wanglab/gogpt-training-data huggingface dataset:
Protein: Shal K[+] channel interacting protein, isoform G (A0A0B4K6C1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAVSNIVCEWLRALGLAQYAESFLDNGYDDLEICKQVGDPDLDAIGVENPAHRHKLLKSIRSLREKGAASVYFMLNDPNSLSGSMEILCETPPNNELELVLREQLETDGVRLTAHPYSTPDGQRGHLEGLASVYCELLMAPFGDILATIERARQAAWAERSPLHSAAQVVGGSGGAGGSTGSGSGGAASGGSGGSSGVLHHRQQHGHRGHSMHGAGLPNSHSQPIYVPGKYSPSSCLSDKEEDEIYGFGYGVFAPRVARGGLTQQQQLLQQQTLQTQQSIQQQQQQMQQQQQQLPIVPGQQQQGPHQHQTLPPNVAHLNFVQQNCLSPRSAYFYEFPPTAEGRETKKRTTLARLLKGLKTVNRRDRNNQQNGAQARAANDRLRHFQMINGGAGGQQHSFEETIHRLKVQEAMRKKEKFQREHEEILRDIRQGLLQMSRGEGRMDDTYMYDEALRTGGGMGIAGLGMPLGVGGNGGGGGAAHYAGGRVRFSNNRESTGVISLRSAGDISLPQRGPPRRGLIVPQQPPNPPTIIPLTHARSHDRESGDYAGSISDLQSVTSRFSTVSIGTNNCTARYRTLSGGIGESPSLSPSPSSDYEDIGVTRGHGCLPPSLLAAKAKKNGLPHGKANTICQKATVHHSGEMRSSAKEIGAFNENGRNFVATKDTSRDFSNSQDNTDRGSMSDQAFACSASSVESLPSASGSSTQALVRPGSPHSSISAEDRTSMASCICKAKALVDSLPNPYDKEALKFKKGDLIDVLSMNASGIWKGRCHGRVGHFKFINVEVLPEQRMKNSSSKTLAAGSRLANSGNGSHNGGPCSVEDLLIRIGLKEYTSVFVLNGYEDLELFKELEPADLDYLGILNQEHRAKLLTAVQLLHDIESTNFARTGSDVDIPGSSSENDEARLNNINMKHGASPFGRRHFPRDSGCYEGSPLPSSQTPTQAVNSTDESNSLDDVVTKCSSEIMKRVESARRCKDNPFKTTLPGGGRLGKKSFLGGNGLMADDTLTRGGLSEKSSDSGVSSSSLSSGPLKSST
Protein: S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (Q8J0F1)
Organism: Candida boidinii (Yeast)
Interaction partners:
Sequence:
MSTVGKTITCKAAVAWKPGEDLSIETIEVAPPKAHEVRIKIEYTGVCHTDAYTLSGADAEGEFPVVFGHEGAGIVESVGEGVTSVKVGDSVICLYTPECRECKFCKSGKTNLCGKIRATQGKGLMPDGTSRFTCKGQPLLHYMGCSTFSQYTVVADISVVAVNPEAPKDRTCLLGCGITTGYRAATNTVKMNEGDNIAVFGVGCIGLSVIQGAVAKKAGKIIAIDINDGKTEWAEKFGATDFVNPTKLAEGETIVSKLIDMTDGGCDFTFDCTGTVQVMRNALEACHKGWGESVIIGVAAAGKEISTRPFQLVTGRVWRGCAFGGVKGRTQMPGIVEDYLSGTLKVDEFITHRHKLDDINKAFHDMHAGDCIRAVITMEE
Protein: Villin-4 (O65570)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds actin and actin filament bundles in a Ca(2+)-insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Involved in root hair growth through regulating actin organization in a Ca(2+)-dependent manner.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21275995}.
Interaction partners:
- CLK4-associating serine/arginine-rich protein
- Nucleolar GTP-binding protein 1
- Brefeldin A-inhibited guanine nucleotide-exchange protein 1
- Conserved oligomeric Golgi complex subunit 6
- Nucleolar GTP-binding protein 1
- Conserved oligomeric Golgi complex subunit 4
Sequence:
MSVSMRDLDPAFQGAGQKAGIEIWRIENFIPTPIPKSSIGKFFTGDSYIVLKTTALKTGALRHDIHYWLGKDTSQDEAGTAAVKTVELDAALGGRAVQYREVQGHETEKFLSYFKPCIIPQEGGVASGFKHVVAEEHITRLFVCRGKHVVHVKEVPFARSSLNHDDIYILDTKSKIFQFNGSNSSIQERAKALEVVQYIKDTYHDGTCEVATVEDGKLMADADSGEFWGFFGGFAPLPRKTANDEDKTYNSDITRLFCVEKGQANPVEGDTLKREMLDTNKCYILDCGIEVFVWMGRTTSLDDRKIASKAAEEMIRSSERPKSQMIRIIEGFETVPFRSKFESWTQETNTTVSEDGRGRVAALLQRQGVNVRGLMKAAPPKEEPQVFIDCTGNLQVWRVNGQAKTLLQAADHSKFYSGDCYVFQYSYPGEEKEEVLIGTWFGKQSVEEERGSAVSMASKMVESMKFVPAQARIYEGKEPIQFFVIMQSFIVFKGGISSGYKKYIAEKEVDDDTYNENGVALFRIQGSGPENMQAIQVDPVAASLNSSYYYILHNDSSVFTWAGNLSTATDQELAERQLDLIKPNQQSRAQKEGSESEQFWELLGGKAEYSSQKLTKEPERDPHLFSCTFTKEVLKVTEIYNFTQDDLMTEDIFIIDCHSEIFVWVGQEVVPKNKLLALTIGEKFIEKDSLLEKLSPEAPIYVIMEGGEPSFFTRFFTSWDSSKSAMHGNSFQRKLKIVKNGGTPVADKPKRRTPASYGGRASVPDKSQQRSRSMSFSPDRVRVRGRSPAFNALAATFESQNARNLSTPPPVVRKLYPRSVTPDSSKFAPAPKSSAIASRSALFEKIPPQEPSIPKPVKASPKTPESPAPESNSKEQEEKKENDKEEGSMSSRIESLTIQEDAKEGVEDEEDLPAHPYDRLKTTSTDPVSDIDVTRREAYLSSEEFKEKFGMTKEAFYKLPKWKQNKFKMAVQLF
Protein: Amine oxidase [flavin-containing] B (EC 1.4.3.21) (EC 1.4.3.4) (Monoamine oxidase type B) (MAO-B) (Q8BW75)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially degrades benzylamine and phenylethylamine (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Catechol O-methyltransferase
- Transmembrane O-methyltransferase homolog
- Aromatic-L-amino-acid decarboxylase
- Dopamine beta-hydroxylase
- Amine oxidase [copper-containing] 3
- E3 ubiquitin-protein ligase parkin
- Amine oxidase
- Amine oxidase
- Histamine N-methyltransferase
- Diamine oxidase [copper-containing]
Sequence:
MSNKSDVIVVGGGISGMAAAKLLHDCGLSVVVLEARDRVGGRTYTIRNKNVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHFVKGKSYAFRGPFPPVWNPITYLDNNNLWRTMDEMGQEIPSDAPWKAPLAEEWDYMTMKELLDKICWTKSTKQIATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFIGGSGQVSERIKDILGDRVKLERPVIHIDQTGENVIVKTLNHEIYEAKYVISAIPPALGMKIHYSPPLPMLRNQLISRVPLGSVIKCMVYYKEPFWRKKDFCGTMVIEGEEAPIAYTLDDTKPDGTYAAIMGFILAHKARKLVRLTKEERLRKLCELYAKVLNSQEALQPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVGKIFFAGTETASHWSGYMEGAVEAGERAAREILHAIGKIPEDEIWQPEPESLDVPARPITSTFLERHLPSVPGLLKLFGLTTILSATALGFLAHKRGLFVHF
Protein: Transcription factor GLABRA 3 (Basic helix-loop-helix protein 1) (AtMYC6) (AtbHLH1) (bHLH 1) (Protein SHAPESHIFTER) (Transcription factor EN 31) (bHLH transcription factor bHLH001) (Q9FN69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator, when associated with MYB75/PAP1, MYB90/PAP2 or TT2. Involved in epidermal cell fate specification. Regulates negatively stomata formation, but, in association with TTG1 and MYB0/GL1, promotes trichome formation, branching and endoreplication. Regulates also trichome cell wall maturation. Together with MYB66/WER, promotes the formation of non-hair cells in root epidermis cells in the N position. Whereas together with CPC, promotes the formation of hair cells in root epidermis cells in the H position by inhibiting non-hair cell formation. Seems also to play a role in the activation of anthocyanin biosynthesis, probably together with MYB75/PAP1. Activates the transcription of GL2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14561633, ECO:0000269|PubMed:15590742}. Note=Moves from developing hair cells (trichoblasts) to developing non-hair cells (atrichoblasts). Also detected in trichome nucleus.
Interaction partners:
- Transcription factor WER
- Protein TRANSPARENT TESTA GLABRA 1
- Transcription factor MYB114
- Transcription factor MYB113
- Transcription factor MYB75
- Transcription factor MYB23
- Transcription factor MYB90
- Transcription factor EGL1
- Trichome differentiation protein GL1
- Transcription factor TT2
Sequence:
MATGQNRTTVPENLKKHLAVSVRNIQWSYGIFWSVSASQSGVLEWGDGYYNGDIKTRKTIQASEIKADQLGLRRSEQLSELYESLSVAESSSSGVAAGSQVTRRASAAALSPEDLADTEWYYLVCMSFVFNIGEGMPGRTFANGEPIWLCNAHTADSKVFSRSLLAKSAAVKTVVCFPFLGGVVEIGTTEHITEDMNVIQCVKTSFLEAPDPYATILPARSDYHIDNVLDPQQILGDEIYAPMFSTEPFPTASPSRTTNGFDQEHEQVADDHDSFMTERITGGASQVQSWQLMDDELSNCVHQSLNSSDCVSQTFVEGAAGRVAYGARKSRVQRLGQIQEQQRNVKTLSFDPRNDDVHYQSVISTIFKTNHQLILGPQFRNCDKQSSFTRWKKSSSSSSGTATVTAPSQGMLKKIIFDVPRVHQKEKLMLDSPEARDETGNHAVLEKKRREKLNERFMTLRKIIPSINKIDKVSILDDTIEYLQELERRVQELESCRESTDTETRGTMTMKRKKPCDAGERTSANCANNETGNGKKVSVNNVGEAEPADTGFTGLTDNLRIGSFGNEVVIELRCAWREGVLLEIMDVISDLHLDSHSVQSSTGDGLLCLTVNCKHKGSKIATPGMIKEALQRVAWIC
Protein: Probable calcium-binding protein CML29 (Calmodulin-like protein 29) (Q9LF54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- Probable calcium-binding protein CML34
- Probable calcium-binding protein CML31
- Probable calcium-binding protein CML21
- IAA-leucine resistant 2
- Calcineurin b subunit-like protein
Sequence:
MADATEKAEHDRIFKKFDANGDGKISAAELEEALKTLGSVTADDVKRMMAEIDTDGDGNISYQEFTDFAGANRGLMKDVAKIF
Protein: Gasdermin-D (Gasdermin domain-containing protein 1) [Cleaved into: Gasdermin-D, N-terminal (GSDMD-NT) (mGSDMD-NTD) (p30); Gasdermin-D, C-terminal (GSDMD-CT) (mGSDMD-CTD) (p20); Gasdermin-D, p13 (Gasdermin-D, 13 kDa) (13 kDa GSDMD); Gasdermin-D, p40] (Q9D8T2)
Organism: Mus musculus (Mouse)
Function: Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-D, N-terminal) binds to membranes and forms pores, triggering pyroptosis.
Subcellular location: [Gasdermin-D]: Cytoplasm, cytosol {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. Inflammasome {ECO:0000269|PubMed:26611636}. Note=In response to a canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 inflammasone with similar kinetics to that of uncleaved CASP1 precursor. {ECO:0000269|PubMed:26611636}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cell membrane {ECO:0000269|PubMed:27339137, ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38538834}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P57764}. Secreted {ECO:0000269|PubMed:27383986}. Mitochondrion membrane {ECO:0000269|PubMed:37001519}. Note=Released in the extracellular milieu following pyroptosis (PubMed:27383986). Mitochondrial localization results in release of mitochondrial DNA into the cytosol (PubMed:37001519). {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:37001519}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cytoplasm, cytosol {ECO:0000269|PubMed:36227980}. Note=(Microbial infection) Upon infection by M.tuberculosis, localization to cell membrane is prevented by M.tuberculosis phosphatase PtpB that catalyzes dephosphorylation of phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol 4-phosphate, thereby inhibiting the membrane targeting of Gasdermin-D, N-terminal and subsequent cytokine release and pyroptosis. {ECO:0000269|PubMed:36227980}.; SUBCELLULAR LOCATION: [Gasdermin-D, p13]: Nucleus {ECO:0000269|PubMed:37327784}.; SUBCELLULAR LOCATION: [Gasdermin-D, C-terminal]: Cytoplasm, cytosol {ECO:0000305|PubMed:27339137}.
Interaction partners:
- Caspase-4
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 3
- Interferon-inducible protein AIM2
- NLR family CARD domain-containing protein 4
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 6
- Interleukin-1 beta
- Pyrin
- High mobility group protein B1
Sequence:
MPSAFEKVVKNVIKEVSGSRGDLIPVDSLRNSTSFRPYCLLNRKFSSSRFWKPRYSCVNLSIKDILEPSAPEPEPECFGSFKVSDVVDGNIQGRVMLSGMGEGKISGGAAVSDSSSASMNVCILRVTQKTWETMQHERHLQQPENKILQQLRSRGDDLFVVTEVLQTKEEVQITEVHSQEGSGQFTLPGALCLKGEGKGHQSRKKMVTIPAGSILAFRVAQLLIGSKWDILLVSDEKQRTFEPSSGDRKAVGQRHHGLNVLAALCSIGKQLSLLSDGIDEEELIEAADFQGLYAEVKACSSELESLEMELRQQILVNIGKILQDQPSMEALEASLGQGLCSGGQVEPLDGPAGCILECLVLDSGELVPELAAPIFYLLGALAVLSETQQQLLAKALETTVLSKQLELVKHVLEQSTPWQEQSSVSLPTVLLGDCWDEKNPTWVLLEECGLRLQVESPQVHWEPTSLIPTSALYASLFLLSSLGQKPC
Protein: Probable crossover junction endonuclease EME2 (EC 3.1.22.-) (A4GXA9)
Organism: Homo sapiens (Human)
Function: Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Structure-specific endonuclease subunit MUS81
- Structure-specific endonuclease subunit EME1
- DNA repair endonuclease XPF
- Fanconi anemia core complex-associated protein 24
- Fanconi anemia group M protein
- Structure-specific endonuclease subunit SLX4
- Exonuclease 1
- DNA replication ATP-dependent helicase/nuclease DNA2
Sequence:
MARVGPGRAGVSCQGRGRGRGGSGQRRPPTWEISDSDAEDSAGSEAAARARDPAGERRAAAEALRLLRPEQVLKRLAVCVDTAILEDAGADVLMEALEALGCECRIEPQRPARSLRWTRASPDPCPRSLPPEVWAAGEQELLLLLEPEEFLQGVATLTQISGPTHWVPWISPETTARPHLAVIGLDAYLWSRQHVSRGTQQPESPKVAGAEVAVSWPEVEEALVLLQLWANLDVLLVASWQELSRHVCAVTKALAQYPLKQYRESQAFSFCTAGRWAAGEPVARDGAGLQAAWRRQIRQFSRVSPAVADAVVTAFPSPRLLQQALEACSTERERMGLLADLPVPPSEGGRPRRVGPDLSRRICLFLTTANPDLLLDLGS
Protein: Protein PRRC1 (Proline-rich and coiled-coil-containing protein 1) (Q96M27)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:15541471}. Cytoplasm {ECO:0000250|UniProtKB:Q5XJA3}.
Interaction partners:
- Protein transport protein Sec23A
- Protein transport protein Sec24C
Sequence:
MMEESGIETTPPGTPPPNPAGLAATAMSSTPVPLAATSSFSSPNVSSMESFPPLAYSTPQPPLPPVRPSAPLPFVPPPAVPSVPPLVTSMPPPVSPSTAAAFGNPPVSHFPPSTSAPNTLLPAPPSGPPISGFSVGSTYDITRGHAGRAPQTPLMPSFSAPSGTGLLPTPITQQASLTSLAQGTGTTSAITFPEEQEDPRITRGQDEASAGGIWGFIKGVAGNPMVKSVLDKTKHSVESMITTLDPGMAPYIKSGGELDIVVTSNKEVKVAAVRDAFQEVFGLAVVVGEAGQSNIAPQPVGYAAGLKGAQERIDSLRRTGVIHEKQTAVSVENFIAELLPDKWFDIGCLVVEDPVHGIHLETFTQATPVPLEFVQQAQSLTPQDYNLRWSGLLVTVGEVLEKSLLNVSRTDWHMAFTGMSRRQMIYSAARAIAGMYKQRLPPRTV
Protein: D-tagatose-1,6-bisphosphate aldolase subunit KbaZ (P0C8K0)
Organism: Escherichia coli (strain K12)
Function: Component of the tagatose-1,6-bisphosphate aldolase KbaYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of KbaY. When expressed alone, KbaZ does not show any aldolase activity.
Interaction partners:
- D-tagatose-1,6-bisphosphate aldolase subunit KbaY
- Putative D-galactosamine-6-phosphate deaminase AgaS
- D-tagatose-1,6-bisphosphate aldolase subunit GatY
- Putative aga operon transcriptional repressor
- D-tagatose-1,6-bisphosphate aldolase subunit GatZ
- ATP-dependent 6-phosphofructokinase isozyme 1
- ATP-dependent 6-phosphofructokinase isozyme 2
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- N-acetylgalactosamine-specific phosphotransferase enzyme IIB component 2
- KHG/KDPG aldolase
Sequence:
MKHLTEMVRQHKAGKTNGIYAVCSAHPLVLEAAIRYASANQTPLLIEATSNQVDQFGGYTGMTPADFRGFVCQLADSLNFPQDALILGGDHLGPNRWQNLPAAQAMANADDLIKSYVAAGFKKIHLDCSMSCQDDPIPLTDDIVAERAARLAKVAEETCLEHFGEADLEYVIGTEVPVPGGAHETLSELAVTTPDAARATLEAHRHAFEKQGLNAIWPRIIALVVQPGVEFDHTNVIDYQPAKASALSQMVENYETLIFEAHSTDYQTPQSLRQLVIDHFAILKVGPALTFALREALFSLAAIEEELVPAKACSGLRQVLEDVMLDRPEYWQSHYHGDGNARRLARGYSYSDRVRYYWPDSQIDDAFAHLVRNLADSPIPLPLISQYLPLQYVKVRSGELQPTPRELIINHIQDILAQYHTACEGQ
Protein: Brivido-1 (MIP06652p) (Q9VVZ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Transient receptor potential cation channel trpm
Sequence:
MAKKFSNIIFYLTLIIIAICVACIWMFSGFRHEYGKFNMILVAFLAVTLLQILIFTPIKFTIMSLDAAFWPAHQAPETPDENANVDTFMDNLRLRLRTLRSELMITERHRNERVNLKYRLITEELWLTGKLFLVYFFMALAFFDELLYFNTEATELLFQCNHGDAFGLLSVGDVPDIYFFVVSSLVLAFTDGKNTSGGAPWIHAEGTRLLGVVRLRQLRTESNRLGLSLPVFTERDFSESWTLPYERVPYTDKYWPIYTPWLPSVSVARDNLLMGINHVGHMFNYPESKGYKVLLSDTRHKSLKIIDYLMKKNWLDANTTALFMDFSLYNADANTFTVCTLWVEKFPYQYPDGHTRIESHTFVEQLREFTKFGMLMVFVFVVTWLQFTKAFFLKVWYDPRQLKTLWVQVDAMIVALSLVVGMIMSVRDNLVQKMIKSVEIAVVVDFLDFREPAQLAYLEDVVTGLAVALVTMRLWKVLQFSATFQLFTKTIAMAWDALLCTFVITVIFIIAIGIATVTINGNYTSNFRDFPKGIVTVTCFAFGYTNLVYPPDIFYGGEWLGILLYTIMGFVVKYMLINLIVSMMRDQMASVKADRDKKVRQRITFWQFLRVEYAHFINYIVKVFHCQKGYQRKNRTVAQNIQRKLNSNELKRRKTKISSIYSETIYVMPIDKDLEQMKYRERIERTFTLAAILHTQMELMERLMFGDEEGNLPSLDQEDEQVPETEED
Protein: Slit2 protein (Q90Z44)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
GASGVNELLLTSNRLETVRDKMFKGLESLKTLMLRSNRVSCVGNDSFTGLSSVRLLSLYDNQITTVAPGSFDTLHSLSTLNLLANPFNCNCHLAWLGDWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPAECTCLDTVVRCSNKGLKALPKGIPKDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPARTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQGPVDVNILAKCNPCLSNPCKNDGTCNNDPVDFYRCTCPYGFKGQDCDIPIHACISNPCNHGGTCHLKEGEKDGFWCTCADGFEGENCEINVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCEEKLDFCAQNLNPCQHDSKCILTPKGYKCDCTPGYVGEHCDIDFDDCQDNKCKNGAQCTDAVNGYTCICPEGYSGLFCEFSPPMVLPRTSPCDNYECQNGAQCIVKESEPICQCLSGYQGEKCEKLISINFVNKESYLQIPSAKIHSQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRVSYDTGSYPASAIYSVETINDGNFHIVELLAMDQILSLSIDGGSPKIITNLSKQSTLNFDSPLYVGGMPVKNNIAALRQSPGQNGTSFHGCIRNLYINSELQDFRNVPLQVGILPGCEPCHKKVCVHGTCHATSQSSFTCECEGGWTGPLCDQQTNDPCLGNKCVHGTCLPINAFSYSCKCLQGHGGVLCDEEEMLFNPCQSIRCKHGKCRLSGLGKPYCECSSGYTGDSCDKEISCRGERIRDYYQKQQGYAACQTTKKVSRLECKGGCSTGQCCGPLRSKRRKYSFECTDGSSFVDEIEKVVKCGCTNCPS
Protein: Carnitine O-palmitoyltransferase 1, muscle isoform (CPT1-M) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, muscle isoform) (CPT I) (CPTI-M) (Carnitine palmitoyltransferase 1B) (Carnitine palmitoyltransferase I-like protein) (Q63704)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:8636126}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Carnitine O-palmitoyltransferase 1, liver isoform
- Palmitoyl thioesterase CPT1C
- Long-chain-fatty-acid--CoA ligase 1
- Fatty acid CoA ligase Acsl3
- Long-chain-fatty-acid--CoA ligase 5
- Putative mitochondrial transporter UCP3
- [Pyruvate dehydrogenase
- Long-chain-fatty-acid--CoA ligase 6
- Mitochondrial brown fat uncoupling protein 1
Sequence:
MAEAHQAVAFQFTVTPDGVDFRLSREALRHIYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVVMATVGSNYCKVDISMGLVHCIQRCLPTRYGSYGTPQTETLLSMVIFSTGVWATGIFLFRQTLKLLLSYHGWMFEMHSKTSHATKIWAICVRLLSSRRPMLYSFQTSLPKLPVPSVPATIHRYLDSVRPLLDDEAYFRMESLAKEFQDKIAPRLQKYLVLKSWWATNYVSDWWEEYVYLRGRSPIMVNSNYYAMDFVLIKNTSQQAARLGNTVHAMIMYRRKLDREEIKPVMALGMVPMCSYQMERMFNTTRIPGKETDLLQHLSESRHVAVYHKGRFFKVWLYEGSCLLKPRDLEMQFQRILDDTSPPQPGEEKLAALTAGGRVEWAEARQKFFSSGKNKMSLDTIERAAFFVALDEDSHCYNPDDEASLSLYGKSLLHGNCYNRWFDKSFTLISCKNGQLGLNTEHSWADAPIIGHLWEFVLATDTFHLGYTETGHCVGEPNTKLPPPQRMQWDIPEQCQTAIENSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDKGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVRAMMTGSHKKQDLQDLFRKASEKHQNMYRLAMTGAGIDRHLFCLYIVSKYLGVRSPFLDEVLSEPWSLSTSQIPQFQICMFDPKQYPNHLGAGGGFGPVADHGYGVSYMIAGENTMFFHVSSKLSSSETNALRFGNHIRQALLDIADLFKISKTDS
Protein: Lipoprotein LprI (Glycolipoprotein LprI) (Lysozyme inhibitor LprI) (P9WK41)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Strongly binds and inhibits lysozyme, may help bacteria survive in lysozyme-producing host cells. When overexpressed in M.tuberculosis or M.smegmatis increases resistance to hen egg white lysozyme. M.smegmatis overexpressing LprI survive better during intracellular infection of peritoneal and monocyte-derived macrophages, both of which produce lysozyme during infection; M.smegmatis does not encode this protein. Somewhat better survival is seen in human cell lines when M.smegmatis cells express both proteins from this operon, i.e. GlbN (HbN) and LprI.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:26589796}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:26589796}. Secreted, cell wall {ECO:0000269|PubMed:26589796}. Cell surface {ECO:0000269|PubMed:26589796}. Note=Protein is accessible to externally added trypsin and alpha-D-mannosidase. {ECO:0000269|PubMed:26589796}.
Interaction partners:
Sequence:
MRWIGVLVTALVLSACAANPPANTTSPTAGQSLDCTKPATIVQQLVCHDRQLTSLDHRLSTAYQQALAHRRSAALEAAQSSWTMLRDACAQDTDPRTCVQEAYQTRLVQLAIADPATATPPVLTYRCPTQDGPLTAQFYNQFDPKTAVLNWKGDQVIVFVELSGSGARYGRQGIEYWEHQGEVRLDFHGATFVCRTS
Protein: Forkhead box protein R1 (Forkhead box protein N5) (Q6PIV2)
Organism: Homo sapiens (Human)
Function: Transcription factor which acts as both an activator and a repressor. Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress. Required for normal brain development (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:34723967}. Cytoplasm {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:34723967}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25609838}. Note=Localizes to the nucleus and cytoplasm with higher levels in the nucleus where it is expressed in a diffuse manner (PubMed:34723967). Located in the cytoplasm of spermatocytes and strongly accumulates at the perinuclear region in elongated spermatids (PubMed:25609838). {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:34723967}.
Interaction partners:
- Myc proto-oncogene protein
- Histone acetyltransferase KAT5
- E1A-binding protein p400
- MRG/MORF4L-binding protein
- Bromodomain-containing protein 8
- Enhancer of polycomb homolog 2
- Mortality factor 4-like protein 1
- Enhancer of polycomb homolog 1
- Chromatin modification-related protein MEAF6
- YEATS domain-containing protein 4
Sequence:
MGNELFLAFTTSHLPLAEQKLARYKLRIVKPPKLPLEKKPNPDKDGPDYEPNLWMWVNPNIVYPPGKLEVSGRRKREDLTSTLPSSQPPQKEEDASCSEAAGVESLSQSSSKRSPPRKRFAFSPSTWELTEEEEAEDQEDSSSMALPSPHKRAPLQSRRLRQASSQAGRLWSRPPLNYFHLIALALRNSSPCGLNVQQIYSFTRKHFPFFRTAPEGWKNTVRHNLCFRDSFEKVPVSMQGGASTRPRSCLWKLTEEGHRRFAEEARALASTRLESIQQCMSQPDVMPFLFDL
Protein: Endophilin-B1 (SH3 domain-containing GRB2-like protein B1) (A0A087WW40)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004450}.
Interaction partners:
Sequence:
MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKIWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETRNSQLNSARLEGDNIMVNFSYMLNFLHVKWLKSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYLSNNNQTSVTPVPSVLPNAIGSSAMASTSGLVITSPSNLSDLKECSGSRKARVLYDYDAANSTELSLLADEVITVFSVVGMDSDWLMGERGNQKGKVPITYLELLN
Protein: Polymerase basic protein 2 (RNA-directed RNA polymerase subunit P3) (Q8QPG7)
Organism: Influenza A virus (strain A/Duck/Hong Kong/2986.1/2000 H5N1 genotype C)
Function: Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062}.
Interaction partners:
Sequence:
MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIIEMIPERNEQGQTLWSKTNDAGSDRVMVSPLAVTWWNRNGPTTSAVYYPKVYKTYFEKVERLKHGTFGPVHFRNQIKIRRRVDINPGHADLNAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKIAPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVIQSMIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGTSVKKEEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEPIDNVMGMIGILPDMTPSTEMSLRGVRVSKMGVDEYSSTERVVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLAITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQDPTMLYNKMEFEPFQSLVPKAARGQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEQSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGALTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN
Protein: Protein AC54 (P41458)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Structural protein that participates in nucleocapsid assembly. Plays an essential role in the proper localization of the major capsid protein VP39, and the minor capsid protein 38K into the capsid assembly site.
Subcellular location: Virion {ECO:0000269|PubMed:23720732, ECO:0000269|PubMed:9188569}. Note=Present in both the budded virus (BV) and the occluded virus (OV). The occluded form allows the virus to be transmitted from insect to insect through ingestion of contaminated food while the budded form is responsible for the dissemination of infection throughout the insect host. {ECO:0000269|PubMed:9188569}.
Interaction partners:
Sequence:
MCSTKKPIKLDLCASVKLTPFKPMRPPKPMQCWIHPRRANCKVTRPRNNYSDPDNENDMLHMTVLNSVFLNEHAKLYYRHLLRNDQAEARKTILNADSVYECMLIRPIRTEHFRSVDEAGEHNMSVLKIIIDAVIKYIGKLADDEYILIADRMYVDLIYSEFRAIILPQSAYIIKGDYAESDSESGQSVDVCNELEYPWKLITANNCIVSTDESRQSQYIYRTFLLYNTVLTAILKQNNPFDVIAENTSISIIVRNLGSCPNNKDRVKCCDLNYGGVPPGHVMCPPREITKKFFHYAKWVRNPNKYKRYSELIARQSETGGGSASLRENVNNQLHARDVSQLHLLDWENFMGEFSSYFGLHAHNV