wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase nu (EC 2.7.7.7) (Q7Z5Q5)
Organism: Homo sapiens (Human)
Function: DNA polymerase with very low fidelity that catalyzes considerable misincorporation by inserting dTTP opposite a G template, and dGTP opposite a T template. Is the least accurate of the DNA polymerase A family (i.e. POLG, POLN and POLQ). Can perform accurate translesion DNA synthesis (TLS) past a 5S-thymine glycol. Can perform efficient strand displacement past a nick or a gap and gives rise to an amount of product similar to that on non-damaged template. Has no exonuclease activity. Error-prone DNA polymerase that preferentially misincorporates dT regardless of template sequence. May play a role in TLS during interstrand cross-link (ICL) repair. May be involved in TLS when genomic replication is blocked by extremely large major groove DNA lesions. May function in the bypass of some DNA-protein and DNA-DNA cross-links. May have a role in cellular tolerance to DNA cross-linking agents. Involved in the repair of DNA cross-links and double-strand break (DSB) resistance. Participates in FANCD2-mediated repair. Forms a complex with HELQ helicase that participates in homologous recombination (HR) repair and is essential for cellular protection against DNA cross-links.
Subcellular location: Nucleus {ECO:0000269|PubMed:12794064}.
Interaction partners:
- Helicase POLQ-like
- DNA polymerase alpha catalytic subunit
- Fanconi anemia group D2 protein
- Proliferating cell nuclear antigen
- DNA-directed DNA/RNA polymerase mu
- Fanconi anemia group I protein
- Fanconi anemia group M protein
- Fanconi anemia group A protein
- E3 ubiquitin-protein ligase RAD18
- Fanconi-associated nuclease 1
Sequence:
MENYEALVGFDLCNTPLSSVAQKIMSAMHSGDLVDSKTWGKSTETMEVINKSSVKYSVQLEDRKTQSPEKKDLKSLRSQTSRGSAKLSPQSFSVRLTDQLSADQKQKSISSLTLSSCLIPQYNQEASVLQKKGHKRKHFLMENINNENKGSINLKRKHITYNNLSEKTSKQMALEEDTDDAEGYLNSGNSGALKKHFCDIRHLDDWAKSQLIEMLKQAAALVITVMYTDGSTQLGADQTPVSSVRGIVVLVKRQAEGGHGCPDAPACGPVLEGFVSDDPCIYIQIEHSAIWDQEQEAHQQFARNVLFQTMKCKCPVICFNAKDFVRIVLQFFGNDGSWKHVADFIGLDPRIAAWLIDPSDATPSFEDLVEKYCEKSITVKVNSTYGNSSRNIVNQNVRENLKTLYRLTMDLCSKLKDYGLWQLFRTLELPLIPILAVMESHAIQVNKEEMEKTSALLGARLKELEQEAHFVAGERFLITSNNQLREILFGKLKLHLLSQRNSLPRTGLQKYPSTSEAVLNALRDLHPLPKIILEYRQVHKIKSTFVDGLLACMKKGSISSTWNQTGTVTGRLSAKHPNIQGISKHPIQITTPKNFKGKEDKILTISPRAMFVSSKGHTFLAADFSQIELRILTHLSGDPELLKLFQESERDDVFSTLTSQWKDVPVEQVTHADREQTKKVVYAVVYGAGKERLAACLGVPIQEAAQFLESFLQKYKKIKDFARAAIAQCHQTGCVVSIMGRRRPLPRIHAHDQQLRAQAERQAVNFVVQGSAADLCKLAMIHVFTAVAASHTLTARLVAQIHDELLFEVEDPQIPECAALVRRTMESLEQVQALELQLQVPLKVSLSAGRSWGHLVPLQEAWGPPPGPCRTESPSNSLAAPGSPASTQPPPLHFSPSFCL
Protein: Probable lysophospholipase 5 (EC 3.1.1.5) (Phospholipase B) (Q9Y7N6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the release of fatty acids from lysophospholipids.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase gde1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase ptl3
Sequence:
MKLSSFGLFLALQLLPALGLPSRIDEVDVSDPELIGLLKPDNVDKPANSIPLSKRSTSPSYAPYTVACPSGSLLRPASDGLSTGEQEFVDKRVSKVNSALESFISKTGLKIDTKSVLNDTDGPRLGIAISGGGFPAMLTGAGAINAFDARNGNTTSLGGILQSSMYLTGLSGGSWLVGSVAVNNFANITFLHDDVWNLDHSLFAPYDDAFENFYIYQEWFEQVLQKKNAGFNVSITDLWGRALALKLVNPLTGGANTTFSSVTNETWFQDGEFPFPIIIADNVIEGETVIPLNDTVFEFTPIEFGTWDTGVESFIPMEYTGTHLINGIPLNESCVRNFDNAGFLMGTSSNVFSGILPATNASLTASNNTFNNAVLSFLEMLAEDQLDVGLYPNPYQGYGNASNTTTTNPLEPYPIIELIDGGSDSEGIPFWPLLHPQRDVDVIFAIDGGYQSATSGWPDGSSLVSTYERVLATNSSGVRGFPYIPDTNTFLALGLNTHPTFFGCDGRNTTAGNHTVNDDTPPLVVYFPNYPWTMYANVTTYTVQLEDTLSSGMIENAAVAATQNNSDSFAVCVACALVQRSLERKNMSTPSQCASCFNQYCWNGTIASTTVTTYAPTVLSAKI
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (E9PNI7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGCFPTHLMPRPRVAMAEAEAGVAVEVRGLPPAVPDELLTLYFENRRRSGGGPVLSWQRLGCGGVLTFREPADAERVLAQADHELHGAQLSLRPAPPRAPARLLLQGLPPGTTPQRLEQHVQALLRASGLPVQPCCALASPRPDRALVQLPKPLSEADVRVLEEQAQNLGLEGTLVSLARVPQARAVRVVGDGASVDLLLLELYLENERRSGGGPLEDLQRLPGPLGTVASFQQWQVAERVLQQEHRLQGSELSLVPHYDILEPEELAENTSGGDHPSTQGPRATKHALLRTGGLVTALQGAGTVTMGSGEEPGQSGASLRTGPMVQGRGIMTTGSGQEPGQSGTSLRTGPMGSLGQAEQVSSMPMGSLEHEGLVSLRPVGLQEQEGPMSLGPVGSAGPVETSKGLLGQEGLVEIAMDSPEQEGLVGPMEITMGSLEKAGPVSPGCVKLAGQEGLVEMVLLMEPGAMRFLQLYHEDLLAGLGDVALLPLEGPDMTGFRLCGAQASCQAAEEFLRSLLGSISCHVLCLEHPGSARFLLGPEGQHLLQGLEAQFQCVFGTERLATATLDTGLEEVDPTEALPVLPGNAHTLWTPDSTGGDQEDVSLEEVRELLATLEGLDLDGEDWLPRELEEEGPQEQPEEEVTPGHEEEEPVAPSTVAPRWLEEEAALQLALHRSLEPQGQVAEQEEAAALRQALTLSLLEQPPLEAEEPPDGGTDGKAQLVVHSAFEQDVEELDRALRAALEVHVQEETVGPWRRTLPAELRARLERCHGVSVALRGDCTILRGFGAHPARAARHLVALLAGPWDQSLAFPLAASGPTLAGQTLKGPWNNLERLAENTGEFQEVVRAFYDTLDAARSSIRVVRVERVSHPLLQQQYELYRERLLQRCERRPVEQVLYHGTTAPAVPDICAHGFNRSFCGRNATVYGKGVYFARRASLSVQDRYSPPNADGHKAVFVARVLTGDYGQGRRGLRAPPLRGPGHVLLRYDSAVDCICQPSIFVIFHDTQALPTHLITCEHVPRASPDDPSGLPGRSPDT
Protein: Sodium channel protein (Q20JQ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
Interaction partners:
Sequence:
MAAILFPPGPDSLHRFTRESLAGIEQRIAEEEARNAKRYQEDRGDVEPPKPRADLEAGKQLPRIFGDIPSALVGVPLEDIDPFYFQNRRTFIVLNKGKAIFRFSATSALYIFSPFHPIRRASIRILVHSLFSLFIMCTILTNCCFMAMSEPAQWAKYVEYTFTGIYTFESLIKILARGFCIGPFTFLRDPWNWLDFSVILMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLADVMILTVFCLSVFALIGLQLFMGNLRQKCVRSASQCLNTTLPTYNNSTFICNNRSWASLEEFFNNEDNFFKVEGAKDALICGNASDAGKCPDGFECLKTGRNPNYGYTSFDTFGWAFLSLFRLMTQDYWENLYHHTLRSAGKAYMVFFVVVIFLGSFYLVNLILAVVAMAYEEQNQATIAEALQKEQEFQLAMEQLKKEQQAAQKAQETESILTADVSPFSTQDKAKLERRKSSRPLSEGTGEDKPAKLDPIEGIKQTHSLLVRTLSLRARRESAVSIFNFRPVNKDSELDFADDEFSNHGDSDSRGGALALPWSRRRTSAQSSCSHSSQFFFPSFNINGKLMVAVEQNGISSQGPLTPMTPLTPLPACTMEKLKEESGQNSSNELSSMLLPQLPPEGRDRALSATSYITDAMEELEEAQQKCHPCWYVFAHKYLVWTCSPRWLKVKEWVKIMVMDPFLDLAITICIVLNTLFMALEHYPMTDEFNRMLSVGNLVFTGIFTAEMVLKIIALDPYYYFQQGWNIFDSLIVSLSLMELGLSNVEGLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYDLCVCKISKDCTLPRWHMKDFFHSFLIVFRVLCGEWIETMWDCMEVAGQPLCILVFMLVMVIGNLVVLNLFLALLLSSFSADNLSAPDEDGEMNNLQIAIARIQRGMLWLRQALCDFFNGNFKRRRQKAKEAKAMLKLKRLTQQAHWAEGNGTAGVIERSSGAGSGEDDSYMTNPNLTISVPIAPGESDVEFPEEEDEEEDEEEEASASSDEEPEPCKPRDDTSLSEGSTIDLRKPGEEEDEYSEMAEEAMDPENCFPDVCVRHFKCCDINTSEGLGRAWWRLRKTCYQIVEHSWFETFIIFMILLSSGALAFEDIYIDQRKVVKVILEYADKIFTYIFILEMSLKWIAYGFRKYFTNYWCWLDFLIVDVSLVSLVANTLGYSDFAAIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCVNRTGFIYNSSDINNRSECLEMNSTQYYWTKVKVNFDNVGAGYLALLQVATFKGWMEIMYAAVDSRAVEEQPIKENSLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKRKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPPNPVQGFFFDLVSKQAFDILIMLLIILNMVTMMVETDEQSPSIKHILDCINLVFIVIFTSECILKIIALRCYFFTVSWNIFDFVVVILSIVGIVLADIIEKYFVSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMANFAYVKKQGGIDDMFNFETFGNSMICLFQITTSAGWDNLLSPILNTPPEECDPEIPHTGTNARGNCGKPSVGITFFVTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFEMFYEVWEKFDPEATQFIEYLKLSDFADTLSEPLRIGKPNKIKLISMDLPMVSGDKIHCLDILFAFTKRVLGESGEMDALKQQMEEKFMMANPSKISYEPITTTLRRKQEEVSAIMIQRSYRRHLIRRQLKQASLLYRQMTMPDADKAGDSSPESQGLIVSMIMENYATEAEITISATSSPPSYDSVTRATSEIFHALIPEETNEILSEHLADAEKESETFL
Protein: N-acetyltransferase domain-containing protein (Q7D9D7)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MHGARTGVSFYAYAMTDHDQTAARREIADALLAALERRHEVADAIVEAANKAAAVEAIVNLLGTSHLAAEAVMSMSFDQLTQDARTKIIAELDDLNKQLSFTVKERPASSGEGLELRPFSPDEDRDIFARRTEEMGAAGDGSGGPAGSVDDEIRAAQKRVDDEEAAWFVAVDSGVKVGMVFGELVHGEVDVRIWIHPDHRKKGYGTAALRKSRSEMAWAFPAVPMVARAPAAQPAQPGSAGR
Protein: NotI restriction endonuclease (Q2I6W2)
Organism: Nocardia otitidiscaviarum
Interaction partners:
Sequence:
MRSDTSVEPEGANFIAEFFGHRVYPEVVSTEAARNDQATGTCPFLTAAKLVETSCVKAETSRGVCVVNTAVDNERYDWLVCPNRALDPLFMSAASRKLFGYGPTEPLQFIAAPTLADQAVRDGIREWLDRGVHVVAYFQEKLGGELSISKTDSSPEFSFDWTLAEVESIYPVPKIKRYGVLEIQTMDFHGSYKHAVGAIDIALVEGIDFHGWLPTPAGRAALSKKMEGPNLSNVFKRTFYQMAYKFALSGHQRCAGTGFAIPQSVWKSWLRHLANPTLIDNGDGTFSLGDTRNDSENAWIFVFELDPDTDASPRPLAPHLEIRVNVDTLIDLALRESPRAALGPSGPVATFTDKVEARMLRFWPKTRRRRSTTPGGQRGLFDA
Protein: Periplasmic nitrate reductase, electron transfer subunit (Diheme cytochrome c NapB) (P0ABL3)
Organism: Escherichia coli (strain K12)
Function: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.
Subcellular location: Periplasm {ECO:0000269|PubMed:10234835, ECO:0000269|PubMed:10548535, ECO:0000269|PubMed:17130127}.
Interaction partners:
- Ferredoxin-type protein NapG
- Cytochrome c-type protein NapC
- Ferredoxin-type protein NapH
- Periplasmic nitrate reductase
- Chaperone NapD
- Ferredoxin-type protein NapF
- Cytochrome c-552
- Cytochrome c-type protein TorC
- Nitrite reductase small subunit
- Respiratory nitrate reductase 1 alpha chain
Sequence:
MKSHDLKKALCQWTAMLALVVSGAVWAANGVDFSQSPEVSGTQEGAIRMPKEQDRMPLNYVNQPPMIPHSVEGYQVTTNTNRCLQCHGVESYRTTGAPRISPTHFMDSDGKVGAEVAPRRYFCLQCHVPQADTAPIVGNTFTPSKGYGK
Protein: PBP1-interacting protein XAC1 (EXpression ACtivator 1) (Q57Y88)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Involved in post-transcriptional regulation of gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32532821}.
Interaction partners:
- Uncharacterized protein
Sequence:
MSKAPSQPAKKWMSARTLAKSEDATNRKSNTAAPASQPSQQPASVMHERPTPPPPAPVQLPQSVFFERQEAVDTLSNLYRNAQSVKKIETGPAAFEARDISKVHEELMDCLRPAAAA
Protein: Cilia- and flagella-associated protein 46 (A8ICS9)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: As part of the central apparatus of the cilium axoneme plays a role in cilium movement and thereby cell motility.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:20421426, ECO:0000269|PubMed:22573824}.
Interaction partners:
Sequence:
MAQPETLHQVLAQPADASRVKQLQTVHEAITASLSGQQPGARVGLETLVLCAEAALKVGSLDVAHDCLERYFLEQRRYTVGMAPVELRDQYLCRAHFARGLLVSERSKGLKGKALIDGTLEGVKHVMAGLEVAAANQPRYQFLVYNASVHHWRVVAPLHRDGLRHHLLASTDRVVQALDKVPGHEEWKVRIYTALALCQSDAATVAAAQAEAAGGKAPAKGGGGAAATHDDAAKTLQRAYDTAAAAKLTELQKDVARLQVHLATLAAAAGGKGAKAGGGGAAGGAGKPGAKGAAAALDEEGALRLIQAVLTGRPDRAVAEQQLREAVAKVDPKGPDGPVKGALLRPVSRAAWAAALAGLPELAERWASRAAASSDSGPRTWSDMTRVQLALQALGPAGDTSLAPVVVAAHVKALEQLEDVLTTFTKLADVEGIHAAARLAWNAGLLLLQPGLRKHVKRAFNAAARALAVAASPLTRLRAALHLEAGKCDAAEEALIKAGQEVGKALALDYLPPPAEAAAVPWLARPLDRWAAPLARALALRTSAEPANPEEEAVSLIERSKESRNPAIKSDLLARAREKLRDLPHPPPPAPTDPPGPDRDAAHAAARRRTAVWAELMRSAASSRMDEHVLAAAPHALCVSWDPAVDREMVLLQAQLAHYEAEAAISALRRRRADISPPTRPSPPEVDGEGVRQPPATTEQLQELVVQASVRSMRGAMSVNEPWLTLNNAVQLYNAALPLMQQHRYADLYRWLRPVAEALVALPVADSDGPLAVAVAEALGRAAEHRLLLATLRAKAARDAGQELEDDDDEDSLDEDGNPPPAGDAGPHFNRRSPAYKPLPDARVAASGLDPRGFPALARLLASIGTVTAVAEAALERAGGASTQGLLEMYARLQQYRGVSSGLPAGAAAASAATSRVVSAIEALSSANRVNEEKQPAGAGAEKGGGDKGRKPHGSLAADAAAAIALLRALPGGPPLELWAKMARAVADAGVWPAALECSAAALAALPGAGRDLDVLRLEAPSDVPEMTPAGWFWASVALSVRAAALLTLVDLPSQGAATALTVRREALLHAAQAARCAAFVNKADLCESACRVAWNAALPFTTKPLLRAALIRPLGTAVEALNRVGPADKGFQVRMNCLYVESLAAAKRWGDAVAACDAASRAVKSRSLHRPLMGWKAACLAMLGKNVNAEMTKVKEHPPEAQAYAWSVLSHHSAARYDQIAAHKAAGEAVEHHGWLKAVALAGYAEWLLSSSDDKEAAEDALLAAADALLEFDTGDLDGDGTDDEDDATKAKPRSRSGGGSSSGRAGGGFRRVLSRSYSRGGGGSADGARPSEGGEGAGPAAPDPNRVPEELGSTHLERLARLYVMACQAAPNATDHTDYMLAAHHNFMRLLTQALHSAAHTAFVAARDSYNGEVAAAALEGRDPPPETPLPKPYAVVPDTLIGWGTWQITPELLETLASDAATGAVTALSRELLPQAELTLAYLELLQACLRARGYHCHCLGLAQLQRVLARMVLRDEGMYVATSLGLVAALDELGLSREAGEVEAALGDVACIGPQEEAQAAEQAALADLVLAAAGKLEAARPRSALAVGRLSFLAGGVRRANNAANAAAAAPLPPVAAASQAAAAADAAAAASFTAAGGGRGGRESPSPHDDGIHYIGGPAPGDSHGQLPEWMEDAARELGNVDLAGSAGGLLSHVSGQLLLRPFTLHDVWLKKGDYLLRRGHYAAARQLLSRARAHAADCGNREAEARCLLALSRTELAAHNPVEAVALVQAAQRFGGDIDFWAELLVQYVDCRLAGAHSTTSDAREALQGGIAMFLALARDDRAAEKPASAAGAVLRVRLARLLLTDMEMLRGQGVSTWRKSYDGAVTLVNQAIMALAAREAGLPHIEALLVQAELMLAEPTHIKDLRPRLKKVEKVLLAAEEMAVRFHAEATPRDLAPRCVTPTARLLACVRCRLAEVQLAAAEERERLAGADREKARPKFPHMRGKRDVQVVIDFIDEAGGAPPAPPGLLPEDSALALATGAAALVAAAPRDRARALLIAGRCLAFKFMMAAPEALDPLRPFVPPPKPPGAPKRPPAGAEEEEDEEGPDTAAADAAAEAAEAAATPEGAAALRLQAQAAAMLSSALASATSVQDWALGEQCALALSTLYGQLSPGLACRSLAAAQACRAAAGGQALLRAAAPAQQPEVLALAQRDKLSEVLPAPQDNVHYSALRRMLSGLKGAAARLDAAAAPPVEQQLAALPQDLRVLMLYLSPDGGRLYAAALNIPDATAEPTPPLNAEKSKKKTDASAPAAAGPRLSLLHVVEVDPAAVEALVAECRAYRRGVERTLREAIASAAAKGVGVPPEDDRPDSPSKKGKKPGSATKRPGSKQGPKSGPGAAAAAAAAAAAAGEAGKVQVFDSRLNEEWSGILEQFEEWLAPLAPWLEAAVPALPLPPPGSPDGKKEKKDKKEAAGPTKHKVALLLDPALQSLPWEAARHLATTCSEVSRSPSLQALAACHTLPRADSAAASEHAAAAAAAPAALPPLDLGRLTVIVDPRHECSTAQQARGPYTAQLIPALSAPELTQVLPAASWWGPGGPGGGLEGVPGRAPSPDTYASLLAGQATGGPCTGLLFLGVGRFAAHVPPAVLASAPLGGCEAALLFDRCNTDDAYWAQLYRDNRKSAEQRRLESPGRVATLLLAKGVRTVLVMSAAAPPAAVVKLMHGVMAGLAAGRVLGEVVYSLLTGGGGSGGAGAGVLDEFELAHLRACLQVWGAPGLLGAVLTQGNKAAKGAKK
Protein: Small ribosomal subunit protein eS10A (40S ribosomal protein S10a) (Q9VB14)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein eS7
- 40S ribosomal protein S27
- 60S ribosomal protein L27
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
Sequence:
MFIPKANRVAIYEYLFKEGVLVAKKDSPIQKHSELDKIPNLQVIKVMQSLNSRGWVKEQFAWRHFYWLLTNEGIEELRRYLHLPPEIVPSTLTQTTRSNAVRPRGGPGGPGGGFGGASKTDDDRSNYRRGPGAYGMDKKGDVGAGTGRVEYRGGFGRASRYDN
Protein: SH2B adapter protein 2 (Adapter protein with pleckstrin homology and Src homology 2 domains) (SH2 and PH domain-containing adapter protein APS) (Q9Z200)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis (By similarity). Involved in stimulation of glucose uptake by insulin. Involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Induces cytoskeletal reorganization and neurite outgrowth in cultured neurons.
Subcellular location: Cytoplasm. Membrane. Note=Recruited to the membrane by binding to an autophosphorylated receptor after receptor stimulation by its extracellular ligand.
Interaction partners:
- E3 ubiquitin-protein ligase CBL
- Insulin receptor
- High affinity nerve growth factor receptor
- Growth factor receptor-bound protein 2
- E3 ubiquitin-protein ligase CBL-B
- BDNF/NT-3 growth factors receptor
- NT-3 growth factor receptor
- Tyrosine-protein kinase JAK2
Sequence:
MNGATPGSAAAPAPVPDWRQFCELHAQVAAVDFAHKFCRFLRDNPTYDTPDAGTSFSRHFAANFLAVFSEEVRRVLGTAADTMEPEPAVTSVTSALKTATYGHSRSSEDVSAHVATKARVRKGFSLRNMSLCVVDGVRDLWHRRASPEPEGGATPKTTEPVSEPRDKWTRRLRLARTLAAKVELVDIQREGALRFMVADDAASGPGGTAQWQKCRLLLRRAVAGERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTGLSCARGGCLASRVTSCSCELLTEADMPRPPETMTAVGAVVTAPHGRARDTVGESLAHVPLETFLQTLESSGGVSESNNTGDEGAELDPDAEAELELSDYPWFHGTLSRVKAAQLVLAGGPRSHGLFVIRQSETRPGECVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVFDMLRHFHTHPIPLESGGSADITLRSYVRAQGPPPDPGPAPNTAAPVPACWTEPAGQHYFSSLATATCPPTSPSNGAGASSSSGSSSSATSVPPRPAEGPLSARSRSNSTEHLLEAASGATEEPADATLGRARAVENQYSFY
Protein: MOB kinase activator-like 1 (Mob as tumor suppressor protein 1) (Dmob1) (Mps one binder kinase activator-like 1) (Q95RA8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Coactivator of Warts (Wts) kinase in the Hippo/SWH (Sav/Wts/Hpo)signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki)oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Mats is essential for early development and is required for proper chromosomal segregation in developing embryos.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm, cytosol. Cell membrane. Note=Colocalizes with wts and cyclin E at the centrosome.
Interaction partners:
- Serine/threonine-protein kinase Warts
- Serine/threonine-protein kinase hippo
- Scaffold protein salvador
- Serine/threonine-protein kinase tricornered
- Transcriptional coactivator yorkie
- Protein phosphatase PP2A 55 kDa regulatory subunit
- Serine/threonine-protein phosphatase PP2A
- Cell division cycle 14, isoform A
Sequence:
MDFLFGSRSSKTFKPKKNIPEGTHQYDLMKHAAATLGSGNLRNAVALPDGEDLNEWVAVNTVDFFNQINMLYGTITEFCTEETCGIMSAGPKYEYHWADGLTVKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFHSSAKTILKRLFRVYAHIYHQHFTEVVTLGEEAHLNTSFKHFIFFVQEFNLIERRELAPLQELIDKLTAKDERQI
Protein: Minor capsid protein VP2 (Minor structural protein VP2) (P03093)
Organism: Simian virus 40 (SV40)
Function: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release. Isoform VP2 may repress SP1 activation of the SV40 early promoter, via specific protein-protein and protein-DNA interactions.
Subcellular location: [Isoform VP2]: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:1847270}. Host endoplasmic reticulum {ECO:0000269|PubMed:17189196}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17189196}. Note=Following host cell entry, the virion enters into the endoplasmic reticulum through a calveolar-dependent pathway. Then, isoform VP2 integrates into the endoplasmic reticulum membrane and participates in the translocation of viral DNA to the nucleus. Shortly after synthesis, a nuclear localization signal directs isoform VP2 to the cell nucleus where virion assembly occurs. {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:1847270}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:1847270}. Host endoplasmic reticulum {ECO:0000269|PubMed:17189196}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:25631089}. Note=Following host cell entry, the virion enters into the endoplasmic reticulum through a calveolar-dependent pathway. Then, isoform VP3 integrates into the endoplasmic reticulum membrane and participates in the translocation of viral DNA to the nucleus. Shortly after synthesis, a nuclear localization signal directs isoform VP3 to the cell nucleus where virion assembly occurs. {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:1847270}.; SUBCELLULAR LOCATION: [Isoform VP4]: Host nucleus {ECO:0000269|PubMed:17658947}.
Interaction partners:
Sequence:
MGAALTLLGDLIATVSEAAAATGFSVAEIAAGEAAAAIEVQLASVATVEGLTTSEAIAAIGLIPQAYAVISGAPAAIAGFAALLQTVTGVSAVAQVGYRFFSDWDHKVSTVGLYQQPGMAVDLYRPDDYYDILFPGVQTFVHSVQYLDPRHWGPTLFNAISQAFWRVIQNDIPRLTSQELERRTQRYLRDSLARFLEETTWTVINAPVNWYNSLQDYYSTLSPIRPTMVRQVANREGLQISFGHTYDNIDEADSIQQVTERWEAQSQSPNVQSGEFIEKFEAPGGANQRTAPQWMLPLLLGLYGSVTSALKAYEDGPNKKKRKLSRGSSQKTKGTSASAKARHKRRNRSSRS
Protein: Bifunctional dTDP-4-dehydrorhamnose 3,5-epimerase/dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) (EC 5.1.3.13) (dTDP-L-rhamnose synthase) (Q9LQ04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional enzyme involved in dTDP-beta-L-rhamnose biosynthesis. Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-4-keto-alpha-D-glucose to form dTDP-4-keto-beta-L-rhamnose and its reduction to yield dTDP-beta-L-rhamnose. Can form UDP-beta-L-rhamnose from UDP-6-deoxy-4-keto-alpha-D-glucose, but cannot convert GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose.
Interaction partners:
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- ADP-glucose pyrophosphorylase family protein
- Probable mannose-1-phosphate guanylyltransferase 2
- Probable mannose-1-phosphate guanylyltransferase 3
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3
- ADP-glucose pyrophosphorylase family protein
- Mannose-1-phosphate guanylyltransferase 1
- NAD
- GDP-mannose 4,6 dehydratase 2
Sequence:
MVADANGSSSSSFNFLIYGKTGWIGGLLGKLCEAQGITYTYGSGRLQDRQSIVADIESVKPSHVFNAAGVTGRPNVDWCESHKVETIRTNVAGTLTLADICREKGLVLINYATGCIFEYDSGHPLGSGIGFKEEDTPNFTGSFYSKTKAMVEELLKNYENVCTLRVRMPISSDLTNPRNFITKIARYEKVVDIPNSMTILDELLPISIEMAKRNLTGIYNFTNPGVVSHNEILEMYRDYIDPSFTWKNFTLEEQAKVIVAPRSNNELDATKLKTEFPELMSIKESLIKFVFEPNKKTEVKA
Protein: Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein) (Q9Z0F6)
Organism: Mus musculus (Mouse)
Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99638}.
Interaction partners:
- Cell cycle checkpoint protein RAD1
- Cell cycle checkpoint protein RAD17
- Checkpoint protein HUS1
- DNA topoisomerase 2-binding protein 1
- ATR-interacting protein
- Serine/threonine-protein kinase ATR
- Replication factor C subunit 2
- Serine-protein kinase ATM
- Replication factor C subunit 4
- Checkpoint protein HUS1B
Sequence:
MKCLITGGNVKVLGKAVHSLSRIGDELYLEPLKDGLSLRTVNSSRSAYACFLFAPLFFQQYQAASPGQDLLRCKILMKAFLSVFRSLAIVEKSVEKCCISLSGSHSHLVVQLHCKYGVKKTHNLSFQDCESLQAVFDPASCPHLLRTPARVLAEAVLSFPLALTEVTLGIGRGRRVILRSYQEEEADSTSKAMVTETSIGDEDFQQLHAPEGIAVTFCLKEFRGLLSFAESANLPLTIHFDVPGRPVIFTIEDSLLDAHFVLATLLEQDSCSQGPCSPKPHQPVPQKQAHSTPHLDDFTSDDIDCYMIAMETTGGNEGSGAQPSTSLPPVSLASHDLAPTSEEEAEPSTVPGTPPPKKFRSLFFGSILAPVHSPQGPNPVLAEDSDGEG
Protein: Transmembrane protein 267 (Q0VDI3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MASETEKTHALLQTCSTESLISSLGLGAFCLVADRLLQFSTIQQNDWLRALSDNAVHCVIGMWSWAVVTGIKKKTDFGEIILAGFLASVIDVDHFFLAGSMSLKAALTLPRRPFLHCSTVIPVVVLTLKFTMHLFKLKDSWCFLPWMLFISWTSHHIRDGIRHGLWICPFGKTSPLPFWLYVIITSSLPHICSFVMYLTGTRQMMSSKHGVRIDV