wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin, heavy polypeptide 2, fast muscle specific isoform X1 (Myosin, heavy polypeptide 2, fast muscle-specific) (Q6IQX1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Myosin, light chain 1, alkali; skeletal, fast
- Troponin C, slow skeletal and cardiac muscles
- Tnnt3b protein)
- Fast muscle troponin I, tandem duplicate 4)
- Fast skeletal muscle myosin light polypeptide 3
- Actinin alpha 3b
- Atrial myosin light chain
- Troponin T type 1
- Si:dkey-7c18.24
- Myosin, light chain 10, regulatory.
Sequence:
MSTDAEMAIYGKAAIFLRKPEKERIEAQSKPFDAKTACYVVDDKELYVKGTIKSKDGGKVTVVTLDTQTEKVVKEDDVHPMNPPKFDKIEDMAMMTHLNEPSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATVAVQGGDKKKEQAAGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAIDILGFTGEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIAYLLGLNSADMLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVIRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFKAGLLGTLEEMRDEKLATLVTMTQALCRAYLMRREFVKMMERRESIYTIQYNIRSFMNVKHWPWMKVYYKIKPLLKSAETEKELATMKEDFVKCKEALAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMASQDESIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKIKKKDFETAQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTVEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKAKKTVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKGEIDRKLAEKDEEMEQIKRNSQRVTEAMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLETDLVQIQSEVEDTVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDAGKAKEE
Protein: Protein NRT1/ PTR FAMILY 2.7 (AtNPF2.7) (Nitrate excretion transporter 1) (Q9M1E2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transporter involved in a passive nitrate efflux. Not competent for chloride transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17993627}; Multi-pass membrane protein {ECO:0000269|PubMed:17993627}.
Interaction partners:
- High-affinity nitrate transporter 2.1
- S-type anion channel SLAH3
- High affinity nitrate transporter 2.5
- High affinity nitrate transporter 2.4
- AGAMOUS-like-56
- Chloride channel protein CLC-a
- WAT1-related protein At1g68170
- High affinity nitrate transporter 2.7
Sequence:
MASSVTGDAETAISADSSTKRRGGGWITFPFMIATLLGLTIAAWGWLLNLIVYLIEEFNVKSIAAAQIANIVSGCICMVPAVAAIASDSFFGTIPVISVSAFISLMGVALLTLTASLDTLRPRPCETASILCQSPSKTQLGVLYTAITLASIGTGGTRFTLATAGANQYEKTKDQGSFFNWFFFTTYLAGAISATAIVYTEDNISWTLGFGLSVAANFFSFLVFVSGKRFYKHDKPLGSPFTSLLCVIFAALRKRKAVVSTNEKDYHNESITMPTKSFRFFNRAALKQEDEVKPDGTIRNPWRLCSVQQVEDFKAVIRIIPLALATIFLSTPIAMQLSLTVLQGLVMDRRLGPSFKIPAGSLQVITLLSTCLFIIVNDRVLYPFYQKLTGKHLTPLQRVGIGHAFNILSMAVTAIVEAKRLKIVQKGHFLGSSSVADMSVLWLFPPLVIVGIGEAFHFPGNVALCYQEFPESMRSTATSITSVVIGICFYTSTALIDLIQRTTAWLPDDINHGRVDNVYWILVIGGVLNLGYFLVCSWLYRYRNLKDDDHKQAANVSH
Protein: SD02996p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform E) (Uncharacterized protein, isoform H) (Q9VX48)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIMRRASACTMPSSGGGGGAGVGSSQREEATTPGESPGGRLSRWFSIRRGSSHQYDVGGRDGRHSTASSFDTPDSGSGNSPKNGSNAVAGTGGAGSQGVALDAASPQKLANLGASKMMPGVPESEDDEATANRFDVDLMMTPGSRANGTARTAHNRLIVPMLPPAPAGLSQQQLKRRHIVAAIVHSENSYVATLQRLVNDYKKPLEECSPPVLNPVKIATLFHCLPDILHSHKLFRISLAECVRNWDRDEKIGDCFVSAFGKPQLLEIYSGFINNFSAAMELAKMEEKRKSALADFFKVKQISAHDRLSFFGLMVKPVQRFPQFILFLQDLLKYTPQGHHDRMSLQLALSQLELLAELLNESKREAEQYQAFKEMLGHISGTFNARSLSLSSVSVSDSAGGHRPRYLLREDNVTHMEFNQAGFIVKCKQRRLLLLNDKVICVSVAPKQSHDFGATEKLTFKWMFPVNDVEIVDNSTSATLSRILTAGLNRGGSLKSNGSSGANGSPYANSTLPGHGGGVSGFSGFGDPHSSPAAQLTNGADNLCSEMSTLMYDYEVISRIQDLVSSLKGSYKELNANTTRNVLNLIQGSIQRKDEEMAWVDSCCLQLIGRHKSGKEETFTFQTQTPAVKKEWITELRLAQLALDPNNSPAWERGGSHPQPAHHHPHHHPLQHPHAGAGDPRQTQEQLQLQEAVQQKQSRKMPLFVKAMPVYKSQHQTEVRCGCYYSIANDTKQSGNARRRHKQLNYLWMCSSDGTSSHITVLAQHPQQAGNLREAGAFDLFETQVSALEFVKGLDQLKSRDEPASLLGDLVWLGTDSRKILIYSARNPEQEEQLGSYSVPGAVQRILYHFDAVYVALSGATVLIFRRGNDGVWQLRDPQTIRLGDTDLVVPSLLPINMCIYASCGNRVYVMNALNGEIQRSFEVQHGATQQVNLMAHSGIGLWISLKNSTMLCLYHTETFKHLQDINIASSVLRHDGKKEQPLNNSSVYVTALMACKGLLWVGTNVGIAVTIPLPRLEGVPIISGGINMSCHAHFGPITFLLPLIPKVYPAYKPPTVGAAPLVPSMGDDLQLPAIDADPKIQELDDGAVVLRRDLAKEEMSSSNPGADSTASSPRSSKLDKQNSLDQSFTAKIRASLANSPAFHRKRFRDDPNRMSKTLPRGLGAAAAGSGAGGASAAGSGTASGNTSQHGEHGICDVYGLYGKLIFVKEDYDAEEGNQGNLMDMMYEGMRRSDPELAAIPGKVCTLDRRLRMKASRPRSLDLSNWSVDSKSSSLYTSSGSEESMGIRHFGGRSVSRNSSSASHKTSGTGSDLGNISENGLMTTADIHHHQQQQQQLNSSAKPDEMSRLGAGNSGLDKPAAAVATLKRKQKQNSKQQQQQNADGPRTVITLMGGRGYWRQMWYNGAGGSPSHKNSSSGGGGGSGSGFSGQTMQSGNPSCSPLTANSNDAHIVVWEKKL
Protein: Oxidized purine nucleoside triphosphate hydrolase (EC 3.6.1.56) (2-hydroxy-dATP diphosphatase) (7,8-dihydro-8-oxoguanine triphosphatase) (8-oxo-dGTPase) (Methylated purine nucleoside triphosphate hydrolase) (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1) (Q7ZWC3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP. Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P36639}. Mitochondrion matrix {ECO:0000250|UniProtKB:P36639}. Nucleus {ECO:0000250|UniProtKB:P36639}.
Interaction partners:
- 8-oxo-dGDP phosphatase NUDT18
- Nucleotide triphosphate diphosphatase NUDT15
- ADP-sugar pyrophosphatase
- m7GpppN-mRNA hydrolase NUDT17
- Bis
- Nudix-type motif 13.
- Uridine diphosphate glucose pyrophosphatase NUDT14
- Nudix-type motif 12.
- Nudix-type motif 22
- 8-oxoguanine DNA glycosylase.
Sequence:
MFTSKLLTLVLVVQPGRVLLGMKKRGFGAGKWNGFGGKVQTGETIEQAARRELLEESGLTVDTLHKIGNIKFEFIGETELMDVHIFRADNYEGEPAESDEMRPQWFDIDKIPFSQMWADDILWFPLMLQKKRFLGYFKFQGHDVIVEHKLDEVEDL
Protein: Phenoloxidase 2 (PO A3) (EC 1.14.18.1) (Phenoloxidase subunit A3) (Processed phenoloxidase A3) (Pro-phenoloxidase A3) (Q9V521)
Organism: Drosophila melanogaster (Fruit fly)
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinonee (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:12834045, ECO:0000269|PubMed:19141111}. Note=Expressed in larval hemolymph.
Interaction partners:
- tyrosinase
- Serine protease inhibitor 27A
- Hemolectin, isoform A
Sequence:
MADKKNLLLLFDHPTEPVFMDKGKRVTVFDVPDSFLTDRYRPISNEVQSRVGDKVEQRVPVREISIPDLRIPMSLGRDEQFSLFLPKHRRIAGRLIDIFMNMRSVDDLQSVAVYARDRVNPVLFNYALSVALLHRPDTQGLDLPSFSQTFPDRFIDSQVIRKMREESFVVQPGSRMPITIPRDYTASDLDPEHRLWYFREDLGINLHHWHWHLVYPFEASDRSIVAKDRRGELFYYMHQQVIARYNAERFSNNLARVLPFNNLRDPIAEGYFPKMDSLVASRAWPPRFESTRLSDLNRESDQLNVEIGDLERWRDRIYEAIHQGFVMDERGNRVPLDEATGIDTLGNMIESSILSPNRVLYGDLHNNGHTFISYAHDPTSKHLESFGVMGDVSTAMRDPVFYKWHSYIDRIFQEHKSRLPAYTENQLNYPGVSIAGIQVDTNGGRPNNLTTFWQQSDVDMSRGFDFLPRGNVFARFTHLQHLPFTYTISLNNDSGAQRFGYVRIFMAPKNDERGQPMLMRDQRSMMIELDKFVTSLNPGPNTIRRRSTESSVTIPFERTFRNLDANRPAAGTPEELEFNFCGCGWPNHMLVPKGLPEGLQCVLFIMVSNYENDRIDQQLVGRCSDAASYCGVRDRLYPDRQSMGFPFDRLPRSGVDRLVNFLTPNMSIVDVNIRHENRTVQRPN
Protein: Recombination signal binding protein for immunoglobulin kappa J region (A0A8I6AFG7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLAYRKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFYIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEQNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPTNESNTNSEGNYTNASTNSTSVTSSTATVVS
Protein: TRAF3-interacting JNK-activating modulator (TRAF3-interacting protein 3) (Q9Y228)
Organism: Homo sapiens (Human)
Function: Adapter protein that plays essential roles in both innate and adaptive immunity. Plays a crucial role in the regulation of thymocyte development. Mechanistically, mediates TCR-stimulated activation through recruiting MAP2K1/MEK1 to the Golgi and, thereby, facilitating the interaction of MAP2K1/MEK1 with its activator BRAF. Also plays an essential role in regulatory T-cell stability and function by recruiting the serine-threonine phosphatase catalytic subunit (PPP2CA) to the lysosome, thereby facilitating the interaction of PP2Ac with the mTORC1 component RPTOR and restricting glycolytic metabolism. Positively regulates TLR4 signaling activity in macrophage-mediated inflammation by acting as a molecular clamp to facilitate LPS-induced translocation of TLR4 to lipid rafts. In response to viral infection, facilitates the recruitment of TRAF3 to MAVS within mitochondria leading to IRF3 activation and interferon production. However, participates in the maintenance of immune homeostasis and the prevention of overzealous innate immunity by promoting 'Lys-48'-dependent ubiquitination of TBK1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30573680}. Golgi apparatus membrane {ECO:0000269|PubMed:26195727}; Single-pass type IV membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q8C0G2}. Mitochondrion outer membrane {ECO:0000269|PubMed:31390091}. Note=Accumulates on the mitochondria after virus infection. {ECO:0000269|PubMed:31390091}.
Interaction partners:
- FGFR1 oncogene partner 2
- Striatin-interacting protein 1
- Striatin-3
- MOB-like protein phocein
- Suppressor of IKBKE 1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein kinase 25
- Serine/threonine-protein kinase 24
- Programmed cell death protein 10
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Sequence:
MISPDPRPSPGLARWAESYEAKCERRQEIRESRRCRPNVTTCRQVGKTLRIQQREQLQRARLQQFFRRRNLELEEKGKAQHPQAREQGPSRRPGQVTVLKEPLSCARRISSPREQVTGTSSEVFPAQHPPPSGICRDLSDHLSSQAGGLPPQDTPIKKPPKHHRGTQTKAEGPTIKNDASQQTNYGVAVLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSWKGQLNEDKLKGKLRSLENQLYTCTQKYSPWGMKKVLLEMEDQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQGLLQNQSLQLQEQEKLLTKKDQALPVWSPKSFPNEVEPEGTGKEKDWDLRDQLQKKTLQLQAKEKECRELHSELDNLSDEYLSCLRKLQHCREELNQSQQLPPRRQCGRWLPVLMVVIAAALAVFLANKDNLMI
Protein: Immunoglobulin kappa variable 2-28 (A0A075B6P5)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
- Immunoglobulin heavy variable 3-72
- Probable non-functional immunoglobulin heavy variable 3-16
- Immunoglobulin heavy variable 3-43D
- Immunoglobulin kappa variable 2D-29
- Interleukin-4 receptor subunit alpha
- Programmed cell death protein 1
- T-cell surface glycoprotein CD5
- Interleukin-17A
- Epidermal growth factor receptor
- Leukocyte surface antigen CD47
Sequence:
MRLPAQLLGLLMLWVSGSSGDIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQALQTP
Protein: Odorant receptor 59a (P81923)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to ethyl acetate, anisole, hexanoic acid, and pyrazines.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 30a
- Odorant receptor 74a
- Odorant receptor 22c
- Odorant receptor 45a
- Odorant receptor 67b
- Odorant receptor 45b
- Odorant receptor 83a
- Odorant receptor 63a
- Aluminum tubes, isoform G
Sequence:
MAEVRVDSLEFFKSHWTAWRYLGVAHFRVENWKNLYVFYSIVSNLLVTLCYPVHLGISLFRNRTITEDILNLTTFATCTACSVKCLLYAYNIKDVLEMERLLRLLDERVVGPEQRSIYGQVRVQLRNVLYVFIGIYMPCALFAELSFLFKEERGLMYPAWFPFDWLHSTRNYYIANAYQIVGISFQLLQNYVSDCFPAVVLCLISSHIKMLYNRFEEVGLDPARDAEKDLEACITDHKHILEWAGGSLVRVLFTFQLFSRLFRRIEAFISLPMLIQFTVTALNVCIGLAALVFFVSEPMARMYFIFYSLAMPLQIFPSCFFGTDNEYWFGRLHYAAFSCNWHTQNRSFKRKMMLFVEQSLKKSTAVAGGMMRIHLDTFFSTLKGAYSLFTIIIRMRK
Protein: 20S-pre-rRNA D-site endonuclease nob1 (EC 3.1.-.-) (Pre-rRNA-processing endonuclease nob1) (Q9UTK0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the synthesis of 40S ribosome subunits. Has a role in processing 20S pre-rRNA into the mature 18S rRNA, where it is required for cleavage at the 3' end of the mature 18S rRNA (D-site). Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm (By similarity).
Subcellular location: Cytoplasm. Nucleus, nucleolus.
Interaction partners:
- Protein LTV1
- Pre-rRNA-processing protein pno1
- Ribosome biogenesis protein tsr1
- Serine/threonine-protein kinase rio1
- Serine/threonine-protein kinase rio2
- Uncharacterized protein C13G1.09
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS15
Sequence:
MSKSITHLVLDTGGIICSSTLLRNSAESFYTIPRVIAEIRDETSRKNFELWGDQVIQRVPKPEFIKKVSEFAKQTGDYSSLSVTDIQILALTYELEVEFNGGDWRLRKYPGQKHINGKPPSNSNSTEDASKPTSSDTASVKETENSDPKSAENEVLEGETTQHSNNKEAHPNTEENKEQEDNEEDDEDDGWITPSNIRKKKAEDGVGESLVQPKHLKVACATTDFSMQNVLLQIGLNLVSSDGFKIQNVKRFVLRCHGCYTVVKDMEKKFCPSCGGNTLIKTTCSINSKGEFQVHLKKNFEWKTRGTKYSLPKPVHGTSNGKGKKNPVLREDQPEYQRAVRRMQRKKEIDLMDEDYLPSLLTGVTKDRMYVQIGAGRKNPNEVRRKKR
Protein: 31 kDa ribonucleoprotein, chloroplastic (RNA-binding protein 1/2/3) (AtRBP33) (RNA-binding protein CP31A) (RNA-binding protein RNP-T) (RNA-binding protein cp31) (Q04836)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for specific RNA editing events in chloroplasts and stabilizes specific chloroplast mRNAs. Associates with the 3'-terminus ndhF mRNAs and protects them against 3'-exonucleolytic degradation. Required for normal chloroplast development under cold stress conditions by stabilizing transcripts of numerous mRNAs under these conditions. May modulate telomere replication through RNA binding domains.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17450127}.
Interaction partners:
- Organelle RRM domain-containing protein 1
- Chloroplast stem-loop binding protein of 41 kDa b, chloroplastic
- Organelle RRM domain-containing protein 6
- NAD
- Protein ACTIVITY OF BC1 COMPLEX KINASE 3, chloroplastic
- Putative elongation factor TypA-like SVR3, chloroplastic
- Probable CCR4-associated factor 1 homolog 7
- Alanine--tRNA ligase
- NAD
Sequence:
MASSIVTSSLKPLAMADSSSSTIFSHPSISSTISSSRIRSSSVSLLTGRINLPLSFSRVSLSLKTKTHLKKSPFVSFVAQTSDWAEEGGEGSVAVEETENSLESQDVSEGDESEGDASEGDVSEGDESEGDVSEGAVSERAEFPEPSEEAKLFVGNLAYDVNSQALAMLFEQAGTVEIAEVIYNRETDQSRGFGFVTMSSVDEAETAVEKFNRYDLNGRLLTVNKAAPRGSRPERAPRVYEPAFRVYVGNLPWDVDNGRLEQLFSEHGKVVEARVVYDRETGRSRGFGFVTMSDVDELNEAISALDGQNLEGRAIRVNVAEERPPRRGY
Protein: Microtubule-associated protein 2 (MAP-2) (P15146)
Organism: Rattus norvegicus (Rat)
Function: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:P20357}.
Interaction partners:
- Tubulin beta-3 chain
- Neuromodulin
- Disks large homolog 4
- Glial fibrillary acidic protein
- Neurofilament light polypeptide
- RNA binding protein fox-1 homolog 3
- Synaptophysin
- Nestin
- Synapsin-1
- Cyclin-dependent kinase 5
Sequence:
MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTVKDERVTEGSQPFAPVFFQSDDKMSLQDTSGSATSKESSKDEEPQKDKADKVADVPVSEATTVLGDVHSPAVEGFVGENISGEEKGTTDQEKKETSTPSVQEPTLTETEPQTKLEETSKVSIEETVAKEEESLKLKDDKAGVIQTSTEQSFSKEDQKGQEQTIEALKQDSFPISLEQAVTDAAMATKTLEKVTSEPEAVSEKREIQGLFEEDIADKSKLEGAGSATVAEVEMPFYEDKSGMSKYFETSALKEDVTRSTGLGSDYYELSDSRGNAQESLDTVSPKNQQDEKELLAKASQPSPPAHEAGYSTLAQSYTSDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKIPCFPIESKEEEDKTEQAKVTGGQTTQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAVVAESSTGLPPVADDSQPVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPSSADKSGLSREFDQDRKANDKLDTVLEKSEEHVDSKEHAKESEEVGDKVELFGLGVTYEQTSAKELITTKETAPERAEKGLSSVPEVAEVETTTKADQGLDVAAKKDDQSPLDIKVSDFGQMASGMSVDAGKTIELKFEVDQQLTLSSEAPQETDSFMGIESSHVKDGAKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADSSIDEKAEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAVVSEPAEVRGEEEEIEAEGEYDKLLFRSDTLQITDLLVPGSREEFVETCPGEHKGVVESVVTIEDDFITVVQTTTDEGELGSHSVRFAAPVQPEEERRPYPHDEELEVLMAAEAQAEPKDGSPDAPATPEKEEVPFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKEARRPSLEKHRKEKPFKTGRGRISTPERREVAKKEPSTVSRDEVRRKKAVYKKAELAKESEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVRILNKKMDFSKVQSRCGSKDNIKHSAGGGNVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL
Protein: Dihydroorotate dehydrogenase (quinone), mitochondrial (EC 1.3.5.2) (Dihydroorotate oxidase) (G5EB61)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- dihydroorotase
- Orotate phosphoribosyltransferase
- Got1 family protein
- Orotidine 5'-phosphate decarboxylase
- Uncharacterized protein
- GMP synthase
- Multifunctional protein pyrABCN
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
- Carbamoyl phosphate synthase arginine-specific small chain
- Nitrate reductase
Sequence:
MATNSFRKLTFSGASRLGGCRRLPLTCRQLRFASDSGAAAATTKATAESAAESASINVKEAPKKAGRGLRRTVLGTSLALTLLVGYVYGTDTRASVHRYGVVPLIRALYPDAEDAHHIGVDTLKMLYKYGLHPRERGDPDGDGALATEVFGYTLSNPIGISGGLDKHAEIPDPLFAIGPAIVEVGGTTPLPQDGNPRPRVFRLPSQRAMINRYGLNSKGADHMAAILEQRVRDFAYANGFGAYDAAKQRVLDGEAGVPPGSLQPGKLLAVQVAKNKATPDGDIEAIKRDYVYCVDRVAKYADILVVNVSSPNTPGLRDLQATAPLTAILSAVVGAAKSVNRKTKPYVMVKVSPDEDSDEQVSGICDAVRASGVDGVIVGNTTNRRPDPIPQGYTLPAKEQATLKETGGYSGPQLFDRTVALVARYRSMLDAESETAGSAKDSAATIAQTEPGSENVPPVEAPSGLPRKVIFASGGITNGKQAHAVLDTGASVAMMYTGVVYGGVGTVTRVKQELRTAKKE
Protein: Protein-export protein SecB (Chaperone SecB) (P0AG86)
Organism: Escherichia coli (strain K12)
Function: One of the proteins required for the normal export of some preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. For 2 proteins (MBP, MalE and PhoA) the substrate is wrapped around the homotetramer, which prevents it from folding. It also specifically binds to its receptor SecA. Its substrates include DegP, FhuA, FkpA, GBP, LamB, MalE (MBP), OmpA, OmpF, OmpT, OmpX, OppA, PhoE, TolB, TolC, YbgF, YcgK, YgiW and YncE.
Subcellular location: Cytoplasm.
Interaction partners:
- Protein translocase subunit SecA
- Protein translocase subunit SecY
- Maltose/maltodextrin-binding periplasmic protein
- Protein translocase subunit SecE
- Membrane protein insertase YidC
- Protein-export membrane protein SecG
- Signal recognition particle receptor FtsY
- Sec translocon accessory complex subunit YajC
- Signal recognition particle protein
- Glutaredoxin 3
Sequence:
MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGAYCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
Protein: Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L6) (UbcM8) (Ubiquitin carrier protein L6) (Ubiquitin-protein ligase L6) (Q9QZU9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-like modifier-activating enzyme 7
- Ubiquitin-like protein ISG15
- E3 ubiquitin/ISG15 ligase TRIM25
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase ARIH1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Polyubiquitin-C
- Ubiquitin-conjugating enzyme E2 L3
Sequence:
MMASKRVAKELESLSKELPPYLRQLSSDDANVLVWHMLLLPDQLPYGLKAFQVRIDFPREYPFKPPTLRFTTKIYHPNVREDGLVCLPLISNENWKPYTKPYQVLEALNVLVSKPNLEEPVRLELADLLTQNPEMFRKKAEEFTLKFGVDRPS