wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase 6 regulatory subunit 2 (SAPS domain family member 2) (O75170)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16769727}.
Interaction partners:
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
- Splicing factor 3B subunit 1
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B
- NF-kappa-B inhibitor epsilon
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Ubiquitin carboxyl-terminal hydrolase 10
- DNA-dependent protein kinase catalytic subunit
Sequence:
MFWKFDLNTTSHVDKLLDKEHVTLQELMDEDDILQECKAQNQKLLDFLCRQQCMEELVSLITQDPPLDMEEKVRFKYPNTACELLTCDVPQISDRLGGDESLLSLLYDFLDHEPPLNPLLASFFSKTIGNLIARKTEQVITFLKKKDKFISLVLKHIGTSALMDLLLRLVSCVEPAGLRQDVLHWLNEEKVIQRLVELIHPSQDEDRQSNASQTLCDIVRLGRDQGSQLQEALEPDPLLTALESQDCVEQLLKNMFDGDRTESCLVSGTQVLLTLLETRRVGTEGLVDSFSQGLERSYAVSSSVLHGIEPRLKDFHQLLLNPPKKKAILTTIGVLEEPLGNARLHGARLMAALLHTNTPSINQELCRLNTMDLLLDLFFKYTWNNFLHFQVELCIAAILSHAAREERTEASGSESRVEPPHENGNRSLETPQPAASLPDNTMVTHLFQKCCLVQRILEAWEANDHTQAAGGMRRGNMGHLTRIANAVVQNLERGPVQTHISEVIRGLPADCRGRWESFVEETLTETNRRNTVDLVSTHHLHSSSEDEDIEGAFPNELSLQQAFSDYQIQQMTANFVDQFGFNDEEFADQDDNINAPFDRIAEINFNIDADEDSPSAALFEACCSDRIQPFDDDEDEDIWEDSDTRCAARVMARPRFGAPHASESCSKNGPERGGQDGKASLEAHRDAPGAGAPPAPGKKEAPPVEGDSEGAMWTAVFDEPANSTPTAPGVVRDVGSSVWAAGTSAPEEKGWAKFTDFQPFCCSESGPRCSSPVDTECSHAEGSRSQGPEKASQASYFAVSPASPCAWNVCVTRKAPLLASDSSSSGGSHSEDGDQKAASAMDAVSRGPGREAPPLPTVARTEEAVGRVGCADSRLLSPACPAPKEVTAAPAVAVPPEATVAITTALSKAGPAIPTPAVSSALAVAVPLGPIMAVTAAPAMVATLGTVTKDGKTDAPPEGAALNGPV
Protein: EG:EG0007.4 protein (Q7K765)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDDAAVAAAAVTGGNLQRMQQITKSASSNIMSQRMHYYTPYNSNNGGGSVNYKQQQQQSQQYQEHYQAPQGQHHHHHHHHHHHHHHHSGSAVSNQVDSSRRKSTSSMPPSEKSDSSDLDSVHSLPIQTGKKKSLGGGNNKQRGAPSASQRQAKQNNNAAAPISYADIARNKQEALNNATASDTELELGDKMQIKSGGKSKSRPDFPELPGAVTAVAASGGAANQATVVSSQNTPPSSSSSISYSQSLNATPPSSSSDAESTNSPELLAQVQIPAYSMITPTLTASMISSVSSSVASTSSTSCSPPALQKSKSVEHDTSYSCNSSNLDQQYPALEKTVKRHSTNNVSVAVAASTSASASSSLYNFAAAAKQQLTENTHSAVSPPAAVTTTSTAVAASAPAPTTVTVPAAVTVPCYSSSSTHGSTQTSTSTASSAIAALPSGKAKAKPKELSPSSSCSKKPTKPSQDVPSISLSISTTPRATTSTSTTTTQKTTAATQTEGAKKLIGGIHKLPSSSCIAKGAGAVLEATAGRRAVIILNDDREAGRSNNEFIFGDFNEDELKLFDDNLDDEEEGQHKQSSNKKQQTEGESDVTQDDTEDVDQDLDKELECLGRRPEKKQERQQDISASSDQHLNDSGAASDAVNSSASLDMLSISAEAAQSSPNAGATATSSSVASPINSSTPSGASSASASTSTSSSSVSISSSSGGNGAACLASVSGMLGGVANQSGDSGIYAAANTSIKEHVNTFLSKASSSEETLPSPNSISMQQLETCNDIEAAIIAAARAAAAARSTSCSRSNSQEQDALQPQVKTKATPNPEAKMVLPVFVTYNNNNNDDDDDEEDDESLQELSFMADLKADAATEDIAMQPPPPSCPAMMTNTELIVDYIAKTWNAIANSKYVTYYNEQEQEQET
Protein: Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (sQC) (Glutaminyl-tRNA cyclotransferase) (Glutamyl cyclase) (EC) (Q16769)
Organism: Homo sapiens (Human)
Function: Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Subcellular location: Secreted {ECO:0000269|PubMed:18486145}.
Interaction partners:
Sequence:
MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL
Protein: Vesicle-associated membrane protein 3 (VAMP-3) (Cellubrevin) (CEB) (Synaptobrevin-3) (Q15836)
Organism: Homo sapiens (Human)
Function: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:23353890}; Single-pass type IV membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:23353890}; Single-pass type IV membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000305}.
Interaction partners:
- Synaptosomal-associated protein 23
- Syntaxin-6
- Syntaxin-1A
- Synaptosomal-associated protein 25
- Syntaxin-4
- Syntaxin-3
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Vesicle-associated membrane protein 7
- Syntaxin-16
- Syntaxin-1B
Sequence:
MSTGPTAATGSNRRLQQTQNQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNCKMWAIGITVLVIFIIIIIVWVVSS
Protein: Putative KRAB domain-containing protein ZNF788 (Zinc finger family member 788, pseudogene) (Q6ZQV5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRNMIPQDNENPPQQGEANQNDSVAFEDVAVNFTPDEWALLDPSQKNLYREVMQETLRNLASIEVLWKRDSLKVKVISMEKF
Protein: Phosphatidylinositol 4-kinase type 2-beta (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-beta) (PI4KII-BETA) (Q8TCG2)
Organism: Homo sapiens (Human)
Function: Together with PI4K2A and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. This contribution may be especially significant in plasma membrane, endosomal and Golgi compartments. The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). Contributes to the production of InsP3 in stimulated cells and is likely to be involved in the regulation of vesicular trafficking.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12324459}. Golgi apparatus membrane {ECO:0000269|PubMed:11923287, ECO:0000269|PubMed:12324459}; Peripheral membrane protein {ECO:0000269|PubMed:12324459}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12324459}. Cell membrane {ECO:0000269|PubMed:11923287, ECO:0000269|PubMed:12324459}. Early endosome membrane {ECO:0000269|PubMed:11923287}. Note=Mainly cytosolic, association with membranes of the Golgi, endoplasmic and plasma membrane is stimulated by active RAC1 (PubMed:12324459). Association with early endosomes has not been confirmed (PubMed:11923287, PubMed:12324459). {ECO:0000269|PubMed:11923287, ECO:0000269|PubMed:12324459}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit beta
Sequence:
MEDPSEPDRLASADGGSPEEEEDGEREPLLPRIAWAHPRRGAPGSAVRLLDAAGEEGEAGDEELPLPPGDVGVSRSSSAELDRSRPAVSVTIGTSEMNAFLDDPEFADIMLRAEQAIEVGIFPERISQGSSGSYFVKDPKRKIIGVFKPKSEEPYGQLNPKWTKYVHKVCCPCCFGRGCLIPNQGYLSEAGAYLVDNKLHLSIVPKTKVVWLVSETFNYNAIDRAKSRGKKYALEKVPKVGRKFHRIGLPPKIGSFQLFVEGYKEAEYWLRKFEADPLPENIRKQFQSQFERLVILDYIIRNTDRGNDNWLVRYEKQKCEKEIDHKESKWIDDEEFLIKIAAIDNGLAFPFKHPDEWRAYPFHWAWLPQAKVPFSEEIRNLILPYISDMNFVQDLCEDLYELFKTDKGFDKATFESQMSVMRGQILNLTQALRDGKSPFQLVQIPCVIVERSQGGSQGRIVHLSNSFTQTVNCRKPFFSSW
Protein: Spermidine N(1)-acetyltransferase (SAT) (EC 2.3.1.57) (GCN5-related N-acetyltransferase) (GNAT) (Protease synthase and sporulation negative regulatory protein PAI 1) (Q9HL57)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.
Interaction partners:
- Major facilitator superfamily
Sequence:
MSIEIRKLSIEDLETLIEVARESWKWTYAGIYSEEYIESWIREKYSKEKLLNEIVRSQSNLDILFLGAFADSTLIGFIELKIIANKAELLRLYLKPEYTHKKIGKTLLLEAEKIMKKKGILECRLYVHRQNSVGFSFYYKNGFKVEDTDGSDFIMEKKYES
Protein: Serine/threonine-protein kinase plk-1 (EC 2.7.11.21) (Polo-like kinase 1) (P34331)
Organism: Caenorhabditis elegans
Function: Required for oocyte nuclear envelope breakdown before entry of oocyte into spermatheca. In meiotic cells, required for spindle dynamics and probably for spindle attachment to the chromosomes. Zygotic role in the development of the germline and nerve cord. In mitotic cells, plays a role in spindle organization and centrosome maturation. Involved in asymmetric nuclear localization of cdc-25.1 during embryogenesis which affects cell division timing. Together with plk-2, regulates cytoplasm polarity in early embryos. May play a minor role in chromosome pairing and synapsis during oocyte meiosis I.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:22018922}. Midbody {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18305005}. Cytoplasm {ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:18316412, ECO:0000269|PubMed:20823068, ECO:0000269|PubMed:22018922}. Nucleus {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:22018922}. Chromosome {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:22018922}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22018922}. Note=In mitosis, remains associated with centrosomes entering prophase through to anaphase. During metaphase, embryos show anterior enrichment and located to the chromosomes of the metaphase plate. In meiosis, detected at centrosomes after pronuclear meeting in post-meiotic 1-cell embryos. Associated with chromatin during chromosome segregation of anaphase and in the region between the dividing chromosomes. Cytoplasmic in mature, unfertilized oocytes (PubMed:10660671). Asymmetric cytoplasmic localization is regulated by mex-5 and mex-6 (PubMed:18199581, PubMed:18316412). {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18316412}.
Interaction partners:
- separase
- Separin homolog sep-1
- G2/mitotic-specific cyclin-B
- Cyclin N-terminal domain-containing protein
- Spindle-defective protein 2
- Spindle-defective protein 5
- Aurora kinase
- Incenp-like protein ICP-1
- Tyrosine-protein phosphatase cdc-14
- Kinesin-like protein
Sequence:
MNRLPNIAKPPQKSNQRKEKAPPEVPALIADKDRGTYYEKGRFLGKGGFAHCYELTNRATREVVAGKVVPKSMLVKQYQRDKVDNERILIHRELGHINIVKLFNFFEDNLNVYITLELCARRSLMELHKRRKAVTEPEARYFTHQIVDGVLYLHDLNIIHRDMKLGNLFLNDDLVVKIGDFGLATTVNGDERKKTLCGTPNYIAPEVLNKAGHSFEVDIWAVGCILYILLFGQPPFESKSLEETYSRIRHNNYTIPSIATQPAASLIRKMLDPEPTRRPTAKQVQRDGFFKSGFMPTRLPVSCLTMVPKFGGHETSMMEENVAPRGVDARSQRPLNGRAGLSALPQHIVSNNADRERAQQQAAEATFREPEDAYLSQLFHQVAVLLEQRIPGLEEEEAALDGYQSPECLPVFWISKWVDYSDKYGIGYQLCDNSVGVLFNDNSRIMLDQAGNELTYIEKSNKEHYFSMHSGEMPGLLNKKVTLLKYFRSYMNDHLVKAGEGSEQRAGDDLARLPTLRVWFRTKSAIVLHLSNGTVQINFFNDHVKMMMCPLMQAVTFIDQNKRMLTYKLNNLQRNGCPEKFLHRLKYAKTMIERLMSDANVVSQNPARQPDMPRSMAAARSASAGSRGPNQAASHLPQSASGSNIHPRR
Protein: Helicase 89B, isoform B (Helicase 89B, isoform C) (Q9VF02)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TATA-box-binding protein
- Negative cofactor 2alpha
- TBP-related factor
- Protein Dr1
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor IIB
- TATA box-binding protein-like 1
- RT01008p
- TBP-related factor 5
- Transcription initiation factor TFIID subunit 1
Sequence:
MTSRLDRLFILLETGSTAATRQAAAKQIGEVQKLYPHELHALLNRLVGYLHSTSWETRIAAAQTVEAILKQVPPWQPEFQVLPKKERCATNTATAAAAAEEDSCQSSGSNSTTASERLLSFDEFDLQQILHKGARLIGSEGNEFDVQEEQPASGGGEEDRSLASRLSRQRAVLNDKLGLTTAAKLGVNLTDMITDEDVALNRSGSTYNVNAEKLPVEHLLNIKTAANGSGQAPLSCREMNRAKRKARQNTSGCSVTAVTPTCSRRNSNSNHSTGSNHSSNGTTGAAIEEPEKKKLKSTDRQEIFYSLNAAVPDATGTWVDAVSWPLENFCSRLFIDLFHAKWEVRHGAATALRELINQHAQGAGKAVLQTREQMDEAHSRWLEDAALRLLCVLCLDRFGDFVSDQVVAPVRETCAQVLGTLVKEMEASKVQRIVNILLQLIQHKNEWDVRHGGLLGLKYVFVVREELLPIYLPQSISNILIGLLDAVDDVGAVAAATLIPVSSWLPKLLNPAQVSSIVKMLWDLLLDQDELTSACNSFMGLLAAILCLPNAARWVEMEPMAILVPRLWPFLSHSTSSVRRSTLKTLMTLTSADRVKSEPKDENQVKEEADKEEMKLNFGVSDWKWELLQQALRHIYQRILVEPQADIQALARQVWSNLIQHADLGALLHAACPFVSSWICLSMQPPRLAFDAGVLIRAGGDVSTPGSTSRKRTPRIGDELGGNILAQSNASLKLYLGGSEATPLDVRDANFMRARISSSRALGALSHYLVQPAPGVVYTPQTESPTDCYTKVLLGHLNAHSAVQRIVCGLIIAFWALEDEPVRPGPPNLQEKLHQCVSEYVYYDEVAISLTRLLQEAQDFIATLKQNKIPINDFNNAKILTLDQIEAVATTLSENLRSYPLKPKVLDMLEERRRSLQASYQQTTSEQSAYHVSAQAALAGAICALHCLPDKLNPVVKPLMESIKREQCLQLQQLSAEFLVHLMDQVCDRNPSPNSKILNNLCTLLRSDPEFTPKLVMPLETLKQTPVSSEVINNCVYYGILTLALQQTVTTTNTRSGAGGATTPTATTAPRGPGRPPTGEILSATNATAHIELKAQQAKEAEAKQCRIQRLGAACAIEKLCRIFGEQIIEKVAVFQHLMFGKVEQFVKEAYDWRLGSLLPDLGVCNELVSSMQLIETAAPHLHVALHPQMFALLPSLGFIVCHPLKAVRHMAARCIAVLAEIDACQTMQFVVHDLLPLLGKIEQLIERQGAIEAIERVVSRLQIKVVPYIVLLVVPLLGAMSDPDESVRLLSTHCFANLVQLMPLDGKTEQLKSDPLQARKTRDREFLDYLFNPKSIPNYKVPVPISVELRCYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHMHRQTANLANLPSLVICPPTLTGHWVYEVEKFLDQGSVLRPLHYYGFPVGREKLRSDIGTKCNLVVASYDTVRKDIDFFSGIHFNYCVLDEGHIIKNGKTKSSKAIKRLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFVQRFSRPILSSRDAKSSAKEQEAGVLAMEALHRQVLPFLLRRVKEDVLKDLPPKITQDLLCELSPLQLRLYEDFSNKHLKDCLDKLGDSSSASMVTENLSAKTHIFQALRYLQNVCNHPKLVLRQSEELTKVTSQLALSNSSLDDIEHSAKLPALKQLLLDCGIGVQTESVSQHRALIFCQLKAMLDIVEQDLLRRHLPSVTYLRLDGSVPASQRQDIVNNFNSDPSIDVLLLTTMVGGLGLNLTGADTVIFVEHDWNPMKDLQAMDRAHRIGQKKVVNVYRLITRNSLEEKIMGLQKFKILTANTVVSAENASLQTMGTSQIFDLFNGGKDKGAESGSSAVQGTASGGMSMNTIIENLPELWSEHQYEEEYDLGNFVQALKK
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit P (Down syndrome critical region protein 5) (Down syndrome critical region protein C) (Phosphatidylinositol-glycan biosynthesis class P protein) (PIG-P) (P57054)
Organism: Homo sapiens (Human)
Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Protein preY, mitochondrial
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- GPI alpha-1,2-mannosyltransferase 3
Sequence:
MVPRSTSLTLIVFLFHRLSKAPGKMVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFIPESWLNSLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNYAKNQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN
Protein: UvrABC system protein C (Protein UvrC) (Excinuclease ABC subunit C) (P9WFC5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
Interaction partners:
- UvrABC system protein B
- UvrABC system protein A
- Nucleotide-binding protein Rv1421
- Putative gluconeogenesis factor
- Probable cell division protein WhiA
- ATP-dependent DNA helicase UvrD1
- Holliday junction branch migration complex subunit RuvB
- Riboflavin biosynthesis protein RibBA
- Recombination protein RecR
- Holliday junction branch migration complex subunit RuvA
Sequence:
MPDPATYRPAPGSIPVEPGVYRFRDQHGRVIYVGKAKSLRSRLTSYFADVASLAPRTRQLVTTAAKVEWTVVGTEVEALQLEYTWIKEFDPRFNVRYRDDKSYPVLAVTLGEEFPRLMVYRGPRRKGVRYFGPYSHAWAIRETLDLLTRVFPARTCSAGVFKRHRQIDRPCLLGYIDKCSAPCIGRVDAAQHRQIVADFCDFLSGKTDRFARALEQQMNAAAEQLDFERAARLRDDLSALKRAMEKQAVVLGDGTDADVVAFADDELEAAVQVFHVRGGRVRGQRGWIVEKPGEPGDSGIQLVEQFLTQFYGDQAALDDAADESANPVPREVLVPCLPSNAEELASWLSGLRGSRVVLRVPRRGDKRALAETVHRNAEDALQQHKLKRASDFNARSAALQSIQDSLGLADAPLRIECVDVSHVQGTDVVGSLVVFEDGLPRKSDYRHFGIREAAGQGRSDDVACIAEVTRRRFLRHLRDQSDPDLLSPERKSRRFAYPPNLYVVDGGAPQVNAASAVIDELGVTDVAVIGLAKRLEEVWVPSEPDPIIMPRNSEGLYLLQRVRDEAHRFAITYHRSKRSTRMTASALDSVPGLGEHRRKALVTHFGSIARLKEATVDEITAVPGIGVATATAVHDALRPDSSGAAR
Protein: Follitropin subunit beta (Follicle-stimulating hormone beta subunit) (Follitropin beta chain) (G1MS74)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKTLNCYVLLFCWKAICCYSCELTNITIAVEREECELCITVNATWCSGYCFTRDPVYKYPPVSSVQQICTFKEVVYETVKIPGCGDHPESFYSYPVATACHCVPVFLRGRKIWGTKSRTVYMFEDYYKKKNNSQFAMLIMSRTMNVISRSPKRERQPLFIYLEINSQGGGGKKEDRGVSEQ
Protein: DNA mismatch repair protein (Q803S7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAKQSSLFNFFSKSPPLAVKAKSSPSPAEGDAPGRSNTSPKEEAKVNSKKTPAKPPSKTQAIAGHAKLFGEKAATTKERKQSPVFSAGSLVWAKMEGHPWWPCMVVPQPLSGQQMRGRGRDQRLHVHFFDEPPTRGWVNTKYIREYQGSNSAVAKSGGMFFSGKPVIRKAMELADVAMKDSPEQRLKMPLCMDPSDEEEEDEEDMEIEKSTVSDAEMSEEEVKEKTKPSRRPPRAAAEKSQKSKRRRIVVASDSDDSGEEFDPNKAGGSSDEDKEEEEGVNSGAEEEESEPETEPDSPVKPIKRKRPTEKPTKSKSKPETPKRAPAALPSVSTDAKSRLSAFSAPDNFDSQSSANGTEGGSTVWDHEKLEWLQDGKRKDAQRKRQSDENYDPTTLYVPEDFLNRTTPGMRRWWQLKSEMFDTVLFYKVGKFYELYHMDAVIGVNELNLTFMKGTWAHSGFPEIGFGRFSDVLVQKGYKVARVEQTETPNMMEARCKKLARPTKFDKVVKREVCRIITRGTQTYSVLDGAPSETQSKYLLSIKEKSEEDSTGHGHIYGVCFIDTSVGRFHIGQFQDDRHCSRLRTLVAHYSPAQVIFEKGNPSIETLKIFKAIVASSLQEGLNAGSQFWDAQKTLKVLAEEDYFKESKDDNKKASVLPPALKAMTPECDALSLTPKTGYELALSALGGCMFYLKKCLVDQELFSMGNFEEYVPVDVEMEQAGGASCFFAKTNQRMVLDGVTLANLEILQNSSTGGPEGTLLERLDTCCTPFGKRLLKQWICAPLCNLSSIGDRLDALEDLMGAPSQTSEVTDLLKKLPDLERLLSKIHSMGTPLKGQDHPDSRAILYEEVVYSKRKIADFLAALEGFKVMKEIVSIMEPVGEDLKSKLLRQVVLLKTENEDGLFPDLSPELKRWDTAFDHQKARTTGVITPKAGFDPEYDQALNGIKECERDLQDYLDRQKKRLGCKNLSYWGTGRNRYQLEVPESVSERSLPEEYEVRSTKKGWKRYSTKDIERMFSELQSWEDKRDAALKDCMRRLFYNFDKNYKDWQTAVECMAVLDVLLSMCRYSQSADGSMARPEMALPGDGSYSAPFLDLRGSRHPCVTKTFFGDDFIPNDIFIGCPGDEEEAQDDTKALAPCVLVTGPNMGGKSTLMRQCGLVVILAQLGCYVPAESLRLTPVDRVFTRLGASDRIMSGESTFFVELSETASILLHATNHSLVLLDELGRGTATYDGTAIASAVVKELSEKICCRTLFSTHYHSLVEDHVQDPAVRLGHMACMVENECEDPSQETITFLYKFIRGACPKSYGFNAARLANIPEDVIQSGHKKARDFERSTVSLRIFKKLCSFAESPRAEREQLTTLIQTLRNL
Protein: Plasma membrane-associated cation-binding protein 1 (AtPCAP1) (Microtubule-destabilizing protein 25) (Q96262)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in intracellular signaling through interaction with PtdInsPs and calmodulin (CaM); may keep PtdInsPs attached to the plasma membrane until Ca(2+)-CaM reaches a competitive concentration subsequent to an increase triggered by a stimulus, thus leading to PtdInsPs release and subsequent activation of InsPs-dependent signaling cascade. Interacts competitively at the N-terminus with calcium ions and CaM (in a calcium-dependent manner), and with the phosphatidylinositol phosphates PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(4,5)P(2) and PtdIns(3,5)P(2). Binds also weakly to PtdIns(3)P, PtdIns(4)P and PtdIns(5)P. Negative regulator of hypocotyl cell elongation by destabilizing cortical microtubules in a calcium-dependent manner. Binds directly to and destabilized microtubules to enhance microtubule depolymerization when cytoplasmic calcium increases. In case of Turnip mosaic virus (TuMV) infection, confers sensitivity by promoting viral cell-to-cell movement through interaction with viral P3N-PIPO.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130, ECO:0000305|PubMed:17644812}; Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, plasmodesma. Note=Shuttles from plasma membrane to cytoplasm (e.g. colocalizes with cortical microtubules) upon calcium levels increase. Co-localizes with Turnip mosaic virus (TuMV) P3N-PIPO at the plasmodesmata.
Interaction partners:
- Calcium-binding protein CP1
- Calmodulin-6
- Calmodulin-like protein 10
- Calmodulin-2
- Calmodulin-1
- Calmodulin-7
- Plasma membrane-associated cation-binding protein 2
- At1g23060/T26J12_16
- WEB family protein At5g16730
- WEB family protein At5g55860
Sequence:
MGYWNSKVVPKFKKLFEKNSAKKAAAAEATKTFDESKETINKEIEEKKTELQPKVVETYEATSAEVKALVRDPKVAGLKKNSAAVQKYLEELVKIEFPGSKAVSEASSSFGAGYVAGPVTFIFEKVSVFLPEEVKTKEIPVEEVKAEEPAKTEEPAKTEGTSGEKEEIVEETKKGETPETAVVEEKKPEVEEKKEEATPAPAVVETPVKEPETTTTAPVAEPPKP
Protein: Glypican-1 (H7BZL4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
XAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKDPAVSLQVIQGCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLCSEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDASDDGSGSGSGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQKT
Protein: Sodium-dependent phosphate transport protein 2C (Sodium-phosphate transport protein 2C) (Na(+)-dependent phosphate cotransporter 2C) (Sodium/phosphate cotransporter 2C) (Na(+)/Pi cotransporter 2C) (NaPi-2c) (Solute carrier family 34 member 3) (Q8K4R8)
Organism: Rattus norvegicus (Rat)
Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:11880379}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the brush border membrane in the kidney. {ECO:0000269|PubMed:11880379}.
Interaction partners:
- Na
- Sodium-dependent phosphate transport protein 2A
- Sodium-dependent phosphate transport protein 2B
- Fibroblast growth factor 23
- Klotho
- Sodium-dependent phosphate transporter 2
- 1,25-dihydroxyvitamin D
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- Phosphate regulating endopeptidase X-linked
- Parathyroid hormone
Sequence:
MPNSLAGDQVPNPTLDAIGLVDWSLRNAGTSGSTPGLEEGGTDPWTFSQLKNTDQLKEVGTASKLHQVVSGFLKACGLLGSLYFFICSLDILSSAFQLLGSKMAGDIFKDNVVLSNPVAGLVIGVVVTVLVQSSSTSSSIVVSMVASKSLTVQASVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFGGSAVHGIFNWLTVLVLLPLENATAALERLSELALGAASLQPGGQAPDILKALTRPFTHLIIQLDSSVVTSSITSNTTNSSLIKHWCGFRGETPQGSSEECDLSGSCTERNSSASPGEDRLLCHHLFAGSELTDLAVGFILLAGSLLVLCVCLVLIVKLLNSVLRGRIAQAVKTVINADFPFPFGWLSGYLAILVGAGLTFLLQSSSVFTAAIVPLMGVGVINLERAYPLFLGSNIGTTTTALLAALASPADTLLFAVQVALIHFFFNLAGILLWYLVPVLRLPIPLAKRFGDLTAQYRWVAIVYLLLTFLLLPLAAFGLSLAGGSVLAAVGGPLVGLVLLIILVNVLQRHRPSWLPRRLQSWAWLPLWLHSLEPWDRLVTGCCPFKAYSNSHMTSKVAHCYENPQVIASQQL
Protein: Methylesterase 17 (AtMES17) (EC 3.1.1.-) (Methyl indole-3-acetic acid esterase) (Q9SG92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylesterase that efficiently and specifically hydrolyzes methyl indole-3-acetic acid (MeIAA) to IAA (auxin). MeIAA is believed to be an inactive form of auxin that needs to be demethylated to exert a biological effect.
Interaction partners:
- Indole-3-acetate O-methyltransferase 1 acetate carboxylmethyltransferase 1)
- DEAD-box ATP-dependent RNA helicase 13
- Probable carboxylesterase 8
Sequence:
MAEENQEETLELKPSRKPPHFVLIHGMSLGSWCWYKIKCLMEVSGFTVTCIDLKSSGIDSSSVDSLTTFDQYNQPLIDFLSSFPEQEQVILVGHSAGGLSLTSAIQRFPKKICLAVFIGASMLKNGLQTDEDMKDGVPDLSEHGDVYELGFGLGPENPPTSAIIKPEYRRKLLYHMSPQQECSLAALMMRPAPILALTTAKLEEEEKEKGQEEQVPRVYIKTLLDRVMKPEQQDAMIRRWPPSQVYELESDHSPFFSNPFVLFGLLIKAAVSVGSI