wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-specific guanine nucleotide-releasing factor 2 (Ras-GRF2) (Ras guanine nucleotide exchange factor 2) (Q99JE4)
Organism: Rattus norvegicus (Rat)
Function: Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15128856}. Cell membrane {ECO:0000269|PubMed:15128856}; Peripheral membrane protein {ECO:0000269|PubMed:15128856}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15128856}; Peripheral membrane protein {ECO:0000269|PubMed:15128856}. Note=Translocates to membranes when activated (By similarity). Found both at cell periphery and along the axon of neurons. {ECO:0000250}.
Interaction partners:
- Ras-related protein R-Ras
- GTPase HRas
- GTPase NRas
- Ras-related protein M-Ras
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- RAS related 2
- Calmodulin-like protein 4
- Ras-specific guanine nucleotide-releasing factor 1
- Calmodulin-like protein 3
Sequence:
MQKSVRYNEGHALYLAFLARKEGTKRGFLSKKAAEASRWHEKWFALYQNVLFYFEGEQSGRPAGMYLLEGCSCERTPAPPRTNAGPAGARDALDKQYYFTVLFGHEGQKPLELRCEEEQAGKEWMEAIHQASYADILIEREVLMQKYIHLVQIVETEKIAANQLRHQLEDQDTEIERLKSEIVALNKTKERMRPYHTHQEEEDPDIKKIKKVQSFMRGWLCRRKWKTIVQDYICSPHAESMRKRNQIVFTMVEAESEYVHQLYILVNGFLRPLRMAASSKKPPISHDDVSSIFLNSETIMFLHEIFHQGLKARLANWPTLVLADLFDILLPMLNIYQEFVRNHQYSLQVLANCKQNRDFDKLLKQYEGNPACEGRMLETFLTYPMFQIPRYIITLHELLAHTPHEHVERKSLEFAKSKLEELSRVMHDEVSDTENIRKNLAIERMIVEGCDILLDTSQTFIRQGSLIQVPSVERGKLSKVRLGSLSLKKEGERQCFLFTKHFLICTRSSGGKLHLLKTGGVLSLIQCTLIEEPDTSDDDTKGPGHMFGHLDFKIVVEPPDAAPFTVVLLAPSRQEKAAWMSDISQCVDNIRCNGLMTIVFEENSKVTVPHMIKSDARLHKDDTDICFSKTLNSCKVPQIRYASVERLLERLTDLRFLSIDFLNTFLHTYRIFTTAAVVLGKLSDIYKRPFTSIPVRSLELFFATSQNNREHLVDGKSPRLCRKFSSPPPLAVSRTSSPVRARKLSLTSSLNSRIGALDLTTSSSSSSPTTTVHSPAASPPPHTAVPESAPADRAGDSTDMSPCRSPSTTPRHLRYRQPGGQVADSTHCAVSPASAFAIATAAAGHGSPPGFNNERTCDKEFIIRRTATNRVLNVLRHWVSKHSQDFELNNELKMNVLNLLEEVLRDPDLLPQERKATANILRALSQDDQDDIHLKLEDIIQMTDCPKAECFETLSAMELAEQITLLDHIVFRSIPYEEFLGQGWMKLDKNERTPYIMKTSQHFNEMSNLVASQIMNYADISSRANAIEKWVAVADICRCLHNYNGVLEITSALNRSAIYRLKKTWTKVSKQTKALMDKLQKTVSSEGRFKNLRETLKNCNPPAVPYLGMYLTDLAFIEEGTPNFTEEGLVNFSKMRMISHIIREIRQFQQTAYRIDQQPKVIQYLLDKALVIDEDTLYELSLKIEPRLPA
Protein: Ureidoacrylate amidohydrolase RutB (EC 3.5.1.110) (P75897)
Organism: Escherichia coli (strain K12)
Function: Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
Interaction partners:
- 3-aminoacrylate deaminase RutC
- Pyrimidine monooxygenase RutA
- FMN reductase RutF
- Putative carbamate hydrolase RutD
- Probable malonic semialdehyde reductase RutE
- Putative pyrimidine permease RutG
- Probable hydrolase YcaC
- NADP-dependent 3-hydroxy acid dehydrogenase YdfG
- HTH-type transcriptional regulator RutR
Sequence:
MTTLTARPEAITFDPQQSALIVVDMQNAYATPGGYLDLAGFDVSTTRPVIANIQTAVTAARAAGMLIIWFQNGWDEQYVEAGGPGSPNFHKSNALKTMRKQPQLQGKLLAKGSWDYQLVDELVPQPGDIVLPKPRYSGFFNTPLDSILRSRGIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLEDATHQAGPKFAQKAALFNIETFFGWVSDVETFCDALSPTSFAHIA
Protein: Membrane protein MLC1 (Megalencephalic leukoencephalopathy with subcortical cysts protein 1) (Q15049)
Organism: Homo sapiens (Human)
Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:22328087}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22328087}. Endoplasmic reticulum {ECO:0000269|PubMed:22328087}.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin light polypeptide 6
- Myosin light chain 6B
Sequence:
MTQEPFREELAYDRMPTLERGRQDPASYAPDAKPSDLQLSKRLPPCFSHKTWVFSVLMGSCLLVTSGFSLYLGNVFPAEMDYLRCAAGSCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLVLNPSAININFNLILLLLLELLMAATVIIAARSSEEDCKKKKGSMSDSANILDEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACFPSAIASHVAAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSIMRIVEMFKDYPPAIKPSYDVLLLLLLLVLLLQAGLNTGTAIQCVRFKVSARLQGASWDTQNGPQERLAGEVARSPLKEFDKEKAWRAVVVQMAQ
Protein: Nuclear transcription factor Y subunit B-5 (AtNF-YB-5) (O82248)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit C-7
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit A-1
- Nuclear transcription factor Y subunit A-9
- Nuclear transcription factor Y subunit C-6
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit A-3
- Nuclear transcription factor Y subunit C-10
Sequence:
MAGNYHSFQNPIPRYQNYNFGSSSSNHQHEHDGLVVVVEDQQQEESMMVKEQDRLLPIANVGRIMKNILPANAKVSKEAKETMQECVSEFISFVTGEASDKCHKEKRKTVNGDDICWAMANLGFDDYAAQLKKYLHRYRVLEGEKPNHHGKGGPKSSPDN
Protein: HL07956p (Mitochondrial ribosomal protein L18) (Q7JVK1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein mL44
- Small ribosomal subunit protein mS25
- GH05406p
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL23m
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein bL35m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL20m
Sequence:
MSRSARPLTSARVLHKIKELTTPQASTEYVINRNPRNLERLRIAYKPVGYHLEKPGRSYWHTLEINTSGRYVSGDVKHFENGTILSASTSEWAIKQQLYKTNDTSAFVNLGRVLAQRCLQSGITEMTCNVEAVPGSKLQKLLQTIQDNGVSFKEPSRLPNEQPWDEKRHEKPWEVSEDALEAPKSK
Protein: Centaurin-gamma-1A (Q9NGC3)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTPase-activating protein for the ADP ribosylation factor family.
Interaction partners:
Sequence:
MSNYHPHSHPHALSHPHPQQVHNQLQNPHQNQLPPPQRHNHAAPTAAASASGAPSSSASASASASILVAHPPQPLISNSLAIRQEIQRFESVHPSIYAIYELIDLLPMADAQIAQSIRDHVVCIEDSFVNSQEWTISRSVPDLRLGIVGSLNSGKSALVHRYLTGSYMQEESPEGGRFKKEVFIDGQSYLLLIRDEGGAPEMQFAGWVDAVIFVFSLENEGSFNTVYNYYTKMAHFRNGQEIPMILVGTQDAISERNPRVIDDTRARKLASDLKRCSYYETCATYGLNVERVFQDACQKILSQRLPLPPQVQPARPTTPQGNRLGLAPYQAPTNGQRGQQQLPLRMSADFAQAEQKLWSLQAASSSTINENNNITKYNPGAANSLQGDCSQVQLRDPRDLAPPPGKELPTPTSTPTTSRKSRRRSNLFIPSSSKKADKEKEPKSSELGSGRSIPIKQGYLYKRSSKSLNKEWKKKYVTLCDDGRLTYHPSLHDYMDDVHGKEIPLQYVTVKVPGQKPRGSKSIITNSALTSSLMANGQRAQNTLSDGIGCLTLAKDNQRKLSEKLSLLGAGSIAAGAGGEPLKSNSSQQTSGDEGIAMSNSNSQTFIAGEVANAGNKLEAQTPNVKKRHRRMKSSSVKANEADDNDGYEFYIVSLDSKQWHFEAANSEERDEWVAAVEQEIFKSLQSIESSKTKQATSTDLAAMLAIRQRVPGNGFCVDCGAPNPEWASLNLGVLMCIECSGVHRNLGSHISKVRSLGLDDWPSPHLSVMLAIGNSLANSVWESNTRQRVKPTSQASREDKERWVRSKYEAKEFLTPLGNGSSAHPSPSPGQQLIEAVIRADIKSIVSILANCPSEVTNANVSARDVRTPLLLACAIGNLAIAQLLIWNGANIKHTDHEGRTCLAYARAAQSLATAKSIKAAAAAQAGTTIPAPAPPTNGGIPAPQYNVEDTTALVELLEGLGCPEAAPLTASGTLPRRRDTLGTPYEKSVSGVI
Protein: Gastric inhibitory polypeptide (Glucose-dependent insulinotropic polypeptide) (A1DPK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKAAMFALVLICLGSVWPSAGSQPLDSSIIHSSPNDIQKLSRRYAESTIASDISKIVDSMVQKNFVNFLLNQREKKSEPALTEDPESHIFNDLLKKEFVMWIQSKGDTFKNQ
Protein: Kit ligand (Hematopoietic growth factor KL) (Mast cell growth factor) (MGF) (Steel factor) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)] (P20826)
Organism: Mus musculus (Mouse)
Function: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:P21583}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P21583}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P21583}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P21583}. Cell projection, filopodium {ECO:0000250|UniProtKB:P21583}.; SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted {ECO:0000250}.
Interaction partners:
- Mast/stem cell growth factor receptor Kit
- Interleukin-3
- Platelet-derived growth factor receptor alpha
- Fms-related tyrosine kinase 3 ligand
- Receptor-type tyrosine-protein kinase FLT3
- Thrombopoietin
- Epidermal growth factor receptor
- Platelet-derived growth factor receptor beta
- C-X-C chemokine receptor type 4
- Insulin receptor
Sequence:
MKKTQTWIITCIYLQLLLFNPLVKTKEICGNPVTDNVKDITKLVANLPNDYMITLNYVAGMDVLPSHCWLRDMVIQLSLSLTTLLDKFSNISEGLSNYSIIDKLGKIVDDLVLCMEENAPKNIKESPKRPETRSFTPEEFFSIFNRSIDAFKDFMVASDTSDCVLSSTLGPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAAKAPEDSGLQWTAMALPALISLVIGFAFGALYWKKKQSSLTRAVENIQINEEDNEISMLQQKEREFQEV
Protein: Mitoferrin-2 (Mitochondrial RNA-splicing protein 3/4 homolog) (MRS3/4) (Mitochondrial iron transporter 2) (Solute carrier family 25 member 28) (Q8R0Z5)
Organism: Mus musculus (Mouse)
Function: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96A46}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Asparaginyl-tRNA synthetase
- ATP-binding cassette sub-family B member 10, mitochondrial
- Frataxin, mitochondrial
- Ferrochelatase, mitochondrial
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- Ferritin, mitochondrial
Sequence:
MELEGRSAGGVAGGPAAGPGRSPGESALLDGWLQRGVGRGAGGGEAGAYQPPVRLDPESGPEYEALPAGATVTTHMVAGAVAGILEHCVMYPIDCVKTRMQSLQPDPAARYRNVLEALWRIMRTEGLWRPMRGLNVTATGAGPAHALYFACYEKLKKTLSDVIHPGGNSHIANGAAGCVATLLHDAAMNPAEVVKQRMQMYNSPYHRVTDCVRAVWQNEGAGAFYRSYTTQLTMNVPFQAIHFMTYEFLQEHFNPQRRYNPSSHVLCGACAGAVAAAATTPLDVCKTLLNTQESLALNSNITGHITGMASAFRTVYQVGGVTAYFRGVQARVIYQIPSTAIAWSVYEFFKYLITKRQEEWRAGK
Protein: Cytochrome P450 3A2 (EC 1.14.14.1) (CYPIIIA2) (Cytochrome P450-PCN2) (Cytochrome P450/6-beta-A) (Testosterone 6-beta-hydroxylase) (P05183)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MDLLSALTLETWVLLAVILVLLYRLGTHRHGIFKKQGIPGPKPLPFLGTVLNYYKGLGRFDMECYKKYGKIWGLFDGQTPVFAIMDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIAFFQKFVHRIKETRLDSKHKHRVDFLQLMLNAHNNSKDEVSHKALSDVEIIAQSVIFIFAGYETTSSTLSFVLYFLATHPDIQKKLQEEIDGALPSKAPPTYDIVMEMEYLDMVLNETLRLYPIGNRLERVCKKDIELDGLFIPKGSVVTIPTYALHHDPQHWPKPEEFHPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALMNMKLALTKVLQNFSFQPCKETQIPLKLSRQAILEPEKPIVLKVLPRDAVINGA
Protein: Methyltransferase (Q9M005)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g25690
- Probable pectinesterase 8
- Uncharacterized protein At3g53670; F4P12.370
- Probable pectinesterase/pectinesterase inhibitor 7
- Pectinesterase/pectinesterase inhibitor 18
Sequence:
METSMGKPSFLRNIMVRVLLFGVLIIVVRFAYVVTITGESCNRGDFCFFSLPENLNFVISGAASGSSAIDAIRSTSPGDDLYTTRDWIKSVQFYSSIFQDLIADGYLSPESKTLCVETAIGQEVHSLREIGVKNSVGISKKASRPLVVRGEGHAIPFEDNAFDFVFSGGDRLGKSLKQLEFADEITRTLKPEGFAVVHVGATDTYSFNSFLDLFNSCRLVKMRDIDGFDPSMPHIREFVIQKYSEIDGGGHHHRGGGDSGGKCWIPGYKRDLIRDAEPLIQEEPLKPWITLKRNIKNIKYVPSMVDIRFKSRYVYVDVGARSYGSSIGSWFKKEYPKQNKTFDVFAIEADKAFHEEYKIKKKVNLLPYAAWVRNETLSFEINHDPGKEVEAKAKGRGMGRIQPVKKSDSSDLAGEVNLIQGFDFADWLKKSVRERDFVVMKMDVEGTEFDLIPRLIKTGAICLIDELFLECHYNRWQRCCPGQRSQKYNKTYNQCLELFNSLRQRGVLVHQWW
Protein: Uncharacterized protein (A0A1D8PP91)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Uncharacterized protein
- mRNA splicing protein
Sequence:
MSNAIDFGVVDDSEEPAVYTTFLPRPISALARVNLVLHEHPVVKYKTITRVRGGDEPLMSGEEERYGTEDERDTEKPLVEHNYDWSLQYLPGLQFGVVSIRRN
Protein: Aquaporin-9a (Q498W2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKQHCALKQRLFKEFLAEFLGTFVLVLFGCGSVAQTVLSRNTLGEPLTIHIGFSTGLMMGVYVSGGVSGGHLNPAVSLAMVILGKLKIWKFPVYVIAQMLGAFAGAAAVFGLYYDAFMEFTSGILSVTGINATGHIFSSYPGRHLTVLGGFVDQVVGTGMLVLCILAIVDGRNIGAPRGVEPLAVGVVLLGISVSMGLNCGYPLNPARDLGPRLFTALAGWGMEVFSTADYWWWIPVAGPLVGGVVGAVIYFLLIELHHSNHNDTPQEEPEEEEDEDEEEDSSLKDKYEMINMS
Protein: FKBP-type peptidyl-prolyl cis-trans isomerase FkpA (PPIase) (EC 5.2.1.8) (Rotamase) (P45523)
Organism: Escherichia coli (strain K12)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Periplasm.
Interaction partners:
- Periplasmic serine endoprotease DegP
- Chaperone SurA
- Thiol:disulfide interchange protein DsbC
- Chaperone protein Skp
- Thiol:disulfide interchange protein DsbA
- Periplasmic chaperone PpiD
- Chaperone protein HtpG
- Trigger factor
- FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
- Peptidyl-prolyl cis-trans isomerase B
Sequence:
MKSLFKVTLLATTMAVALHAPITFAAEAAKPATAADSKAAFKNDDQKSAYALGASLGRYMENSLKEQEKLGIKLDKDQLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSSAQAKMEKDAADNEAKGKEYREKFAKEKGVKTSSTGLVYQVVEAGKGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPPNSTLVFDVELLDVKPAPKADAKPEADAKAADSAKK
Protein: Immunoglobulin heavy variable 1-46 (Ig heavy chain V-I region DOT) (Ig heavy chain V-I region HG3) (Ig heavy chain V-I region Mot) (P01743)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy 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:
Sequence:
MDWTWRVFCLLAVAPGAHSQVQLVQSGAEVKKPGASVKVSCKASGYTFTSYYMHWVRQAPGQGLEWMGIINPSGGSTSYAQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCAR
Protein: ALF transcription elongation factor 3 (H7C4C2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
GNNRASHRKELRSSVTCEKRRTRGLSRIVPKSKEFIETESSSSSSSSDSDLESEQEEYPLSKAQTVAASASSGNDQRLKEAAANGGSGPRAPVGSINARTTSDIAKELEEQFYTLVPFGRNELLSPLKDSDEIRSLWVKIDLTLLSRIPEHLPQEPGVLSAPATKDSESAPPSHTSDTPAEKALPKSKRKRKCDNEDDYREIKKSQGEKDSSSRLATSTSNTLSANHCNMNINSVAIPINKNEKMLRSPISPLSDASKHKYTSEDLTSSSRPNGNSLFTSASSSKKPKADSQLQPHGGDLTKAAHNNSENIPLHKSRPQTKPWSPGSNGHRDCKRQKLVFDDMPRSADYFMQEAKRMKHKADAMVEKFGKALNYAEAALSFIECGNAMEQGPMESKSPYTMYSETVELIRYAMRLKTHSGPNATPEDKQLAALCYRCLALLYWRMFRLKRDHAVKYSKALIDYFKNSSKAAQAPSPWGASGNSVGSQGSLSNASALSPSTIVSIPQRIHQMAANHVSITNSILHSYDYWEMADNLAKENREFFNDLDLLMGPVTLHSSMEHLVQYSQQGLHWLRNSAHLS
Protein: Uncharacterized protein (Q384Y6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- IF rod domain-containing protein
- ODAD1 central coiled coil region domain-containing protein
- Flagellar attachment zone protein 1 conserved domain-containing protein
Sequence:
MDTSEEATDKANGSRRPSAEEQLRDLQEKTNLWKQSVAQQLSEATKKNKQLRDELKQVNANHGSEMGALRVQLEKEFRERTSLKDEELQNVQTQLMELRKEKRSMVEQHERDLEQAIARVRETCAVEHTMRTDAETQQHEAELHKLRDAMELKEKELALSEHEVCVMKTRLERLAEQYRELSALMTQNTTQLESGGDAANKEKVLENALKASDAAHQQQLETVRSEMSNLEERHAAKLREMQRAHELEQQRCMNEVYQREEQLATLQTLLHQAQHEAEAAQRRISNVRLEREQMEQQLTERVAGLSRELASRMEYAQQLAAEVNSLQRELGRQEGLVRSLEEEANMREEAFQTLLLSEENRALVMGLQEALQKSRDDAEAWARKYEEAVQQTKSTCAVPIGYPCDGNDGDERKFRELAQREKALEEENLRLQTKAKLLRAMELRLEELKRSMASQASTILEHHNSGNRGSRMGDSRYGEERKGSRSASPLRRMQLMWNQHSSVSGRLSRCAFELSRCRLPQCMLLFAFCVALLLIIFVVRSFSL
Protein: Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide (E9PFG0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFELLNSGQSIRTVLTF
Protein: Chaperone protein ClpB (ClpB disaggregase) (Heat shock protein F84.1) (P63284)
Organism: Escherichia coli (strain K12)
Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8376377}.
Interaction partners:
- Chaperone protein DnaK
- Protein GrpE
- Chaperone protein DnaJ
- Chaperone protein HtpG
- Small heat shock protein IbpA
- Chaperonin GroEL
- ATP-dependent protease ATPase subunit HslU
- Small heat shock protein IbpB
- ATP-dependent Clp protease proteolytic subunit
- Co-chaperonin GroES
Sequence:
MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGDVQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIVAVQ
Protein: DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]) (P00970)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: DNA ligase, which is expressed in the early stage of lytic development, has been implicated in T4 DNA synthesis and genetic recombination. It may also play a role in T4 DNA repair.
Interaction partners:
Sequence:
MILKILNEIASIGSTKQKQAILEKNKDNELLKRVYRLTYSRGLQYYIKKWPKPGIATQSFGMLTLTDMLDFIEFTLATRKLTGNAAIEELTGYITDGKKDDVEVLRRVMMRDLECGASVSIANKVWPGLIPEQPQMLASSYDEKGINKNIKFPAFAQLKADGARCFAEVRGDELDDVRLLSRAGNEYLGLDLLKEELIKMTAEARQIHPEGVLIDGELVYHEQVKKEPEGLDFLFDAYPENSKAKEFAEVAESRTASNGIANKSLKGTISEKEAQCMKFQVWDYVPLVEIYSLPAFRLKYDVRFSKLEQMTSGYDKVILIENQVVNNLDEAKVIYKKYIDQGLEGIILKNIDGLWENARSKNLYKFKEVIDVDLKIVGIYPHRKDPTKAGGFILESECGKIKVNAGSGLKDKAGVKSHELDRTRIMENQNYYIGKILECECNGWLKSDGRTDYVKLFLPIAIRLREDKTKANTFEDVFGDFHEVTGL
Protein: Inositol 1,4,5-triphosphate receptor associated 1 (Inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate) (JAW1-related protein MRVI1) (Protein MRVI1) (Q9Y6F6)
Organism: Homo sapiens (Human)
Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation.
Subcellular location: Cytoplasm, perinuclear region. Sarcoplasmic reticulum {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- cGMP-dependent protein kinase 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- cGMP-dependent protein kinase 2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
Sequence:
MGMDLTCPFGISPACGAQASWSIFGADAAEVPGTRGHSQQEAAMPHIPEDEEPPGEPQAAQSPAGQGPPAAGVSCSPTPTIVLTGDATSPEGETDKNLANRVHSPHKRLSHRHLKVSTASLTSVDPAGHIIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSPGDSPSAVSPNLSPSASPTSSRSNSLTVPTPPGLDVCSGPPSPLPGAPPQQKGDEADVSSPHPGEPNVPKGLADRKQNDQRKVSQGRLAPRPPPVEKSKEIAIEQKENFDPLQYPETTPKGLAPVTNSSGKMALNSPQPGPVESELGKQLLKTGWEGSPLPRSPTQDAAGVGPPASQGRGPAGEPMGPEAGSKAELPPTVSRPPLLRGLSWDSGPEEPGPRLQKVLAKLPLAEEEKRFAGKAGGKLAKAPGLKDFQIQVQPVRMQKLTKLREEHILMRNQNLVGLKLPDLSEAAEQEKGLPSELSPAIEEEESKSGLDVMPNISDVLLRKLRVHRSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEENTEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEVVGAVRQEKRMSKATEVMMQYVENLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLTLGKNMPRRRVSVAVVPKFNALNLPGQTPSSSSIPSLPALSESPNGKGSLPVTSALPALLENGKTNGDPDCEASAPALTLSCLEELSQETKARMEEEAYSKGFQEGLKKTKELQDLKEEEEEQKSESPEEPEEVEETEEEEKGPRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAVMLVLTVVLGLYNSYNSCAEQADGPLGRSTCSAAQRDSWWSSGLQHEQPTEQ
Protein: Nuclear envelope phosphatase-regulatory subunit 1 homolog (NEP1-R1) (Transmembrane protein 188) (Q9XXN3)
Organism: Caenorhabditis elegans
Function: May form with the serine/threonine protein phosphatase scpl-2 an active complex dephosphorylating and activating lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May play a role in nuclear membrane dynamics being crucial for early development of the embryo.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:Q8N9A8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N9A8}. Cytoplasm {ECO:0000250|UniProtKB:Q8N9A8}.
Interaction partners:
- CTD nuclear envelope phosphatase 1 homolog
- Phenylalanine-4-hydroxylase
- LNS2/PITP domain-containing protein
- Torsin
- Torsin
Sequence:
MAIQARRMPEDPSTACEDLKFFEKRLTEVITYMGPTCTRWRIAIVIFAVLVGVIGSKYFANEKIEIFQIPMIDMFLTTHLDFTLCFFVGLLLFAVFGVHRRIVAPTIVARRCRDALSPFSLSCDHNGKLIVKPAVRNSAP