wanglab/gogpt-training-data huggingface dataset:
Protein: YlmG homolog protein 1-1, chloroplastic (AtYLMG1-1) (YGGT family protein YLMG1-1) (Q9SRS3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the proper distribution of nucleoids in chloroplasts. The nucleoid partitioning by YLMG1-1 may be related to chloroplast division processes.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:20359373}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in punctate structures on the thylakoid membranes which are adjacent to a subset of nucleoids. {ECO:0000269|PubMed:20359373}.
Interaction partners:
- Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB3, chloroplastic
- Protein TIC 20-I, chloroplastic
- Triglyceride lipase
- Translocase of chloroplast 34, chloroplastic
- Chloroplastic import inner membrane translocase subunit HP30-2
- F20H23.8 protein
- Mitochondrial import inner membrane translocase subunit TIM22-3
- Chloroplastic import inner membrane translocase subunit TIM22-2
- Chloroplastic import inner membrane translocase subunit HP30-1
- E3 ubiquitin-protein ligase SPL1
Sequence:
MAAITALTLRSPVYLPSSATSPRFHGFTNQPPPARLFFPLNPFPSLSIQNPKSIRISASASPITTPILQTEKSTARSSTLTGSTRSLATLAALAIAVTRVLAQKLSLAIQTSSPVIADGLRFSLSTAGPVFFASLRDRPPGYLNTPLTVVAVGIKKWLDIYSGVLMVRVLLSWFPNIPWERQPLSAIRDLCDPYLNLFRNIIPPIFDTLDVSPLLAFAVLGTLGSIVHGSTG
Protein: WD repeat-containing protein PAC11 (P40960)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for viability in the absence of the kinesin-related CIN8 mitotic motor. May be a dynein intermediate chain.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Dynein light chain 1
- Dynein heavy chain, cytoplasmic
- Tubulin beta chain
- Cytoplasmic dynein intermediate light chain DYN3
- Nuclear migration protein JNM1
- Tubulin alpha-3 chain
- Tubulin alpha-1 chain
- Protein NIP100
- Nuclear migration protein NUM1
- UPF0768 protein YBL029C-A
Sequence:
MERLKQLEEKRRQLKELRERRKQASLFPGSETMGHHPTEVHAKATMVSVSVQTDMEEGSKIQEPQSAYLRRKEVITYDKGIQTDQIEEEQLQENENHTTTDAVAIETTAADENNKDKAENDQPRLELAKPFLVEEAAATLSNASFARLETEVSASGQQAPSNMQQDKDNLMQWNMVSENLQSETDCDCIAQEYDPGKGVLVVVYLRLPPADLQYASSEAAWSVVNVVKCDNASGRNGLLIDMVEFRGTRIMTATILRRYHPESNVISILLATLTGKIILYELRLKQKKPETPVVYVVQRNMVARHYFQHPVVAVIETSSVQDQERVLVAADNGNIMELSCLDLTVLRKPQQLRPVPLSQLLSLENDTCTYTERLQRLAKFDEVGIACMAYTSEDPQYVWIGGEDGGIYKVFWDQPGPLYLSLDNNGFQPAENHSTRVTGLEFHWDDARRLMLLLSCSTDWTVRLWDARAGKAIIGAPLLLGGPVLRARWLEKNNGGENSRTLRCQVWCADGRLVVVNWAFDAKTSLYTATVIS
Protein: E3 ubiquitin-protein ligase Arkadia (EC 2.3.2.27) (RING finger protein 111) (RING-type E3 ubiquitin transferase Arkadia) (Q99ML9)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development. Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP. Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP. In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (By similarity). Associates with UBE2D2 as an E2 enzyme (By similarity). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates. Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML. The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs).
Subcellular location: Nucleus {ECO:0000269|PubMed:14657019}. Cytoplasm {ECO:0000250|UniProtKB:Q6ZNA4}. Nucleus, PML body {ECO:0000269|PubMed:23530056}. Note=Upon TGF-beta treatment, translocates from nucleus to cytosol. {ECO:0000250|UniProtKB:Q6ZNA4}.
Interaction partners:
- Mothers against decapentaplegic homolog 7
- Axin-1
- Mothers against decapentaplegic homolog 3
- Ski-like protein
- Axin-2
- Mothers against decapentaplegic homolog 2
- Small ubiquitin-related modifier 1
- E3 ubiquitin-protein ligase SMURF2
- Small ubiquitin-related modifier 2
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MSQWTPEFNELYTLKVAMKSGTPDAPTTQESLKAVLLHPQPLGATKSFPAEVEMINSKVGNEFSHLCDDSQKQEKDMTGNQQEQEKSGVVRKKRKSQQAGPSYVQNCVKENQEILGRRQQLETPSDEDNDSSLSECLSSPSSSLHFGGSDTVTSDEDKEVSVRHTQPVLSAKSRSHSARSHKWPRTEADPVPSLLMKRPCFHGSALRRVTCRKRLVKSSSSQRTQKQKERMLVQRKKREALAQRKYALLSSSSSSSENDLSSDSSSSSSTDGEEDLCASASENPSNPAAPSGSIDEDVVVIEASFTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHTGRPQESRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTIVPTTSARMDSQTTSASINNSNPSTSEQASDTTSTVASSQPSTVSETEATLTSNSATGSSVGDDVRRTASSAVPESGPPAMPRLPSCCPQHSPCGGTSQSHHALAHPHSSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPQVQAPCGANSSSGSSYHDQQALPVDLSNSALRTHGSGGFHGASAFDPCCPVTSSRAAVFGHQAAAAPTQPLSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACHHSHGNAPPQTQPPPQVDYVIPHPVHAFHSQISSHAASHPVAPPPPTHLGSTAAPIPQHLPPAHQPISHHIPAPAPSAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERTAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGASFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES
Protein: Stonin-1 (Stoned B-like factor) (Q8CDJ8)
Organism: Mus musculus (Mouse)
Function: May be involved in the endocytic machinery.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Some fraction is membrane-associated. {ECO:0000250}.
Interaction partners:
- TFIIA-alpha and beta-like factor
Sequence:
MYSTNPGSWVTFDDDPAFQSSQKRKDFSLETQGVCRPNGLKLTLPTLRDPPSTPSSASSTPLSSPMVDFYFSPGPPSNSPLSTPTKDFPGFPGIPKAGTHVLYPIPECSSSSAPTTAGGVGPPLLLTKPDCSPHVSLPSSHSHTQPTPTLGFTEDAGPQRVQSEARQFEYFQDHCAFSNPFWKDEGSASPFPLDSLASRKPFSPKDKEVPIGHKSLTQCSLDYICEKLEHLHSAETQDPLGDLSMQDPYAGDTVSFVPHSLFRSQPRAGWSFMLRIPEKKNMMSSRQWGPIFLKVLPGGILQMYYEKGLEKPFKEFQLDPHCRLSEPKLENFSMAGKIHTVKVEHVSYSEKRKYHAKTEVVHEPEVEQMLKLGSTEHRDFLEFLTTVEEELIKLPATAKPKNKSYEEQEICLDIQDSLWGKVTKEGQLVESAVVTQICCLCFLNGPAECFLALNDRELQKRDECYFEKEPEKKGIAILDYHFHTCVKAEEFEQSRIIKFVPLDACRFELMRFKTSYEAGELPFAVKSVVTVQGAYVELQAFVNMTPAAQGSPHAGALRSCNNIMIHFPVPAQWIKALWTRNLQRQKSLKAKMNRRACLGSLQEPESEPVIQVTVGSAKYESAYRAVVWKIDRLPDKNSSPDQPHCLSYKLELGSDQEVPSDWYPFATVQFSMLEACASRTEVRSLGVESDAQPQKHVCQRACYNIQVEIEKKWIQVDGEDADKTGGCVTQ
Protein: FI16617p1 (A1Z7L0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSPKRRLIDDSIAPSAADLQRTYDGHDGPHVFGTPGNQVYIRGQNDGVYKVPGVGGQFHHASSPADHVYTDEQGITYVHKKDAGGPGTHTLRGPGLAAVQPAYSTVQPAGLRNPQFHVERSGRTVDVGSGGFVVQRSRRSPQFHVERPGRTVDVGSGGFFVQRGRRSPQFPVERPWQRALKD
Protein: Apolipoprotein A-V (Apo-AV) (ApoA-V) (Apolipoprotein A5) (Regeneration-associated protein 3) (Q6Q788)
Organism: Homo sapiens (Human)
Function: Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL. May also be associated with chylomicrons. Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and an inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate) (By similarity). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages. Binds heparin.
Subcellular location: Secreted {ECO:0000269|PubMed:12810715}. Early endosome {ECO:0000269|PubMed:18603531}. Late endosome {ECO:0000269|PubMed:18603531}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:18603531}. Note=In the presence of SORL1, internalized to early endosomes, sorted in a retrograde fashion to late endosomes, from which a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network. {ECO:0000269|PubMed:18603531}.
Interaction partners:
- Apolipoprotein C-III
- Apolipoprotein C-II
- Apolipoprotein E
- Apolipoprotein B-100
- Apolipoprotein A-II
- Lipoprotein lipase
- Apolipoprotein A-I
- Apolipoprotein C-I
- Apolipoprotein
- Apolipoprotein M
Sequence:
MASMAAVLTWALALLSAFSATQARKGFWDYFSQTSGDKGRVEQIHQQKMAREPATLKDSLEQDLNNMNKFLEKLRPLSGSEAPRLPQDPVGMRRQLQEELEEVKARLQPYMAEAHELVGWNLEGLRQQLKPYTMDLMEQVALRVQELQEQLRVVGEDTKAQLLGGVDEAWALLQGLQSRVVHHTGRFKELFHPYAESLVSGIGRHVQELHRSVAPHAPASPARLSRCVQVLSRKLTLKAKALHARIQQNLDQLREELSRAFAGTGTEEGAGPDPQMLSEEVRQRLQAFRQDTYLQIAAFTRAIDQETEEVQQQLAPPPPGHSAFAPEFQQTDSGKVLSKLQARLDDLWEDITHSLHDQGHSHLGDP
Protein: Calpain-11 (EC 3.4.22.-) (Calcium-activated neutral proteinase 11) (CANP 11) (Q6J756)
Organism: Mus musculus (Mouse)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:16541461}.
Interaction partners:
- Calpastatin
- Calpain small subunit 1
- Calpain small subunit 2
Sequence:
MLNYSDISWAEKGMVATINHSRLKDKGVGQHQNAYNYKNQNYEDLRAECLRKGELFEDPFFPAEPRSIGVKNLGPNSEHMQNIYWQRPKDIIHNPQFITNDFSPTDICQGILGDCWLLAAIGSLTTCPKLLYRVVPRNQSFKKNYAGIFHFQLWQFGHWLNVVVDDRLPTRNNKLVFVHASHRQDFWSALLEKAYAKLIGSYGALSGGSTLEGLEDFTGGVAQCIPLQKPPGNMLRLLKKALEKSSLMGCSIEVTDNSEVETMTHNMLVRGHAYAVTGLEDVYYRDKLETLIRIQNPWGRVEWNGAWSDKATEWEEVSPDVRVQLLHKKDDGDFWMSYEDFMSNFTLLEICNLTPDALNTWDYKSRWHSTFYEGSWRRGSTAGGCRNHPETFWSNPQFKISLPEVDDPEDDSEKNEMVCTCLVALMQKNWRHAREGPQLLTIGFVIFSVPKEFQNLRDIHLKKDFFLKYRDHGFSEIFINSREVNSHLRLPPGEYVIIPSTYEPHKDADFLLRVFTEKHSETWLLDDANRFEHLQEETVTDKDLDKDSLQLFKIMANEDGEVDMYALHKLLNRMTAKLRNFKTKGFSLEVCRRMINLLDKDGSGKLELHEFQVLWKKIKKWTEIFKECDEDRSGNLNSYEMRLAIEKAGIKMNNRVTEVVVARYSDNMIVDFDSFLNCFLRLKAMFAFFLSMDTKKTGSICLDINQWLQITMWG
Protein: Outer membrane protein (Q8ZQ03)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- Periplasmic protein
- Periplasmic protein
- Lipoprotein
Sequence:
MKNVKTLIAAAVLSSLSFASFAAVEVQATPEGQQKFGTISANGGTNLGSLEDQLAQKAQEMGAKSFRITSVTGPNTLHGTAVIYK
Protein: DNA-binding protein Rv2175c (O53509)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds DNA at low salt concentrations.
Interaction partners:
- Serine/threonine-protein kinase PknL
- Manganese transport regulator
- Probable transcriptional regulatory protein
- NAD-dependent protein deacylase
- Possible exported protein
- HTH hxlR-type domain-containing protein
- HTH-type transcriptional regulator Rv0880
- Transcriptional regulatory protein KdpE
- Transcriptional regulatory protein
- Putative mycofactocin biosynthesis transcriptional regulator MftR
Sequence:
MPGRAPGSTLARVGSIPAGDDVLDPDEPTYDLPRVAELLGVPVSKVAQQLREGHLVAVRRAGGVVIPQVFFTNSGQVVKSLPGLLTILHDGGYRDTEIMRWLFTPDPSLTITRDGSRDAVSNARPVDALHAHQAREVVRRAQAMAY
Protein: Uncharacterized protein (Q38G17)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGISFCVSLHSLFEDDLISLEVVENKYMQFVSKDMRNICKTENYLVVAGIPSLDNDERFRRRNLQRDTCWSYPEVGRNSNNFSVKLLIIYVISPHINYNCELREIVGEEDI
Protein: Diacylglycerol acyltransferase/mycolyltransferase Ag85B (DGAT) (EC 2.3.1.122) (EC 2.3.1.20) (30 kDa extracellular protein) (Acyl-CoA:diacylglycerol acyltransferase) (Antigen 85 complex B) (85B) (Ag85B) (Extracellular alpha-antigen) (Fibronectin-binding protein B) (Fbps B) (P9WQP1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Diacylglycerol acyltransferase/mycolyltransferase Ag85C
- Secreted chorismate mutase
- Diacylglycerol acyltransferase/mycolyltransferase Ag85A
- 6 kDa early secretory antigenic target
- Immunogenic protein MPT64
- ESAT-6-like protein EsxB
- Triacylglycerol lipase
- ESAT-6-like protein EsxH
- Diacylglycerol kinase
- Peptidase M23 domain-containing protein
Sequence:
MTDVSRKIRAWGRRLMIGTAAAVVLPGLVGLAGGAATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETFLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG
Protein: Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit) (p50Cdc37) [Cleaved into: Hsp90 co-chaperone Cdc37, N-terminally processed] (Q61081)
Organism: Mus musculus (Mouse)
Function: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q16543}.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Cyclin-dependent kinase 4
- RAC-alpha serine/threonine-protein kinase
- Heat shock 70 kDa protein 1B
- Stress-induced-phosphoprotein 1
- Serine/threonine-protein phosphatase 5
- Endoplasmin
- Prostaglandin E synthase 3
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQIKHFGMLHRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLLEAVPKAGNEKDVSA
Protein: Axin-2 (Axin-like protein) (Axil) (Axis inhibition protein 2) (Conductin) (O88566)
Organism: Mus musculus (Mouse)
Function: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2T1}.
Interaction partners:
- Catenin beta-1
- Glycogen synthase kinase-3 beta
- Axin-1
- Adenomatous polyposis coli protein
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-3
- Transcription factor 7
- Lymphoid enhancer-binding factor 1
- Adenomatous polyposis coli protein 2
Sequence:
MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSDPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGVPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHQHHHHQQCHTLLPTGGKLPPVAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHPKAPEPLPGEQFCGSRGGTLPKRNAKGTEPGLALSARDGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSAQSIRKSYPLESACAAPGERVSRHHLLGASGHSRSVARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHSAAGQAGASPFANPSLAPEDHKEPKKLASVHALQASELVVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
Protein: Putative dehydration-responsive element-binding protein 2H (Protein DREB2H) (Q9SIZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone H4
- FACT complex subunit SSRP1
Sequence:
MPRKRKSRGTRDVAEILRKWREYNEQTEADSCIDGGGSKPIRKAPPKRSRKGCMKGKGGPENGICDYTGVRQRTWGKWVAEIREPGRGAKLWLGTFSSSYEAALAYDEASKAIYGQSARLNLPLLPLCQARLLHFLMNLKFVHVRIQMQDLVLVRSD
Protein: Rho-related GTP-binding protein RhoF (Rho family GTPase Rif) (Rho in filopodia) (Q9HBH0)
Organism: Homo sapiens (Human)
Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Causes the formation of thin, actin-rich surface projections called filopodia. Functions cooperatively with CDC42 and Rac to generate additional structures, increasing the diversity of actin-based morphology.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton.
Interaction partners:
- Protein diaphanous homolog 1
- Protein diaphanous homolog 3
- Alpha-actinin-1
Sequence:
MDAPGALAQTAAPGPGRKELKIVIVGDGGCGKTSLLMVYSQGSFPEHYAPSVFEKYTASVTVGSKEVTLNLYDTAGQEDYDRLRPLSYQNTHLVLICYDVMNPTSYDNVLIKWFPEVTHFCRGIPMVLIGCKTDLRKDKEQLRKLRAAQLEPITYMQGLSACEQIRAALYLECSAKFRENVEDVFREAAKVALSALKKAQRQKKRRLCLLL
Protein: Protein Churchill (Q5U3N7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional activator that mediates FGF signaling during neural development (By similarity). Plays a role in the regulation of cell movement. Does not bind DNA by itself (By similarity).
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- ATPase family AAA domain-containing protein 2
- F-box only protein 46
- Ankyrin repeat and SOCS box protein 13a.1
Sequence:
MCTGCVQKQYPDRGNTCLENGSYLMNFVGCANCHQRDFVLISDRTMVNEDEEEIVTYLHMCKNCEHVIARHEYTFTVVDDYQEYTMLCMLCGKAEDSISVLPDDPRQTAPLF
Protein: DNA-directed RNA polymerases I and III subunit RPAC2 (RNA polymerases I and III subunit AC2) (AC19) (DNA-directed RNA polymerase I subunit D) (Q6DRI4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit
- RNA polymerase I and III subunit C.
- Polymerase
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase III subunit RPC6
Sequence:
MAELGQKHALEMVRTDGADEGCVTFVLNEEDHTLGNSLRYMIMKSQDVEFCGYSITHPSESKINFRIQTRDGVPASEPLRNGLNNLTDVCKHVLQTFEARMKEFKEQEESMT
Protein: Protein sex-lethal (P19339)
Organism: Drosophila melanogaster (Fruit fly)
Function: Sex determination switch protein which controls sexual development by sex-specific splicing. Regulates dosage compensation in females by suppressing hyperactivation of X-linked genes. Expression of the embryo-specific isoform is under the control of primary sex-determining signal, which depends on the ratio of X chromosomes relative to autosomes (X:A ratio). Expression occurs in 2X:2A cells, but not in X:2A cells. The X:A ratio seems to be signaled by the relative concentration of the X-linked transcription factors SIS-A and SIS-B. As a result, the embryo-specific product is expressed early only in female embryos and specifies female-adult specific splicing; in the male where it is not expressed, the default splicing gives rise to a truncated non-functional protein. The female-specific isoform specifies the splicing of its own transcript, thereby initiating a positive autoregulatory feedback loop leading to female development pathway. The female-specific isoform controls the sex-specific splicing of transformer (TRA); acts as a translational repressor for male-specific lethal-2 (MSL-2) and prevents male-less (MLE), MSL-1 and MSL-3 proteins from associating with the female X chromosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:7516476}. Cytoplasm {ECO:0000269|PubMed:9182767}.
Interaction partners:
- RNA-binding protein Unr
- Female-specific protein transformer
- E3 ubiquitin-protein ligase msl-2
- U1 small nuclear ribonucleoprotein A
- Pre-mRNA-splicing regulator female-lethal
- Protein doublesex
- Protein virilizer
- YTH domain-containing protein 1
- Protein nanos
- Transformer-2 sex-determining protein
Sequence:
MYGNNNPGSNNNNGGYPPYGYNNKSSGGRGFGMSHSLPSGMSRYAFSPQDTEFSFPSSSSRRGYNDFPGCGGSGGNGGSANNLGGGNMCHLPPMASNNSLNNLCGLSLGSGGSDDLMNDPRASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSFGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGKAKAAHFMSQMGVVPANVPPPPPQPPAHMAAAFNMMHRGRSIKSQQRFQNSHPYFDAKKFI
Protein: RH16520p (Q7YU70)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALSKTIKSKAGAKDEQNELVEFEPKDDEESNEVTASNCDTEAITKEEEWITKRKTELTTTRQIETRVKRQVKLQDGKVIEDSGPIVSTNTTEDTDKQETETTEKRDLDLPDDLDGNAQLIDVAALQAGAINETQLAQIQEVFGPADGAGKLVKRMVPRPVDGLVRQTDDKRVISHEEIKDYHETEDVQHHGDFTDQTYVNAVRDGVENLEAVLCSPESQRQLVPLGPKVVANRSKSRKTIDSEDTQKRCLAQEDGTLVTESRRTTEHELIVDDELPDPPANGASDDLGLQLQVGEQVTTTAANQRFFRQRDEQHVDVLANGRLQSTEMRYAAETTQMDKDGPTDLERPGDWDSLSDRMRKLRRSQQQQQKEVALLADRKDALTKRPLDFDREEETRKGETMKWLESHFGSESTASNDSRDDEADAEVEPTKKSYFNVTIKSQSHAQSHLATQQHSHPQHISHGHHPQTLPRSAERERERERERERERERERERERDRDRHPLAMTASASQERKAPANSAGGRSKYFQGISNWSERKDPGPPVNHFSSQAFRDDLQETIRRNGLKKKVSGPGSSQGSALAQETVVQPKDSYVSREDILQQKRQSLSSQFLARSMRGSRDALDDLEAIPGPGPGPSMISPRAEEPSHKRVAYGHRGNNGTHINGHALNGVAPTLVNGRGKSYEPPAPPPAAVPPLEFGGGGSQLGQNPRPTVPQRRRAIEKKLGEHSHTHSHSHSHSSHTSHSAHLPVKSQAPMPSQLNQLEPPPDYSPPPRSRSRSSSPQVDYLMTREMPASTMTLSRKQQQRTRFAPTSSYPPATGGTGNLRPPGATSVSTSNLSAMSGGVSTSKSSRMGQVIGNSLRKLVSKIRSASAERKFRMKSAASKSREQSPSPGQDPRGVGPPVTTYQQYNVIDGHIGSHDSEDSNRQSATQGAGEGARKRAGTGTGA
Protein: N-alpha-acetyltransferase 38, NatC auxiliary subunit (L-A virus GAG protein N-acetyltransferase subunit MAK31) (Maintenance of killer protein 31) (N-terminal acetyltransferase C complex subunit MAK31) (NatC complex subunit MAK31) (P23059)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus Gag protein. MAK31 is necessary for the structural stability of L-A double-stranded RNA-containing particles. Necessary for growth at 37 degrees Celsius as well as for maintenance of the killer plasmid.
Interaction partners:
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 30
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D2
- LSM complex subunit LSM2
- Small nuclear ribonucleoprotein Sm D1
- LSM complex subunit LSM6
- Small nuclear ribonucleoprotein-associated protein B
- LSM complex subunit LSM7
Sequence:
MDILKLSDFIGNTLIVSLTEDRILVGSLVAVDAQMNLLLDHVEERMGSSSRMMGLVSVPRRSVKTIMIDKPVLQELTANKVELMANIV