175)
Organism: Escherichia coli (strain K12)
Function: This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Interaction partners:
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS13
- Elongation factor Tu 1
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
- Large ribosomal subunit protein uL14
- DNA-directed RNA polymerase subunit alpha
Sequence:
METIAKHRHARSSAQKVRLVADLIRGKKVSQALDILTYTNKKAAVLVKKVLESAIANAEHNDGADIDDLKVTKIFVDEGPSMKRIMPRAKGRADRILKRTSHITVVVSDR
Protein: Eukaryotic translation initiation factor 5B (eIF-5B) (EC 3.6.5.3) (Translation initiation factor IF-2) (Q05D44)
Organism: Mus musculus (Mouse)
Function: Plays a role in translation initiation. Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome. The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12426392}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS19
- Eukaryotic translation initiation factor 5
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS17
- ATPase inhibitor, mitochondrial
Sequence:
MGKKQKNKSEDSTKDDTDLGALAAEIEGAGAAKEQEPQKSKGKKKKEKKKQDFDENDILRELEELSLEAQGIRADRDAAAVKPTENNEEESASKQDKKKKGQKGKKTSFDENDSEELEDKDSKSKKTARPNSEAPLSGSEDADDSNKLSKKGKKAQKSTKKRDGSEEDEDNSKRSKERSRVNSSGESGGESDEFLQSRKGQKKNQKNKSVPTVDSGNEDDDSSFKIKTVAQKKAEKKEREKKKRDEEKAKLRKMKEKEELEKGKKEQSKQREPQKRPEEEVLTLRGTPDTGAASEEKGDTAAALEDDNEGDKKKKDKKKKKTEKDEKEKEKKKGPSKSTVKAIQEALAKLKEEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEVTLRHLQAQGVEVPSKDSLPKKRPVYEDKKKKKTPQQLESKEVSETLEISAPVEAVDQGGPEKEETPPSVEPEEEEDTEDAGLDDWEAMASDEEREKEGNMIHIEVEENPEEEEEEEEEEEEEESEDEEEEGDSEGSDGDEEDCKLSDEKDSGKAGDTKPSKDASSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHGKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKDDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNSRDPIVIGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII
Protein: Coiled-coil domain-containing protein 8 (Q9H0W5)
Organism: Homo sapiens (Human)
Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Required for localization of CUL7 to the centrosome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24793695}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24793695}.
Interaction partners:
- Obscurin-like protein 1
- Cullin-7
- Ankyrin repeat family A protein 2
- Cellular tumor antigen p53
- Cullin-9
- F-box/WD repeat-containing protein 8
Sequence:
MLQIGEDVDYLLIPREVRLAGGVWRVISKPATKEAEFRERLTQFLEEEGRTLEDVARIMEKSTPHPPQPPKKPKEPRVRRRVQQMVTPPPRLVVGTYDSSNASDSEFSDFETSRDKSRQGPRRGKKVRKMPVSYLGSKFLGSDLESEDDEELVEAFLRRQEKQPSAPPARRRVNLPVPMFEDNLGPQLSKADRWREYVSQVSWGKLKRRVKGWAPRAGPGVGEARLASTAVESAGVSSAPEGTSPGDRLGNAGDVCVPQASPRRWRPKINWASFRRRRKEQTAPTGQGADIEADQGGEAADSQREEAIADQREGAAGNQRAGAPADQGAEAADNQREEAADNQRAGAPAEEGAEAADNQREEAADNQRAEAPADQRSQGTDNHREEAADNQRAEAPADQGSEVTDNQREEAVHDQRERAPAVQGADNQRAQARAGQRAEAAHNQRAGAPGIQEAEVSAAQGTTGTAPGARARKQVKTVRFQTPGRFSWFCKRRRAFWHTPRLPTLPKRVPRAGEARNLRVLRAEARAEAEQGEQEDQL
Protein: C-type lectin domain family 4, member a4 (Dendritic cell inhibitory receptor 2) (Q5YIR8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Lymphocyte antigen 75
Sequence:
MASEITYAEVRITNESDSLDTYSKCPAAPREKPIRDLRKPGSPSLLLTSLMLLLLLLAITFLVAFIIYFQKYSQLLEEKEAAKNIMYKELNCIKNGSLMEDKVWSCCPKDWKPFVSHCYFILNDSKASWNESEEKCSHMGAHLVVIHSQAEQDFITSNLNTSAGYFIGLLDAGQRQWRWIDQTPYNKSATFWHKGEPNQDWERCVIINHKTTGWGWNDIPCKDEHNSVCQVKKIYL
Protein: Ladybird late, isoform C (A0A0B4KH37)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MPQRTPSPANSDVSVGSPSPPPLRSLNMKRLRLLRSPISLEHDRQKSSPVRVKSFSIADILGRGHEEDRVEKKPERIAIPNALPGVPAPLALINERLQIPLVPNCPPPAALHTFLSPALLHSYEQRLAWDYQRQLQEHFQAQAQLLRQMTLNPAIIASEDGSSERSQRSSSSNGSTECCSPTQAEKVEKRSQEDRMEVPKKSPEEQPKGASKSSGDTPLDALFQLSTKNFDEEQDPATLNIFATRSNPKKKRKSRTAFTNQQIFELEKRFLYQKYLSPADRDEIAGGLGLSNAQVITWFQNRRAKLKRDMEELKKDVQCEKIPDQSADPNRSHHNHPHYHQQHQHYAHMQSIGSDRDMDKDRCREKEKDKDKEELRMLKLMTLMRYSDGKLLYQQPPASYLPIPHRQNAD