wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (D4A584)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|PIRNR:PIRNR000632}.
Interaction partners:
- Plexin-A1
- Dihydropyrimidinase-related protein 5
- Dihydropyrimidinase-related protein 2
- Plexin-A2
- Plexin-A3
- Plexin-A4
Sequence:
MGFSSELCSPQGHGAVQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSWSSGPDSPVSQSWAEITSQTENLSRVLRQHAEDLNSGPLSKLSVLIRERQHLRKTYNEQWQQLQQELTKTHSQDIEKLKSQYRTLTRDSAQARRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHYHQFMLPGLLQSLQDLHEEMAGILKDILQEYLEISSLVQDDVASIHRELAAAAARIQPEFEYLGFLRQYGSAPDVPPCVTFDVSLLEEGEQLEPGDLQLNELTLESVQHTLTSVTDELAVATKEVLSRQEMVSQLQRELQCEEQNTHPRERVQLLGKRQVLQEAMQGLQVALCNQDKLQAQQELLQSKMEQLGTGEPPAVPLLQDDRHSTSSTEQERDGGRTPTLEIIKSHFSGIFRPKFSIPPPLQLVPEVQKPLHEQLWYHGAIPRAEVAELLTHSGDFLVRESQGKQEYVLSVLWDGQPRHFIIQSSDNLYRLEGDGFPSIPLLITHLLSSQQPLTKKSGVVLFRAVPKDKWVLKHEDLVLGEQIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFLQEARILKQYNHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGIYAASAGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLTNQQTREFVEKGHRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTICQELQSIRKRHR
Protein: Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip) (Q6WCQ1)
Organism: Homo sapiens (Human)
Function: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14506264, ECO:0000269|PubMed:16257966}. Note=Colocalizes with F-actin.
Interaction partners:
- Transforming protein RhoA
- Protein phosphatase 1 regulatory subunit 12A
- Inorganic pyrophosphatase
- cGMP-dependent protein kinase 1
- Protein phosphatase 1 regulatory subunit 12C
Sequence:
MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEGRTGQKFSLCILTPEKEHFIRAETKEIVSGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKVAVTSSSSSSSSSSSIPSAEKVPTTKSTLWQEEMRTKDQPDGSSLSPAQSPSQSQPPAASSLREPGLESKEEESAMSSDRMDCGRKVRVESGYFSLEKTKQDLKAEEQQLPPPLSPPSPSTPNHRRSQVIEKFEALDIEKAEHMETNAVGPSPSSDTRQGRSEKRAFPRKRDFTNEAPPAPLPDASASPLSPHRRAKSLDRRSTEPSVTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEIDLSACYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVHPTTAPDVTSSLPEEKNKSSCSFETCPRPTEKQEAELGEPDPEQKRSRARERRREGRSKTFDWAEFRPIQQALAQERVGGVGPADTHEPLRPEAEPGELERERARRREERRKRFGMLDATDGPGTEDAALRMEVDRSPGLPMSDLKTHNVHVEIEQRWHQVETTPLREEKQVPIAPVHLSSEDGGDRLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSVNSDVEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEATGSPLAQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPDSATVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDT
Protein: Claudin-3 (Rat ventral prostate.1 protein) (RVP1) (Q63400)
Organism: Rattus norvegicus (Rat)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Z0G9}. Cell membrane {ECO:0000250|UniProtKB:Q9Z0G9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z0G9}.
Interaction partners:
- Occludin
- Tight junction protein ZO-1
- Claudin-12
- Claudin-5
- Tight junction protein 2
- Tight junction protein 3
- Claudin-11
- Claudin-1
- Claudin-16
- Claudin
Sequence:
MSMGLEITGTSLAVLGWLCTIVCCALPMWRVSAFIGSSIITAQITWEGLWMNCVVQSTGQMQCKMYDSLLALPQDLQAARALIVVSILLAAFGLLVALVGAQCTNCVQDETAKAKITIVAGVLFLLAAVLTLVPVSWSANTIIRDFYNPLVPEAQKREMGTGLYVGWAAAALQLLGGALLCCSCPPREKYAPTKILYSAPRSTGPGTGTGTAYDRKDYV
Protein: Innexin inx2 (Innexin-2) (Gap junction protein prp33) (Pas-related protein 33) (Q9V427)
Organism: Drosophila melanogaster (Fruit fly)
Function: Structural components of the gap junctions. Involved in gap junctional communication between germline and somatic cells which is essential for normal oogenesis. In embryonic epidermis, required for epithelial morphogenesis. Required for keyhole formation during early stages of proventriculus development in response to wg signaling. In follicle cells, promotes the formation of egg chambers in part through regulation of shg and baz at the boundary between germ cells and follicle cells. In inner germarial sheath cells, required for survival of early germ cells and for cyst formation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction. Cytoplasm. Apical cell membrane. Apicolateral cell membrane. Basolateral cell membrane. Lateral cell membrane. Note=In ovary, localizes to the apicolateral membrane between follicle cells and to the apical membrane between follicle cells and germline cells. Accumulates in the apicolateral membrane of epithelial cells in the epidermis. In salivary gland cells, accumulates in the basolateral membrane. In hindgut epithelial cells, accumulates in the lateral membrane. In nurse cells, localizes around the nuclei at oogenesis stage 10a and then, during stages 10b and 11, in cytoplasmic clouds and particles which become delivered into the oocyte during nurse cell regression.
Interaction partners:
- DE-cadherin
- Innexin inx3
Sequence:
MFDVFGSVKGLLKIDQVCIDNNVFRMHYKATVIILIAFSLLVTSRQYIGDPIDCIVDEIPLGVMDTYCWIYSTFTVPERLTGITGRDVVQPGVGSHVEGEDEVKYHKYYQWVCFVLFFQAILFYVPRYLWKSWEGGRLKMLVMDLNSPIVNDECKNDRKKILVDYFIGNLNRHNFYAFRFFVCEALNFVNVIGQIYFVDFFLDGEFSTYGSDVLKFTELEPDERIDPMARVFPKVTKCTFHKYGPSGSVQTHDGLCVLPLNIVNEKIYVFLWFWFIILSIMSGISLIYRIAVVAGPKLRHLLLRARSRLAESEEVELVANKCNIGDWFLLYQLGKNIDPLIYKEVISDLSREMSGDEHSAHKRPFDA
Protein: Soluble pyridine nucleotide transhydrogenase (STH) (EC 1.6.1.1) (NAD(P)(+) transhydrogenase [B-specific]) (P27306)
Organism: Escherichia coli (strain K12)
Function: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
Subcellular location: Cytoplasm.
Interaction partners:
- NAD
- NAD
- NAD kinase
- NAD-dependent protein deacylase
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Nucleoside triphosphate pyrophosphohydrolase
- NAD-capped RNA hydrolase NudC
- Trifunctional NAD biosynthesis/regulator protein NadR
- NH
- Nicotinate-nucleotide adenylyltransferase
Sequence:
MPHSYDYDAIVIGSGPGGEGAAMGLVKQGARVAVIERYQNVGGGCTHWGTIPSKALRHAVSRIIEFNQNPLYSDHSRLLRSSFADILNHADNVINQQTRMRQGFYERNHCEILQGNARFVDEHTLALDCPDGSVETLTAEKFVIACGSRPYHPTDVDFTHPRIYDSDSILSMHHEPRHVLIYGAGVIGCEYASIFRGMDVKVDLINTRDRLLAFLDQEMSDSLSYHFWNSGVVIRHNEEYEKIEGCDDGVIMHLKSGKKLKADCLLYANGRTGNTDSLALQNIGLETDSRGQLKVNSMYQTAQPHVYAVGDVIGYPSLASAAYDQGRIAAQALVKGEATAHLIEDIPTGIYTIPEISSVGKTEQQLTAMKVPYEVGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIHIGQAIMEQKGGGNTIEYFVNTTFNYPTMAEAYRVAALNGLNRLF
Protein: Tetratricopeptide repeat protein 32 (TPR repeat protein 32) (Q5I0X7)
Organism: Homo sapiens (Human)
Interaction partners:
- WD repeat-containing protein 35
Sequence:
MEGQRQESHATLTLAQAHFNNGEYAEAEALYSAYIRRCACAASSDESPGSKCSPEDLATAYNNRGQIKYFRVDFYEAMDDYTSAIEVQPNFEVPYYNRGLILYRLGYFDDALEDFKKVLDLNPGFQDATLSLKQTILDKEEKQRRNVAKNY
Protein: Leucine-rich repeat and fibronectin type III domain-containing protein 1 (Synaptic adhesion-like molecule 2) (Synaptic differentiation-enhancing molecule 1) (Q2WF71)
Organism: Mus musculus (Mouse)
Function: Promotes neurite outgrowth in hippocampal neurons. Involved in the regulation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Postsynaptic density membrane {ECO:0000250}. Note=Detected in excitatory, but not inhibitory, synaptic plasma membrane. {ECO:0000250}.
Interaction partners:
- Disks large homolog 4
- Receptor-type tyrosine-protein phosphatase delta
- Disks large homolog 1
- Receptor-type tyrosine-protein phosphatase S
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor 1
- Disks large homolog 3
Sequence:
MAPGPFSSGLFSPPPAALPFLLLLWAGASRGQPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSLVHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRKVESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHKLVRLDMTSNRLHKLPPDGLFLRSQGGGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDDLETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLRCRAVGDPEPVVHWVAPDGRLLGNSSRTRVRGDGTLDVTITTLRDSGTFTCIASNAAGEATAPVEVCVVPLPLMAPPPAAPPPLTEPGSSDIATPGRPGANDSTSERRLVAAELTSSSVLIRWPAQRPVPGIRMYQVQYNSSADDSLVYRMIPSTSQTFLVNDLAAGRAYDLCVLAVYDDGATALPATRVVGCVQFTTAGDPAPCRPLRAHFLGGTMIIAIGGVIVASVLVFIVLLMIRYKVYGDGDSRRIKGTSRTPPRVSHVCSQTNGAGAQQASAPPAPDRYEALREVAVPAAIEAKAMEAEATSTELEVVLGRSLGGSATSLCLLPSEETSGEESRAMTGPRRSRSGALGPPTSAPPTLALVPGGAPARPRPQQRYSFDGDYGALFQSHSYPRRARRTKRHRSTPHLDGAGGGAAGEDGDLGLGSARARLAFTSTEWMLESTV
Protein: Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Asparagine-linked glycosylation protein 12) (Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase) (Extracellular mutant protein 39) (Mannosyltransferase ALG12) (P53730)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Glc:Glc
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Man:Man
- Alpha-1,2-mannosyltransferase ALG9
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- GDP-Man:Man
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5
Sequence:
MRWSVLDTVLLTVISFHLIQAPFTKVEESFNIQAIHDILTYSVFDISQYDHLKFPGVVPRTFVGAVIIAMLSRPYLYLSSLIQTSRPTSIDVQLVVRGIVGLTNGLSFIYLKNCLQDMFDEITEKKKEENEDKDIYIYDSAGTWFLLFLIGSFHLMFYSTRTLPNFVMTLPLTNVALGWVLLGRYNAAIFLSALVAIVFRLEVSALSAGIALFSVIFKKISLFDAIKFGIFGLGLGSAISITVDSYFWQEWCLPEVDGFLFNVVAGYASKWGVEPVTAYFTHYLRMMFMPPTVLLLNYFGYKLAPAKLKIVSLASLFHIIVLSFQPHKEWRFIIYAVPSIMLLGATGAAHLWENMKVKKITNVLCLAILPLSIMTSFFISMAFLYISRMNYPGGEALTSFNDMIVEKNITNATVHISIPPCMTGVTLFGELNYGVYGINYDKTENTTLLQEMWPSFDFLITHEPTASQLPFENKTTNHWELVNTTKMFTGFDPTYIKNFVFQERVNVLSLLKQIIFDKTPTVFLKELTANSIVKSDVFFTYKRIKQDEKTD
Protein: 4Fe-4S ferredoxin-type domain-containing protein (Q09409)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTDEQRSGSRRRGGALGGGRGGNSQNSGRKRSSNSPADSASSSQKTSRNPSQNRPPMNIVPQKVTILKRNQDSQPTSPINRNAPPGPLVAAVQPLMAVELGDSGASLKGWNSNPTTPEKTTINVAGRQAEANKKQTQEYYFSKNAGSAVSAQTFQETVQYPMSSFPLEKNVPIQIDNNFTLLITPTTSKCNGLFIKVKLQHGDDNITTGALLKLDADEKTIRKSCRETIENLLKAKSSSDRFPFSKCSEGFLTSCLIKKLVDRLEAFPEAIYYCEKCDYHINTIGHAKAHLESSTHFDDVKRQEQREHLLKIIPPPTEAHLESVEKVLEGTLKSYQQVRQNGIEIGETIIYYLSTTVFPSIGLQDVILRPFGSVTYDVTLPDSDYNVAYTMSIPEGTPIFALLEQVRKKIADDGHPADHSMEMGTPSTIIFTFKGVRVKLCWMSCFNHRIQLHFSELMKTYVNLREEVAQFLQLIRLWATKAGLDSKNKPRIGLPRYGFDIMAIHFLQQIGCLPVLHELFEAGPETEKIEEMSAEKTAKLQSEEAGQRRMRLMSRYEKNTEKIGTKFDLKKSWNLAELFIGFFRYYVERHRDVVIQITQLIPMSRDVSRWNKKILHVVDPFRGDNVLSIPKVSTWQPFFFNCLLTSFVSFSIPRTKNGPLIEVSFVHNKTIKPGKKFKDTPKKATVEAPIPLTQIMEEHYQEPVYEIVNDKDHLKYMKELKERLMIDGILVNERKPIDYHTDDHRECVYGRNSLLRFKRVLKPGLNGKMAASMDGLSFVTKKGKKFINRWKKANVIILSEDSSEIDEKTKAADSNVSEIAEKLEETLKISSQKNIDVAVTSMPVSTEIKPEPITKLSNEAPVKIKNVAQPQCDLIEAPQESLMNESMMESSFDETESPMKTPIVQKPVKQNATFGKSTISTVIPDKQFCSEEFFIKLNSNLKDIVSKSKSLKPSDFHYEFSTDLFCGDFEMEMKCTHCDGSHCVENCPMMEIPPIKKYQARTPEDLKDIDDMIDKYYHENILDERRLKMLDHKIDELQSFLRKNYREDVTLTTFGSVMTGLSVNCSDIDICLRFGDGDVPPKDLTAKEVIQKTESVLRKCHLVKRVQAIVTAKVPIVKFQVKLSNGAIIDVDISYYNILAIYNTALLKEYSLWTPDKRFAKLALFVKTWAKNCEIGDASRGSLSSYCHVIMLISYLQNCDPPVLPRLQEDFRSDNRERRLVDNWDTSFAQVETSLLQRWPKNKESCAQLLIGYFDYYSRFDFRNFVVQCRREMILSKMEKEWPRPLCVEDPFDLSHNLSSGVNKKMFVFIMKVFINSRAVFMSEKPPMNRDHTFLSSYQHQLLRKCNQGSAPTDRQCHQCHRIGHFVESCPQRALAKEARKRFGSNSTNSSYRSNDSGRGFKNGEEGGDRLTYHKRTYYHRSYNK
Protein: GTP-binding protein YPT52 (P36018)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for transport in the endocytic pathway and for correct sorting of the vacuolar hydrolases suggesting a possible intersection of the endocytic with the vacuolar sorting pathway.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:21389113}. Note=Also found in association with endoplasmic reticulum vesicles having SED5 on their surface.
Interaction partners:
- Vacuolar protein sorting-associated protein 8
- Vacuolar morphogenesis protein 6
- Vacuolar protein sorting-associated protein 3
- Vacuolar membrane protein PEP3
- Vacuolar protein sorting-associated protein 16
- Vacuolar protein sorting-associated protein 41
- E3 ubiquitin-protein ligase PEP5
- Vacuolar protein sorting-associated protein 33
- Vacuolar protein sorting-associated protein 21
- Phosphatidylinositol 3-kinase VPS34
Sequence:
MLQFKLVLLGDSSVGKSSIVHRFVKDTFDELRESTIGAAFLSQSITIHPNDGNETKDVVIKFEIWDTAGQERYKSLAPMYYRNANAALVVYDITQEDSLQKARNWVDELKNKVGDDDLVIYLLGNKVDLCQETPSTETSPDSNEGGDEEQKVRAISTEEAKQYAQEQGLLFREVSAKTGEGVKEIFQDIGEKLYDLKKDEILSKQNRQIGGGNNGQVDINLQRPSTNDPTSCCS
Protein: S phase cyclin A-associated protein in the ER (Q8BIZ8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQNTAVECKITSTTGEKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIQSPSTDRMNVTSTARRSLNFGSLPGAVTAPCLAPTGVSWADKVKAHHTGSAPPEATPAQSCAPMTVQKTSRKNERKDAEGWETVQRGRPVRSRSTAVIPKVSLVTETLRSKDDSDKENICLLPEESIQKGKLEDRCSTVESLSKDSLLHSSDHPLSERTQEHLSLKKYVVDIVIESAAPPEPVKDGEERQKNKKKAKKIKARMNIRAKEYENLVETKNSGSESPYKAKLQRLTKDLVKQLQVQDSGSWVNNKASALDRTLGEIARILEKENVPDQISFQVAGGLTALENILQVVTPATNMNTVSRIPPKSLCNAINVYSLACNNCSENCTDVLFSNKITFLMDLLIHQLTVYVPDENNAVLGRNTNKQVFEGLTTGLLRAGAVVFSCLIANRPDGNSRPATPKISTQEMKNKPSQGDAFNSRVQDLISYVVNMGLIDRLHGCFLSVQGPVDENPKMATFLQHAAGFLRGMCMLCFAVTGRSSSIFDNNHQDPTGLTAALQATDLAGVLHMLYCILFHGTISDAGTSPKDSYTQNTIQVAIQSLRFFNSFAILDLSAFQSVVGAEGLSLAFRHMASSLLGHCSQVSCESLLHEVIVCVGYFTVNHPDNQVIVQSGRHPTVLQKLCQLPFQYFSDPRLIKVLFPSLITACHNNHQNKLILEQEMSCVLLATFIQDFAQTPGHVDNQSSSLKGKFQNPGNYLELANRFPQQAWEEARQFFLKKEKK
Protein: Type IV secretion system protein virB8 (Q7CEG3)
Organism: Brucella suis biovar 1 (strain 1330)
Function: The VirB system could be required for the establishment of the replication niche in the host.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MFGRKQSPQKSVKNGQGNAPSVYDEALNWEAAHVRLVEKSERRAWKIAGAFGTITVLLGIGIAGMLPLKQHVPYLVRVNAQTGAPDILTSLDEKSVSYDTVMDKYWLSQYVIARETYDWYTLQKDYETVGMLSSPSEGQSYASQFQGDKALDKQYGSNVRTSVTIVSIVPNGKGIGTVRFAKTTKRTNETGDGETTHWIATIGYQYVNPSLMSESARLTNPLGFNVTSYRVDPEMGVVQ
Protein: Regulatory factor X associated ankyrin containing protein (Regulatory factor X-associated ankyrin-containing protein, isoform CRA_c) (A0A024R7P0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELTQPAEDLIQTQQTPASELGDPEDPGEEAADGSDTVVLSLFPCTPEPVNPEPDASVSSPQGSSLKHSTTLTNRQRGNEVSALPATLDCDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKVQQVIENHILKLFQSNLVPADPE
Protein: LIM domain binding 3 (A0A8I5Y5H4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000256|ARBA:ARBA00004216}.
Interaction partners:
Sequence:
MGAARADISVDSILSQLFLGALHSLTRQQGTQQARPEEATAVGTSMSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPIQSPLPVIPHQKDPSLDTNSSLATPSPSPEARASPGTSGTLEFGDTFSSSFSQTSVCTSHMEASGPVLPLGSPVAKASSEGTQGSVSPKVLPGPSQPRLYNNPIGLYSAETLREMAQMYQMSLRGKASGAGLLGGSLPVKDLAVDSASPVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSRPQASAYSPAAATSPAPAAHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASPYSPSPGANYSPTPYTPSPAPAYTPSPAPTYTPSPAPTYSPSPAPAYTPSPAPNYNPTPSAAYSGGPSESASRPPWVTDDSFSQKFAPGKSTTSVSKQTLPRGAPAYNPTGPQVTPLARGTFQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFNCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPICAKCNTKIMGEVMHALRQTWHTTCFICAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAHAINV
Protein: DNA polymerase (EC 2.7.7.7) (P04495)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Eukaryotic-type DNA polymerase involved in viral genomic replication. DNA synthesis is protein primed, and acts in a strand displacement replication. Assembles in complex with viral pTP, DBP, host NFIA and host POU2F1/OCT1 on viral origin of replication. The polymerase covalently transfers dCMP onto pTP, thereby initiating complementary strand synthesis.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03261, ECO:0000255|HAMAP-Rule:MF_04055}.
Interaction partners:
Sequence:
MALVQAHRARRLHAEAPDSGDQPPRRRVRQQPTRAAPAPARARRRRAPAPSPGGSGAPPTSGGSPASPLLDASSKDTPAAHRPPRGTVVAPRGCGLLQAIDAATNQPLEIRYHLDLARALTRLCEVNLQELPPDLTPRELQTMDSSHLRDVVIKLRPPRADIWTLGSRGVVVRSTVTPLEQPDGQGQAAEVEDHQPNPPGEGLKFPLCFLVRGRQVNLVQDVQPVHRCQYCARFYKSQHECSARRRDFYFHHINSHSSNWWREIQFFPIGSHPRTERLFVTYDVETYTWMGAFGKQLVPFMLVMKFGGDEPLVTAARDLAANLGWDRWEQDPLTFYCITPEKMAIGRQFRTFRDHLQMLMARDLWSSFVASNPHLADWALSEHGLSSPEELTYEELKKLPSIKGIPRFLELYIVGHNINGFDEIVLAAQVINNRSEVPGPFRITRNFMPRAGKILFNDVTFALPNPRSKKRTDFLLWEQGGCDDTDFKYQYLKVMVRDTFALTHTSLRKAAQAYALPVEKGCCAYQAVNQFYMLGSYRSEADGFPIQEYWKDREEFVLNRELWKKKGQDKYDIIKETLDYCALDVQVTAELVNKLRDSYASFVRDAVGLTDASFNVFQRPTISSNSHAIFRQIVFRAEQPARSNLGPDLLAPSHELYDYVRASIRGGRCYPTYLGILREPLYVYDICGMYASALTHPMPWGPPLNPYERALAARAWQQALDLQGCKIDYFDARLLPGVFTVDADPPDETQLDPLPPFCSRKGGRLCWTNERLRGEVATSVDLVTLHNRGWRVHLVPDERTTVFPEWRCVAREYVQLNIAAKERADRDKNQTLRSIAKLLSNALYGSFATKLDNKKIVFSDQMDAATLKGITAGQVNIKSSSFLETDNLSAEVMPAFQREYSPQQLALADSDAEESEDERAPTPFYSPPSGTPGHVAYTYKPITFLDAEEGDMCLHTLERVDPLVDNDRYPSHLASFVLAWTRAFVSEWSEFLYEEDRGTPLEDRPLKSVYGDTDSLFVTERGHRLMETRGKKRIKKHGGNLVFDPERPELTWLVECETVCGACGADAYSPESVFLAPKLYALKSLHCPSCGASSKGKLRAKGHAAEGLDYDTMVKCYLADAQGEDRQRFSTSRTSLKRTLASAQPGAHPFTVTQTTLTRTLRPWKDMTLARLDEHRLLPYSESRPNPRNEEICWIEMP
Protein: Putative transcription factor Ovo-like 1 (hOvo1) (O14753)
Organism: Homo sapiens (Human)
Function: Putative transcription factor. Involved in hair formation and spermatogenesis. May function in the differentiation and/or maintenance of the urogenital system (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MPRAFLVKKPCVSTCKRNWSELPDEERGEIYVPVSLGFCPPQPYREPEPSVAEPPSCPLALNMSLRDSSYSMAPGPCVVAQLPSEDMGHLTDPQSRDHGFLRTKMKVTLGDSPSGDLFTCRVCQKAFTYQRMLNRHMKCHNDVKRHLCTYCGKGFNDTFDLKRHVRTHTGVRPYKCSLCDKAFTQRCSLESHLKKIHGVQQKYAYKERRAKLYVCEECGCTSESQEGHVLHLKEHHPDSPLLRKTSKKVAVALQNTVTSLLQGSPHL
Protein: MORC family CW-type zinc finger protein 1 (Protein microrchidia) (Q9WVL5)
Organism: Mus musculus (Mouse)
Function: Required for spermatogenesis. Essential for de novo DNA methylation and silencing of transposable elements in the male embryonic germ cells. Not required for piRNA biosynthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10369865, ECO:0000269|PubMed:25503965}.
Interaction partners:
Sequence:
MDKYALLQRAKLHLDFIHANSTTHSFLFGALAELLDNARDAGAVRLDVFSVDNETLQGGFMLCFLDDGCGMSPDEASDVIYFGTSKKRLSTLKFIGQYGNGLKSGSMRIGKDCILFTKKEETMTCLFFSQTFCEKEGLTEVVVPIPSWLTRTRESITDDPQKFFTELSIIFKYSPFKTEAELMQQFDMIYGRCGTLLIIYNLKLLLSGEPELDVTTDKEDILMAEAPEEIPERRSFRAYTAVLYFEPRMKIFIQAKRVQTKHLCYSLYKPRKYQYTTSSFKGKFKTEVQKAEEAVKRAELLFKEVQAKVNQPDRIALSSTQDALQKALQDVDTKHKSLRQKQRALRKARTLSLFFGVNTEDQHQAGMFIYSNNRLIKMYEKVGPQLKMKSLLGAGIIGIVNIPLETMEPSHNKQEFLNVQEYNHLLKVMGQYLIQYCKDIGISNRNLTLFWDEFKYQHSKDTDSSLESLQWRRRQAMGIPFILQCDLCLKWRVLPSSSNYQEKGLPDLWICASNPNNLENSCNQIERLPSIPLGTVNRRPPSKDERERQLQESVQRYQDKLVEAQPQKSQLIVTSKIPEFKSSCLSSALKEKSKLGRIQPSGADLTQGSPSSVKLSFMQRSQKRSTEDTHSDVEFICMTKIPKKSVKKTVKYLQPGHAPALLENLKLEDTAQVSSREIKKQQSESLVQAGKASTDVASSRDPTVTMVWDQSSTKVSLKQEEEEEVPLIKPDKQELCDDTPVVKGNSSALHWKSLPGVQMEDLSPRSGHKINSVSGDCQLPASPMPSQSMSVEETARKLLSNLREILLYFVPEFQLSSEFECTSVEELITNPELERCPENINEKLKTCFNQIQNIYMAQYEKRLKRKMQSIVYEANRRGLLNQVFLGQCELKRKRTEEKLSDLRAKLALLLQKLQLGGPAGDPQQIDAYLEDLLKEDRLPTALHEKSPESA
Protein: Uncharacterized vacuolar membrane protein YNR061C (P53747)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized membrane protein YDL218W
- Non-classical export protein 2 homolog 1
Sequence:
MLKLTTTSVTFHVLRYFQLGLSVTNLLLASFAIITNYKVDRILRLSLAVSIISSVYFGIVRFLPVLLIFVMEIVQTVLWFTAFVTLASKFGSMSCSSMPRGINFDYSGSCKIAKIDILPEAVLFILFLATTYASYITVLSQAKENGSSTRSVLKACVKALRDTVDRLETSLEESEPLLDLEVQEDARTETESIEDSTDSEDNANIEQEKVIDGSIEHSS
Protein: RNA-splicing ligase RtcB (EC 6.5.1.8) (3'-phosphate/5'-hydroxy nucleic acid ligase) (P9WGW5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: GTP-dependent RNA ligase that is involved in tRNA splicing and RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends.
Interaction partners:
- Probable protein archease
- Uncharacterized protein Rv2629
- Putative phosphoribosyl transferase Rv0571c
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Putative zinc metalloprotease Rip3
- Uncharacterized protein Rv2003c
Sequence:
MQVVNVATLPGIVRASYAMPDVHWGYGFPIGGVAATDVDNDGVVSPGGVGFDISCGVRLLVGEGLDREELQPRLPAVMDRLDRAIPRGVGTAGVWRLPDRNTLQEVLTGGARFAVEQGHGVALDLERCEDGGVMTGADAAKISDRALQRGLGQIGSLGSGNHFLEVQAVDRVYDPVAAAPMGLAEGTVCVMIHTGSRGLGHQICTDHVRQMEQAMGRYGIAVPDRQLACVPVHSPDGQAYLAAMAAAANYGRANRQLLTEATRRVFADATGTPLDLLYDVSHNLAKIETHPIDGQLRSVCVHRKGATRSLPPHHHELPAELAAVGQPVLIPGTMGTASYVLAGVTGNPAFFSTAHGAGRVLSRHQAARHTSGEAIRASLAKRGIIVRGTSRRGIAEEKPEAYKDVDEVIEASHQSGLARKVARLVPLGCVKG
Protein: Ecdysone-induced protein 75B, isoforms C/D (E75-A) (Nuclear receptor subfamily 1 group D member 3, isoforms C/D) (P17671)
Organism: Drosophila melanogaster (Fruit fly)
Function: Implicated in the regulation of ecdysone-triggered gene hierarchies. Probably plays a key role in mediating the regulation of the larval molt by 20-OH-ecdysone.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
Sequence:
MLMSADSSDSAKTSVICSTVSASMLAPPAPEQPSTTAPPILGVTGRSHLENALKLPPNTSVSAYYQHNSKLGMGQNYNPEFRSLVAPVTDLDTVPPTGVTMASSSNSPNSSVKLPHSGVIFVSKSSAVSTTDGPTAVLQQQQPQQQMPQHFESLPHHHPQQEHQPQQQQQQHHLQHHPHPHVMYPHGYQQANLHHSGGIAVVPADSRPQTPEYIKSYPVMDTTVASSVKGEPELNIEFDGTTVLCRVCGDKASGFHYGVHSCEGCKGFFRRSIQQKIQYRPCTKNQQCSILRINRNRCQYCRLKKCIAVGMSRDAVRFGRVPKREKARILAAMQQSTQNRGQQRALATELDDQPRLLAAVLRAHLETCEFTKEKVSAMRQRARDCPSYSMPTLLACPLNPAPELQSEQEFSQRFAHVIRGVIDFAGMIPGFQLLTQDDKFTLLKAGLFDALFVRLICMFDSSINSIICLNGQVMRRDAIQNGANARFLVDSTFNFAERMNSMNLTDAEIGLFCAIVLITPDRPGLRNLELIEKMYSRLKGCLQYIVAQNRPDQPEFLAKLLETMPDLRTLSTLHTEKLVVFRTEHKELLRQQMWSMEDGNNSDGQQNKSPSGSWADAMDVEAAKSPLGSVSSTESADLDYGSPSSSQPQGVSLPSPPQQQPSALASSAPLLAATLSGGCPLRNRANSGSSGDSGAAEMDIVGSHAHLTQNGLTITPIVRHQQQQQQQQQIGILNNAHSRNLNGGHAMCQQQQQHPQLHHHLTAGAARYRKLDSPTDSGIESGNEKNECKAVSSGGSSSCSSPRSSVDDALDCSDAAANHNQVVQHPQLSVVSVSPVRSPQPSTSSHLKRQIVEDMPVLKRVLQAPPLYDTNSLMDEAYKPHKKFRALRHREFETAEADASSSTSGSNSLSAGSPRQSPVPNSVATPPPSAASAAAGNPAQSQLHMHLTRSSPKASMASSHSVLAKSLMAEPRMTPEQMKRSDIIQNYLKRENSTAASSTTNGVGNRSPSSSSTPPPSAVQNQQRWGSSSVITTTCQQRQQSVSPHSNGSSSSSSSSSSSSSSSSSTSSNCSSSSASSCQYFQSPHSTSNGTSAPASSSSGSNSATPLLELQVDIADSAQPLNLSKKSPTPPPSKLHALVAAANAVQRYPTLSADVTVTASNGGPPSAAASPAPSSSPPASVGSPNPGLSAAVHKVMLEA