wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleotide-binding protein Rv1421 (P9WFQ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Displays ATPase and GTPase activities.
Interaction partners:
- Putative gluconeogenesis factor
- Probable cell division protein WhiA
- UvrABC system protein C
- Phosphoenolpyruvate transferase
- Riboflavin biosynthesis protein RibBA
- Ribonuclease E
Sequence:
MMNHARGVENRSEGGGIDVVLVTGLSGAGRGTAAKVLEDLGWYVADNLPPQLITRMVDFGLAAGSRITQLAVVMDVRSRGFTGDLDSVRNELATRAITPRVVFMEASDDTLVRRYEQNRRSHPLQGEQTLAEGIAAERRMLAPVRATADLIIDTSTLSVGGLRDSIERAFGGDGGATTSVTVESFGFKYGLPMDADMVMDVRFLPNPHWVDELRPLTGQHPAVRDYVLHRPGAAEFLESYHRLLSLVVDGYRREGKRYMTIAIGCTGGKHRSVAIAEALMGLLRSDQQLSVRALHRDLGRE
Protein: Mitochondrial chaperone BCS1 (BCS1-like protein) (Q9VL22)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
- AT01695p
- Caseinolytic protease chaperone subunit, isoform C
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein bL19m
- AT02348p
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL27m
- Mitochondrial ribosome-associated GTPase 1
Sequence:
MTLPDLVAGLSSNPYFGAGFGLFGVGAAAAILRKGLQGGVILFRRHCMITLEVPCRDKSYQWLLKWITIRGARKTQHLSVETNFVQNDNGTIKTSYDFIPSIGKHLFQYKGNWIQVERTREQQTLDLHMGVPWETVTLTAFGNNKGIYFDILEEARQLALEATEGKTVLYTAMGAEWRPFGHPRRRRPTGSVVLDRGTSQRIIADCQDFIKSSLWYTQRGIPYRRGYLLYGPPGCGKSSFITALAGELEYSVCLLNLSERGLTDDRLNHLLNVAPEQSIILLEDIDAAFVSREATPQQKSAFDGLNRITFSGLLNCLDGVGSTEARIVFMTTNYIDRLDPALVRPGRIDLKEYIGYCTQYQLEEMFKNFFASSDTTKAEEFGKRVNSFGRSASPAQIQGFFMKHKLSSPQTVIDSCEDIWENVLDHNKKIN
Protein: TBC1 domain family member 1 (Q60949)
Organism: Mus musculus (Mouse)
Function: May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:7566974}.
Interaction partners:
- Ras-related protein Rab-8A
- Ras-related protein Rab-10
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-3
- 5'-AMP-activated protein kinase subunit gamma-1
- Ras-related protein Rab-2A
- 5'-AMP-activated protein kinase subunit gamma-2
- Ras-related protein Rab-14
- 5'-AMP-activated protein kinase subunit beta-1
Sequence:
MEAITFTARKHPFPNEVSVDFGLQLVGSLPVHSLTTMPMLPWVVAEVRRLSGQCSKKEPRTKQVRLWVSPSGLRCEPDLEKSQPWDPLICSSIFECKPQRVHKLIHNSHDPSYFACLIKEDAAHRQSLCYVFKADDQTKVPEIISSIRQAGKIARQEELRCPSEFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRRTDWEAPTGQPSAPGPRPMRKSFSQPGLRSLAFRKEFQDASLRSSTFSSFDNDIENHLIGGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGSGGFHFVCYVFQCTNEALVDEIMMTLKQAFTVAAVQQTAKAPAQLCEGCPLQGLHKLCERIEGMNSSKTKLELQKHLTTLTNQEQATIFEEVQKLRPRNEQRENELIISFLRCLYEEKQKEHSHTGEPKQTLQVAAENIGSDLPPSASRFRLDSLKNRAKRSLTESLESILSRGNKARGLQDHSASVDLDSSTSSTLSNTSKELSMGDKEAFPVSETSFKLLGSSDDLSSDSEGHIAEESALLSPQQAFRRRANTLSHFPVECPAPPEPAQSSPGVSQRKLMRYHSVSTETPHERNVDHLPGGESQGCPGQPSAPPPPRLNPSASSPNFFKYLKHNSSGEQSGNAVPKSVSYRNALRKKLHSSSSVPNFLKFLAPVDENNTCDFKNTNRDFESKANHLGDTDGTPVKTRRHSWRQQIFLRVATPQKACDSPSRYEDYSELGELPPRSPLEPVCEDGPFGPVQEEKRKTSRELRELWKKAILQQILLLRMEKENQKLQASENDLLNKRLKLDYEEITPCLKEVTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRGEIWKFLAEQFHLKHPFPSKQQPKDVPYKELLKKLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLLHMSEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEHEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKNTLPNLGLVQMEKTISQVFEMDIAKQLQAYEVEYHVLQEELIESSPLSDNQRMEKLEKTNSSLRKQNLDLLEQLQVANARIQSLEATVEKLLTSESKLKQAALTLEVERSALLQMVEELRRQSARPSTPEPDCTQLEPTGD
Protein: Collagen alpha-6(VI) chain (Q8C6K9)
Organism: Mus musculus (Mouse)
Function: Collagen VI acts as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18276594}. Note=Deposed in the extracellular matrix of skeletal muscle.
Interaction partners:
- Platelet glycoprotein VI
- CD44 antigen
- Integrin alpha-9
- Integrin alpha-8
- Integrin alpha-6
- Integrin alpha-7
- Integrin beta-6
- Integrin alpha-11
- Integrin beta-4
- Integrin beta-8
Sequence:
MLLVLCLTMICFHVCVNQDSGPEYADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLKIGNALQEAHRTYFSAPTNGRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATSQFHFNLRTARDLSVFAPNMTEIIKDVTQYREGMADDIIVEACQGPSVADVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVGQAYTGAALRKTRKEIFSAQRGSRKNQGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQFTSKLGNFSELATHNQTFLKKLRNQITHTVSVFSERTETLKSACVDTEEADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNTNTGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIAGEEKRVYYVHEFDALRNIRNQVVQEICAEEACRDMKADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTLTGSALTFVSQYFSPDKGARPNVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKPEMVFYVENFDILQHIEDDLVLGICSPREECKRIEVLDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNTYTAEALAFSDHMFTEARGSRLHKGVPQVLIVITDGESHDAEKLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDKYYFVETFGGLKGIFSDVSASVCNSSKVDCEIEKVDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTHIGDALRKVKYYFQPDMGSRINAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEKKLTVHNFDELKKVKKRIVRNICTSGGESNCFVDVVVGFDISSLQRGQTLLEGQPWMGSYLQDLLRAISSLNGVSCEVGTETQVSIAFQVTNAMERYPSKFEIYSENILSSLQGVTVNGPSRLNANLLSSLWDTFQNKSAARGKVVLLFSDGLDDGIEKLEQKSDELRKEGLNALITIAVDGAADSSDLADLLYIEFGKGFEYRTQFTIGMRNLGSQLSRQLINVAERTCCCLLCKCTGGDGAMGDPGSAGKKGPPGFKGSDGYLGEEGIAGERGASGPMGEQGTKGCFGAKGPKGTRGLSGEEGEVGEDGLDGLDGEQGDHGIPGRRGEKGDEGSQGNPGRRGAAGDRGAKGLRGDPGTPGRDSSIQGPKGLKGDLGRQGRRGWPGSPGTPGSRRKMVVHGRRGHIGPQGNPGTPGPDGLAGSPGLRGPQGPRGEVGEKGEKGSLGMKGPQGPPGPGGQAGSQGHLGSQGNKGEPGDLGEKGAAGFPGPRGLQGDDGSPGYGSIGRKGTKGQEGFPGESGLKGDIGDPGDPGEAGPKGARGKTVSAGIPGEPGSPGEPGPPGRKGVKGARGLASFSTCDLIQYVRDHSPGRHGKPECPVHPTELVFVLDQSRDVTEQDFERMKGMMVSLVRDVKVREANCPVGARVAILAYNSHTRHLIRFSDAYRKDQLLTAIKALPYERSSDSREIGKAMRFISRNVFKRTLPGAHVRRIATFFSSGPSADAQTITTAAMEFSALDIVPVVIAFSNVPSVKRAFSIDDTGTFQVIVVPSGSDEGPALERLQRCTFCYDLCKPDASCDQAKPPPIQSYLDTAFLLDGSRHVGSAEFEDMRDFLEALLDHFEITSEPETSVTGDRVALLSHAPLDFLPNTQRSPVRTEFNLTSYSSKRLMKRHVDQAVQQLHGDAFLGHALGWALDNVFLNTPNLRRNKVIFVISAGETSHLDAETLKKESLRAKCHGYALFVFSLGPDWDDKELEDLASHPVDQHLIQLGRIHKPDHGYSVKFVKSFINSIRHGINKYPPVNLKAKCNRLGSRDLKPPPRQFRSFVPGPQKANLKDHTAEAAKLFQDKKRLSSMLKGGRATISSLSRSTRYAFKQGKEAIKATSKLGKRSA
Protein: Earmuff, isoform B (M9PBS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQPCSPAGEIAMMPPSKSPVMESAASEQNPAQQSQQQDEQSAKRACPLKFSIAKIMEPDHRPSQVPPPQPAPVSFATNDDDEDEDPEIDADSERSCSPIEVISLDQSPSTVNYDSAFKKYVPGPCSGATSSVASPPSTAAVQQFVSSRHQELLSQYPLLYYAPNQLMCAAAAAQYAALTAQQQSLASAAHLSSFTASLNASLHHSQSLRRNLGHPLAAAAAVAAVAQSQAVPNLQHTLEKSPVAQRTAQSSGLQANLKRKRSPQDQGEVTPPPASTATSATGARSRSPSPQGSIEDSSPGSASGGKPKTFSCLECGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTSEKPHKCQTCGKAFNRSSTLNTHSRIHAGYKPFVCEYCGKGFHQKGNYKNHKLTHSGEKAYKCNICNKAFHQVYNLTFHMHTHNDKKPYTCRVCAKGFCRNFDLKKHMRKLHEIGGDLDDLDMPPTYDRRREYTRREPLASGYGQASGQLTPDSSSGSMSPPINVTTPPLSSGETSNPAWPRSAVSQYPPGGFHHQLGVAPPHDYPSGSAFLQLQPQQPHPQSQQHHQQQQRLSETFIAKVF
Protein: Mitochondrial ribosome associated GTPase 2 (A2AFK4)
Organism: Mus musculus (Mouse)
Interaction partners:
- Mitochondrial ribosome-associated GTPase 1
- Mitochondrial assembly of ribosomal large subunit protein 1
- rRNA methyltransferase 2, mitochondrial
- Transcription termination factor 4, mitochondrial
- 5-cytosine rRNA methyltransferase NSUN4
- Putative GTP-binding protein 6
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL20m
- Nitric oxide-associated protein 1
- Translation initiation factor IF-2, mitochondrial
Sequence:
MVSTRLVLARTCTVFEGVLKWAPSTRAVLRPSHLLLQASCRLLSVGIVDHAKHREPSGKKVLSEKKLKRHFVDHRRVLVRGGSGGSGMSCFHSEPRKEFGGPDGGDGGNGGHIILRVDQQVKSLSSVLSQYQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVKEGDKIVADLSNLGDEYVAALGGAGGKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPEPWTQVDDLKYELEKFEEGLSERSHVIIANKIDLPQARARLPQLQARLGQEAIGLSALTGENLEQLLLHLKELHDAHIEAELEQGRQPLRW
Protein: Si:dkey-231l1.4 protein (A7E2G4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSLFTSVFRQLSACFTPSWGRRLSPQIADIGAEAGESKAMSTQKHRKVKSHHGHRPGKEGEGLKDQAEEEKQALSAENIQSTEREGGNGEPGGKKRKRRKLKNKKTLPLPVEVKPLPAPACFSSSPPVGDQPEHPDVLALPAAGLKPLLKDKESLPRLVEVKPLPASACFSSLTPVGDQPEHPEVLVLPASHLKALSPLSNPASRPQSPVEGTDEVLPSSVIQVAPCVSPEPVLLPLQSSSEVASLCSIPSFSEPSLLQSPPETLPIPPIFALTEVVSLVKPQASECSPSSGLMLFGFEDEELEFMEYTEEDIEAFYESEMKPRRMAAWLEQEEVTEVQKDGGKGASQVIQNPLNEVSRDEAFEELLIQAFCTGPPVYTEIKSRKKPKRNGPLVLFSLMEEKVKKKQEKKLRKEEERNERNLLRERYRNDPKLKHLCINKHNPNFCWS
Protein: Cinnamoyl-CoA reductase 1 (OsCCR1) (EC 1.2.1.44) (Q6K9A2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Probably involved in the formation of lignin in defense responses.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16380417}.
Interaction partners:
- tricin synthase
- 40S ribosomal protein S29, putative, expressed
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS9
- 4-coumarate--CoA ligase 4
- Os10g0411700 protein
- 4-coumarate--CoA ligase 1
- Hydroxycinnamoyltransferase 1
- 40S ribosomal protein S15, putative, expressed
- Small ribosomal subunit protein uS19
Sequence:
MSSNFEANNNNNGEKQLVCVTGAGGFIGSWVVKELLIRGYHVRGTARDPADSKNAHLLELEGADERLSLCRADVLDAASLRAAFSGCHGVFHVASPVSNDPDLVPVAVEGTRNVINAAADMGVRRVVFTSSYGAVHMNPNRSPDAVLDETCWSDYEFCKQTDNLYCCAKMMAEMTATEEAAKRGLELAVVVPSMTMGPMLQQTLNFSTNHVARYLMGTKKSYPNAVAAYVDVRDVARAHVLVYERPEARGRYLCIGTVLHRAELLRMLRELFPRYPATAKCEDDGKPMAKPYKFSNQRLKDLGLEFTPLRKSLNEAVLCMQQKGHLPLIYPVPKRAYL
Protein: Cystatin-like cysteine protease inhibitor EPIC2B (Extracellular protease inhibitor with cystatin-like domain protein 2B) (Secreted effector EPIC2B) (D0NBV3)
Organism: Phytophthora infestans (strain T30-4) (Potato late blight agent)
Function: Secreted effector that interacts with and inhibits the pathogenesis-related papain-like cysteine proteases C14, PIP1 and RCR3 of host plants. Inhibition of host proteases by a pathogen extracellular protease inhibitor forms a specific type of defense-counterdefense mechanism between plants and microbial pathogens.
Subcellular location: Secreted {ECO:0000269|PubMed:17085509, ECO:0000269|PubMed:19171904, ECO:0000269|PubMed:20940351}. Note=Localizes to host apoplast where it targets defense proteases for inhibition. {ECO:0000269|PubMed:17085509, ECO:0000269|PubMed:19171904, ECO:0000269|PubMed:20940351}.
Interaction partners:
- Cysteine protease family
- Extracellular protease inhibitor 1
- Extracellular protease inhibitor 10
- RxLR effector protein Avrblb2
Sequence:
MSFLRPTLALLAVTALVTTSAQLNGYSKKEVTPEDTELLQKAQSNVSAYNSDVTSRICYLKVDSLETQVVSGENYKFHVSGCSVNSDKELGGCANQNCESSKYDIVIYSQSWTNTLKVTSITPAN
Protein: Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) (Q90473)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side {ECO:0000250|UniProtKB:P11142}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P11142}.
Interaction partners:
- Heat shock protein HSP 90-alpha 1
- BCL2-associated athanogene 3.
- DnaJ heat shock protein family
- Heat shock protein b8
- DnaJ heat shock protein family
- Heat shock protein HSP 90-beta
- DnaJ heat shock protein family
- DnaJ homolog subfamily A member 2
- Heat shock protein beta-1
- J domain-containing protein.
Sequence:
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVLDANRLNGRQFDDGVVQSDMKHWPFNVINDNSRPKVQVEYKGESKSFYPEEISSMVLTKMKEIAEAYLGKTVSNAVITVPAYSNDSQRQATKDAGTISGLNVLVIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGSFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFITEFKRKHKKDISDNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDYFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGIMNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDDVQRDKVSAKNGLESYAFNMKSTVEDEKLKGKISDEDKQKILDKCNEVIGWLDKNQTAEREEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPEGMPGGFPGAGAAPGGGSSGPTIEEVD
Protein: Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)] (Q3ZCJ8)
Organism: Bos taurus (Bovine)
Function: Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P53634}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Legumain
- Cystatin-A
- Cathepsin D
- Ia antigen-associated invariant chain
- Peptidase S1 domain-containing protein
Sequence:
MGPWSGSRLVALLLLVYGAGSVRGDTPANCTYPDLLGTWVFQVGSSGSQRDVNCSVMGPPEKKVVVHLKKLDTAYDDFGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGGKVTSYCHETMTGWVHDVLGRNRACFTGRKTGNTSENVNVNTARLAGLEETYSNRLYRYNHDFVKAINAIQKSWTAAPYMEYETLTLKEMIRRGGGHSRRIPRPKPAPITAEIQKKILHLPTSWDWRNVHGINFVTPVRNQGSCGSCYSFASMGMMEARIRILTNNTQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEDCFPYTGTDSPCRLKEGCFRYYSSEYHYVGGFYGGCNEALMKLELVHQGPMAVAFEVYDDFLHYRKGVYHHTGLRDPFNPFELTNHAVLLVGYGTDAASGLDYWIVKNSWGTSWGENGYFRIRRGTDECAIESIALAATPIPKL
Protein: Autophagy-related protein 9 (Q54NA3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). Required for lipopolysaccharide (LPS)-enhanced bacterial clearance through the autophagic pathway.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:20070309}; Multi-pass membrane protein {ECO:0000269|PubMed:20070309}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20070309}; Multi-pass membrane protein {ECO:0000269|PubMed:20070309}.
Interaction partners:
- Autophagy-related protein 18
- Serine/threonine-protein kinase atg1
- Probable serine/threonine-protein kinase vps15
- Ubiquitin-like protein atg12
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy protein 5
- Autophagy-related protein 3
- Autophagy-related protein 8
- Probable serine/threonine-protein kinase DDB_G0291918
- Probable autophagy-related protein 17
Sequence:
MSHEDRGGDYYPMMDDPEDRNFIQAKYPNSTGHMSSGGGSNHMSFDDNHGIEMLRDDEHSLLHESPVSIPAIHNLDSFLTDVYNYFRGKGFMCIFFNDLFELVSSLFVVLFFTFLVCFVDYSKLFSEQMPPPALRESVNFSAPIPIWLMVFLVIFSLYWLSKLFSFFSSIKTNWEISSFYKNTLKINEDDIQTIEWREVVSKIVLVPRLCIVKENMNALDIANRIMRKENYIIGLINQRILNLSIPFPFLRNLTFITKTLEWSLMYSLFNYIFDENGIIKSEFQDPTQRKRLSRGLSRRFMTIGILGLFTTPFIFFFLLINFFFEYAEELKNRPGSLFSREWSPLARWEFRELNELPHYFQNRLNLSYSHANQYVESFPSQMLSTIAKFISFLFGSVLAVFIVLGIVSDHFIMNYQIFDRTPIWYIGILGTIVAITRSLIVDENQVFQPAKHMARTVQNTHYLPMSWVGKTHTHKVRDEFLVLFEYRIVDFVRDIFSVLFTPFILIFSLPKSSQAIIDFFGNNTVVLEGVGPICQLGDFSNIRKLGDNSFGSLNHSQNKISLTNNAKLEKSIINFKCLNPEWNTDNNELLQNLNEFSKIKNNNNNNNNNGSNNHIGNHSQLPTTSVDDFQFIHDSHYIPHEIIDAVLGTHHHSQQSNNNAPRFKTGRVDQNILNAVNDLHQSFYESQYKHKNDNFVNSI
Protein: Oligogalacturonate specific porin (E0SBW0)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- LPS-assembly lipoprotein LptE
Sequence:
MKFKILTMMVASVVSMSSMAVTFDYRHEMKDTQNANHQDRLLISHRFENGFGLSSEVKWKQSSNDNTPNKPYNEQVSNGTEVTASYLYKFDKMFNVEAGFNLVTDSSTNSYRPYIRGGVNFTDSLYYTLRYRPFYKRYSGSINTTPPAEATNMKGYTITSVLGYKFLDNFTVEYELEYNKNTKAGNFGYIYDNDNDNLTHDVKLAYKIDKNWTPYIQVANVEGPSKTTDERQTRYRVGVQYNF
Protein: phosphatidate phosphatase (EC 3.1.3.4) (A8DY69)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNIDEGDAPISSATNNNNTSSSNDEQLSAPLVTARTGDDSPLSEIPHTPTSNPRLDLDIHFFSDTEITTPVGGGGAGSGRAAGGRPSTPIQSDSELETTMRDNRHVVTEESTASWKWGELPTPEQAKNEAMSAAQVQQSEHQSMLSNMFSFMKRANRLRKEKGVGEVGDIYLSDLDAGSMDPEMAALYFPSPLSKAASPPEEDGESGNGTSLPHSPSSLEEGQKSIDSDFDETKQQRDNNRYLDFVAMSMCGMSEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQLMSQTVDGKCLPGDEKQEAVAQADNGGQTKRYWWSWRRSQDAAPNHLNNTHGMPLGKDEKDGDQAAVATQTSRPTSPDITDPTLSKSDSLVNAENTSALVDNLEELTMASNKSDEPKERYKKSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSYCSMTYIVDQLFPPVKLDEASAEFSNFNYWRDPIPDLEIPELETALVPPSTKVDMATLRPIPEK
Protein: THAP domain-containing protein 1 (Q9NVV9)
Organism: Homo sapiens (Human)
Function: DNA-binding transcription regulator that regulates endothelial cell proliferation and G1/S cell-cycle progression. Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA sequence and acts by modulating expression of pRB-E2F cell-cycle target genes, including RRM1. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. May also have pro-apoptotic activity by potentiating both serum-withdrawal and TNF-induced apoptosis.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:12717420}. Nucleus, PML body {ECO:0000269|PubMed:12717420}.
Interaction partners:
- Torsin-1A
- PRKC apoptosis WT1 regulator protein
- THAP domain-containing protein 11
- 52 kDa repressor of the inhibitor of the protein kinase
- THAP domain-containing protein 7
- Zinc finger CCHC domain-containing protein 10
- Epsilon-sarcoglycan
- Ribonucleoside-diphosphate reductase large subunit
- Guanine nucleotide-binding protein G
- Anoctamin-3
Sequence:
MVQSCSAYGCKNRYDKDKPVSFHKFPLTRPSLCKEWEAAVRRKNFKPTKYSSICSEHFTPDCFKRECNNKLLKENAVPTIFLCTEPHDKKEDLLEPQEQLPPPPLPPPVSQVDAAIGLLMPPLQTPVNLSVFCDHNYTVEDTMHQRKRIHQLEQQVEKLRKKLKTAQQRCRRQERQLEKLKEVVHFQKEKDDVSERGYVILPNDYFEIVEVPA
Protein: C-C chemokine receptor type 3 (C-C CKR-3) (CC-CKR-3) (CCR-3) (CCR3) (CKR3) (CD antigen CD193) (O54814)
Organism: Rattus norvegicus (Rat)
Function: Receptor for C-C type chemokine. Binds and responds to a variety of chemokines, including CCL11, CCL26, CCL7, CCL13, RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing the intracellular calcium ions level. In addition acts as a possible functional receptor for NARS1.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- C-C motif chemokine ligand 24
- Eotaxin
- C-C motif chemokine 5
- C-C motif chemokine ligand 26
- C-C motif chemokine 2
- C-C motif chemokine 3
- C-C motif chemokine 4
- C-C motif chemokine 7
- C-X-C motif chemokine 10
- C-C chemokine receptor type 5
Sequence:
MASNEEELKTVVETFETTPYEYEWAPPCEKVSIRELGSWLLPPLYSLVFIVGLLGNMMVVLILIKYRKLQIMTNIYLLNLAISDLLFLFTVPFWIHYVLWNEWGFGHCMCKMLSGLYYLALYSEIFFIILLTIDRYLAIVHAVLALRARTVTFATITSIITWGFAVLAALPEFIFHESQDNFGDLSCSPRYPEGEEDSWKRFHALRMNIFGLALPLLIMVICYSGIIKTLLRCPNKKKHKAIQLIFVVMIVFFIFWTPYNLVLLLSAFHSTFLETSCQQSIHLDLAMQVTEVITHTHCCINPIIYAFVGERFRKHLRLFFHRNVAIYLRKYISFLPGEKLERTSSVSPSTGEQEISVVF
Protein: Transcription initiation factor TFIID subunit 11 (TFIID subunit p30-beta) (Transcription initiation factor TFIID 28 kDa subunit) (TAF(II)28) (TAFII-28) (TAFII28) (Q15544)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF11, together with TAF13 and TBP, play key roles during promoter binding by the TFIID and TFIIA transcription factor complexes.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 4B
- Transcription initiation factor TFIID subunit 1
Sequence:
MDDAHESPSDKGGETGESDETAAVPGDPGATDTDGIPEETDGDADVDLKEAAAEEGELESQDVSDLTTVEREDSSLLNPAAKKLKIDTKEKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKGQIPNSKHKKIIFF
Protein: Cation transporter, putative (Q38F06)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- GP-PDE domain-containing protein
Sequence:
MSGSLNVEQGPREASPGSATLLDSPAATGMSTRHAEQVVQSIKVLYELHKSGALSLEEFNAAKQQILFPPHSLLSVSGRSSEVGHAEYVRSRHIKKRENRGSKRGSSHWSSTSSSSSSISTVSNFMVAPRPRVWLPLVDEGSGDGVNHDAVMKEELDEGFLSGPVDKAGYYSLRSRTLSQDRGRPCAPPSSNGHGSNLKRYGTFRSPWPVVIGDTSIPKESVRAPMLPVNQVFVEYFNCRGERGQTFSSVELKEHQLRPPLFLHKRFATGQRERVPEALSTLAHTQELVPSESAVLHEEYPAAEPPDAPSVSGNSSLELCLNWYWVDMVGRDPSEVMYKNALRHLTKQFDIAESFLLDREHPLVLPQICSSPEDPSQFLICLRVATAKIALDDDSVKELTNRWILVVDLKRKVVITIHRMDSSYIANMRYHWKSLMERSDISFEEFLVRIMHDAVCTYTSHLIAHSDILEKCEAKLFVSSRRGTNNVPGTEYSASKQHAEGRIFSLFVDGSSSPFLLKLMDTKNKEPMDKGLMNIFLYHLHRRASVHHRVLNMTRVVLSESFTKLGLCSKEYADEMCVHCIELIDRALEICDDAKTLLDMHISLQSFRTNELMALLTKFSAFFTPSSFLAAVYGMNFPHIPELQWAWGYPCYWLACIVACVLIYLYMYRRGLLE