wanglab/gogpt-training-data huggingface dataset:
Protein: Forked, isoform F (Q0KHR2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, stereocilium {ECO:0000256|ARBA:ARBA00004645}.
Interaction partners:
- Neither inactivation nor afterpotential protein C
- Endonuclease III homolog lyase)
- N-glycosylase/DNA lyase
- Protein singed
Sequence:
MASCAPVIVWNGAQFTASSRELEQLRRDYGLDARMLEATLVPRYKRHKPQAAARNDHVRVTKEQQSDWILKQDRSTNVSQVNFHPWAGAHFDLVPWRRTRSALDLTAVEDYNHGLVDPKSLKGLEKLELRQQRRRLQRARSTHQGLRRLVRVRLIFSIELRHKRMEVLRKSSLPVRVFEQRFALSENESAAYERILLDANAGVDQHVGYFSKRQVVTSNRESNEELVVDFASETEADEKADEQPEKEEAQYATIAPAEKGGSAAVPDKESGQVPCVKCRDIAIKLRTINDYALNSNLHLSHNTKLNNLHSNKLLHSNQSHSSSINPSTRMHSHQLDSYLGGVGSMMNLGGMGQVGQMYHPGSVSGSERPNGGALALHYAAARGCLDCVQLLVAASVDICYFSTINVKKGLLGRMTTSLTSYRRSKQKSKSNNDIHTIIATEVVTAAILSSSVHSSSTGSEIGDGGQGNTSLIEEAAAQDQSSEEQDRQHQHAKDPLAQTEMNHHPHSHHQRKSAVEVVRQQMDDDGDQDSNDDDETMPMMSGVGRKEQNNRRSVVSANTQMDNDVTPVYLAAQEGHLEVLKFLVLEAGGSLYVRARDGMAPIHAASQMGCLDCLKWMVQDQGVDPNLRDGDGATPLHFAASRGHLSVVRWLLNHGAKLSLDKYGKSPINDAAENQQVECLNVLVQHGTSVDYNGKSSSQRHKSQQQLHQQHQQQQQQQQQQHLSSSCNSNSNSSKQTSRSNTIKSKSSSTLSSDVEPFYLHPPALAGGSGGSGMGLGMGMGMGMGMSMGLGISRKNSDALYSQQSRSSSEKLYNGSSSLGGNPGGNSSSGGGGVGGGGGSGGALLPNDGLYVNPMRNGGMYNTPSPNGSISGESFFLHDPQDIIYNRVRDLFVDSDCSSSVKQHGKSHAHQLLQSKAGNAMTIQADVHSSSSGAGSGSDESVSISSSFNSPKQQQQLRSQSFNRHGSSSNISASGNIKNNNYKAHKGKPSNQNGGGDHDYEDIYLVREESRKQHQQQQQHQLQQQQQLQHQATQQQQQQQQQQQQLQHKYNVGRSRSRDSGSHSRSASASSTRSTDIVLQYSNHHLNNKRNMNNNSNMNNSSSNIAQSSSSNNNNNSLLNRNKSHSIIGLHSSKYESSLKDNYSAKNVNLKNQLLNGGIKSDTYESVCPPEDVAERTKQTHKNSMIRNNLADASSNNNTSGSINNISNIGNMNGGNQSSRNLKRVSSAPPMQNLAVVNGPPPPPLPPPLRAPVQQQRNNLSVDQPNSMTGNNGIYKKNVFGPNQGPTNANGTGGAAPPPVPAPNPVATEAVDSDSGLEVVEEPSLRPSELVRGNHNRTMSTISANKKAKLLNAGSTNGSSIAASSDDSQSRYGGSVHAANGSAANGHFYGYSEGNKNQGSNGNGNGNGNGGGGNYHSHPNQPHYATGQPHQYTPSLYGGGSSAEDHYELTQQQQQIYGETHLPSGQRTGGPNLVNKQLVLPFVPPSFPNKSQDGVTHLIKPSEYLKSISIDKRSCPSSARSTDTEDYMQIQIAQQQSHPHQHQHHPHPHPHPHHPHQLHGMGEQPPLPPPPPPLPHGMLPPQPPMGPPMGVAGGQDATMSGKSHKPKKPHGSAPNSQDTATRKQHQPLSAISIQDLNSVQLRRTDTQKVPKPYQMPARSLSMQCLTSSTETYLKSDLIAELKISKDIPGIKKMKVEQQMASRMDSEHYMEITKQFSGNNYVDQIPERDQAGNAIPDWKRQMMAKKAAERAKKDFEERMAQEAESRRLSQIPQWKRDLLARREETENKLKAAIYTPKVEENNRVADTWRLKNRAMSIDNININLAGMEQHYQQIQFQQKQQQLQLGNKENHVDPKGADQDQEHGVGIGSGVGNANSGVIGGQELIDPSEGSQGRAEEEEDNIIPWRAQLRKTNSRLSLI
Protein: Pentatricopeptide repeat-containing protein At5g11310, mitochondrial (Q9LFM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MNSLFTAFRRNLLLNPNPHRNFFLHRLLSSSRRSSPLIPVEPLIQRIQSPAVPDSTCTPPQQNTVSKTDLSTISNLLENTDVVPGSSLESALDETGIEPSVELVHALFDRLSSSPMLLHSVFKWAEMKPGFTLSPSLFDSVVNSLCKAREFEIAWSLVFDRVRSDEGSNLVSADTFIVLIRRYARAGMVQQAIRAFEFARSYEPVCKSATELRLLEVLLDALCKEGHVREASMYLERIGGTMDSNWVPSVRIFNILLNGWFRSRKLKQAEKLWEEMKAMNVKPTVVTYGTLIEGYCRMRRVQIAMEVLEEMKMAEMEINFMVFNPIIDGLGEAGRLSEALGMMERFFVCESGPTIVTYNSLVKNFCKAGDLPGASKILKMMMTRGVDPTTTTYNHFFKYFSKHNKTEEGMNLYFKLIEAGHSPDRLTYHLILKMLCEDGKLSLAMQVNKEMKNRGIDPDLLTTTMLIHLLCRLEMLEEAFEEFDNAVRRGIIPQYITFKMIDNGLRSKGMSDMAKRLSSLMSSLPHSKKLPNTYREAVDAPPDKDRRKSILHRAEAMSDVLKGCRNPRKLVKMRGSHKKAVGEDINLIDDINERNGDAGDFE
Protein: DNA repair RAD52-like protein 2, chloroplastic (Organellar DNA-binding protein 2) (Q9FIJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in double-stranded DNA break repair.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:22202891, ECO:0000269|PubMed:22762281}. Note=Distributed in a punctate pattern within chloroplast. {ECO:0000269|PubMed:22202891}.
Interaction partners:
- DNA repair protein XRCC2 homolog
Sequence:
MALQVQQTSAAFTISSPSTAAARIKLSPFRTVAVNRGVRCSGGGVGGGDAGKKKAVPNSNYVVPIDKFSSSSSITRPLIEILRDLNKKIPDNIVKSHDPPSTSAATSGFIPWYHANRMLSFYAPGWCGEVRDVIFSENGNVTVVYRLTIRGSDGEAHRESTGTVTTTDDHIEDPVTAAEEIAFCRACARFGLGLYLYHE
Protein: Vascular endothelial growth factor A (VEGF-A) (Vascular permeability factor) (VPF) (P15691)
Organism: Bos taurus (Bovine)
Function: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin (By similarity). Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Also binds the DEAR/FBXW7-AS1 receptor (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin. {ECO:0000250}.
Interaction partners:
- receptor protein-tyrosine kinase
- Adhesion G protein-coupled receptor L2
- Vascular endothelial growth factor receptor 2
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
- Insulin-like growth factor 1
- Neuropilin
- Interleukin-6
- Interleukin-8
- Hypoxia-inducible factor 1-alpha
Sequence:
MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGQKPHEVVKFMDVYQRSFCRPIETLVDIFQEYPDEIEFIFKPSCVPLMRCGGCCNDESLECVPTEEFNITMQIMRIKPHQSQHIGEMSFLQHNKCECRPKKDKARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR
Protein: Putative membrane protein YdgH (P96706)
Organism: Bacillus subtilis (strain 168)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator YdgG
- Probable multidrug resistance protein YoeA
- Transcriptional regulatory protein YdfI
- Uncharacterized transporter YisQ
- Multidrug resistance protein EbrA
- Multidrug resistance protein EbrB
- Probable guanidinium efflux system subunit GdnD
Sequence:
MRAIIKFKWAIAAIVLALTVVLSLFSPNLTELANQKGQAQLPADAVSERANAILKQAGEDNNSISVVFTLDNAIKKETENQLRIIIDKIKKIDGVEEVTSPLSAEKEVKDQLMSKDKKTVLMPVTITGSDKKAEKIADEIYQIVPDDLTAYITGASLINQDFAHSSEEGLKKTEVITVCLIIGLLLIVFRSVVTPFIPIVVVGFSYLISQSILGILVYNVDFPISTFTQTFLVAILFGIGTDYCILLLTRFREELANGHDKKEAALIAYRTGGKTLFISGFAVLIGFSALGFAKFAIFQSAVGVAVGVGILMIILYTLLPLFMVTLGEKLFWPSKKVLSHSDNKLWAFLGRHSVARPFLFIVITVVITLPFILTYDDQISFDSTAEISSDYKSIKALEAIKDGFGEGKAFPINVVVKGDKDLTTADTIPYLGNISKAIEKVDHVDSVMTITQPTGKKIKDLYIDNQLGSVSDGLDKTVKGIADVQSGLTDIENGLNQMAGQTGSASNGGSGGSLGDAADGLGKINQQLQLVSKQISQTGNTAQTVQQLTAISGQLGQIQTGLEQANQQLSGQQAQAGTLTESLKKLSEGVKSANEGLTKVSDGITASSDILEDMSKSPTVRDTGIFIPDQVMKDKDFKKSIDQYSFADGKGVQLSVVLDSNPYSEQAITTINQIKKAVANEVDGTPLENAQIVYGGVTSMNADLKELSTTDFSRTMVIMIIGLFIVLTILFRSMIMPIYMIASLLLTYYTSISITELIFVNGLGNAGVSWAVPFFSFVILIALGVDYSIFLLDRFKEEVHLGIEQGVVRSMSKMGSVIITAAIILAGTFAAMMPSGVNTLMQVASVIIIGLLLYGLVILPLFIPAIIATFGEGNWWPFGRKKGKE
Protein: Protein phosphatase 1 regulatory subunit 27 (Dysferlin-interacting protein 1) (Toonin) (Q86WC6)
Organism: Homo sapiens (Human)
Function: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes.
Interaction partners:
Sequence:
MPSRTARYARYSPRQRRRRMLADRSVRFPNDVLFLDHIRQGDLEQVGRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLPSDLIDPDYKELVELFKGTTMD
Protein: Mechanosensitive channel MscK (Potassium efflux system KefA) (P77338)
Organism: Escherichia coli (strain K12)
Function: Mechanosensitive channel that opens in response to membrane tension and specific ionic conditions. Requires high concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate. May participate in the regulation of osmotic pressure changes within the cell, although it does not appear to have a major role in osmolarity regulation. Forms an ion channel of 1.0 nanosiemens conductance. The channel can remain active for between 30 seconds and over 3 minutes; it does not desensitize upon extended pressure. Its activity is masked in wild-type cells by the MscS channel.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:11985727, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:11985727, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Mechanosensing system component YbdG
- Large-conductance mechanosensitive channel
Sequence:
MTMFQYYKRSRHFVFSAFIAFVFVLLCQNTAFARASSNGDLPTKADLQAQLDSLNKQKDLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPLVKQELEINQQLSQRLITATENGNQLMQQNIKVKNWLERALQSERNIKEQIAVLKGSLLLSRILYQQQQTLPSADELENMTNRIADLRLEQFEVNQQRDALFQSDAFVNKLEEGHTNEVNSEVHDALLQVVDMRRELLDQLNKQLGNQLMMAINLQINQQQLMSVSKNLKSILTQQIFWVNSNRPMDWDWIKAFPQSLKDEFKSMKITVNWQKAWPAVFIAFLAGLPLLLIAGLIHWRLGWLKAYQQKLASAVGSLRNDSQLNTPKAILIDLIRALPVCLIILAVGLILLTMQLNISELLWSFSKKLAIFWLVFGLCWKVLEKNGVAVRHFGMPEQQTSHWRRQIVRISLALLPIHFWSVVAELSPLHLMDDVLGQAMIFFNLLLIAFLVWPMCRESWRDKESHTMRLVTITVLSIIPIALMVLTATGYFYTTLRLAGRWIETVYLVIIWNLLYQTVLRGLSVAARRIAWRRALARRQNLVKEGAEGAEPPEEPTIALEQVNQQTLRITMLLMFALFGVMFWAIWSDLITVFSYLDSITLWHYNGTEAGAAVVKNVTMGSLLFAIIASMVAWALIRNLPGLLEVLVLSRLNMRQGASYAITTILNYIIIAVGAMTVFGSLGVSWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRIRATTITDFDRKEVIIPNKAFVTERLINWSLTDTTTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVMHEPMPEVFFTAFGASTLDHELRLYVRELRDRSRTVDELNRTIDQLCRENDINIAFNQLEVHLHNEKGDEVTEVKRDYKGDDPTPAVG
Protein: Krt78 protein (A1L0X5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSLSPCRAQRGFSAHSACSAFSGARGRTGFSSRSLSSSRRCRGSSCGRAWGAETRQGIRFGQGKGGPGFSQCPPGGIQAVTVDQSLLTPLKIEVDPQFQVVKTQETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQGNRSPQGLECIFETCLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLYEEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEECRISTEHTSQVTVSITEGSIVPGRTCGGQVVVPGRIGTGQVVMPGRECGGHVVMPGRGSGGQVTIPGRGSGGHVTVP
Protein: Aurora kinase A- and ninein-interacting protein (AIBp) (Q9H7T9)
Organism: Homo sapiens (Human)
Function: DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination. Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing homologous recombination repair. Inhibits non-homologous end joining (NHEJ). Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:29042561}. Chromosome {ECO:0000269|PubMed:29042561}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20596670}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20596670}. Note=Accumulates at sites of DNA damage by binding to DNA substrates that mimick structures generated at stalled replication forks (PubMed:29042561). Localizes to the centrosome in interphase and to the spindle pole in metaphase (PubMed:20596670). {ECO:0000269|PubMed:20596670, ECO:0000269|PubMed:29042561}.
Interaction partners:
- Aurora kinase A
- Denticleless protein homolog
Sequence:
MRRTGPEEEACGVWLDAAALKRRKVQTHLIKPGTKMLTLLPGERKANIYFTQRRAPSTGIHQRSIASFFTLQPGKTNGSDQKSVSSHTESQINKESKKNATQLDHLIPGLAHDCMASPLATSTTADIQEAGLSPQSLQTSGHHRMKTPFSTELSLLQPDTPDCAGDSHTPLAFSFTEDLESSCLLDRKEEKGDSARKWEWLHESKKNYQSMEKHTKLPGDKCCQPLGKTKLERKVSAKENRQAPVLLQTYRESWNGENIESVKQSRSPVSVFSWDNEKNDKDSWSQLFTEDSQGQRVIAHNTRAPFQDVTNNWNWDLGPFPNSPWAQCQEDGPTQNLKPDLLFTQDSEGNQVIRHQF
Protein: Condensin subunit 1, putative (Q38F58)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Condensin complex subunit 2
- Structural maintenance of chromosomes protein
- Nuclear condensin complex subunit 3 C-terminal domain-containing protein
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- DNA polymerase
Sequence:
MSDLLEFFVPAYARDLENIEKVGVTQYHISEPCDFDVPPRQQLDDLTRLFDSLHREKSPTALFSKPELFAALFTYIKAMEDKETSFAVTRGARHKICHESAERLKKLLQICVTYLRRNAENGFRDSLLLCLRSNIKMYVFVLCNTLLSTAPGIDDDEGMSPSFQRTGRKRKRNKGNQEAGIGEDDSGVDQDGREQALSALIDIFSQDILQLWTGELIEESMLTLMLRMLLHMITQKCNIHADVQSVSGALVVLLSKISAQMMARGSIEPNDFVSPMIELVLKSEVTALFFTRFVAETENEGASANHAGRVVTALIEGVAGVALYDVVGDPSAAKNVALFFSEVARRCVSVTSRMSDIVMQTINSESYEVRKSIITCVTEMVIQRYSGPNCNGEGEEEIRDGYLSELLCRLMDCNPYVRNHVVHMWEKLLEARAVPKRFRLPLTGAIVGRLEDRNYLVRDSALQVVVSILNKSWFGSVLSPSLLEEKIREATAAAEVLFESVEMYVRCLEGVRKSSTFTEPQASGLAEEATGDVPVPIEMSSEQESAIDRVISFEASMEFAKLIAKSLTHATSLLDSRTERDAIEAIKLVVACNRHRIDEAEKAFLHVLVMVYEGEIKIQYAVRDALVDVVFNAFSRSTTSLAVQNTASAHKLISFLRGAKEGDISAVDRVFALIRTNPPHWRLISGHFIDALWGIAGGALDGGATLVERRIAMRLFSIVCKHDWHALVSRKESVVEFLKSGTMKDNVVLAYCLKSLEVEGQDPHYQPISSKFAPGEHVILEQLVFHLCRTTTTLSSWLIVADAAISAVHRLCEVPAVVYIYVLEYLAQRVDADVNTQAQLFFVLGRTALKQLVAVDCLERQHLKRVDVEAMAKKPATEQSVVGDADAMHKELGLGSHEYRRHAIQELAQRRKQAIMSEGSIWHRLSKDVVDVCRKKASRSVGNPLERVCAVMTMSELMIVSDQFCEQHLDLLFTIVSDKRESWVVKTNAVIALGDLACVHPNLLSPYLKVPTTGFFKLLNDADVRVRAVTIQVCSHLVLGEMLRIRDHLYIIVRLVADPNETIASNAVTFVQNLALKEKERTGNLIPPLVVQLSHVVPADKFQLAMRSLLERVEGDKPTESLIERLCQRFEPYSERGTKKRQIARNLAFCLHELTYATERTIKRITSEVCYQQYKQWLRDDVVLDYFKDIAAKAKKVGLRIGTERRDKAAIEEWEARMQADCCGLDDPRGSRQLTGDESREAGDQNERDNWDTTADGL
Protein: Protein REDUCED WALL ACETYLATION 4 (EC 2.3.1.-) (Q9FXG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable O-acetyltransferase involved in the acetylation of xylan during secondary wall biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21673009}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Xyloglucan O-acetyltransferase 1
- xyloglucan O-acetyltransferase 2
- Pectin acetylesterase 8
- ATP-citrate synthase alpha chain protein 1
- Protein PMR5
- Pectin acetylesterase 9
- Protein trichome birefringence-like 31
Sequence:
MVVSQPITPGQVSFLLGVIPLMIAWLYSEFLEYRRSSFHAKVHSDKNLVELEMVTNKEDEGTVLMEGGLPRSASSKFYSSPIKTNLIRFLTLEDSFLLENRATLRAMAEFGAILLYFYICDRTSLIGQSQKNYSRDLFLFLFCLLIIVSAMTSLKKHTDKSPITGKSILYLNRHQTEEWKGWMQVLFLMYHYFAAVEFYNAIRVFIAGYVWMTGFGNFSYYYIRKDFSLARFTQMMWRLNFFVAFCCIILNNDYMLYYICPMHTLFTLMVYGALGIYSQYNEIASVMALKIASCFLVVILMWEIPGVFEIFWSPLAFLLGYTDPAKPDLPRLHEWHFRSGLDRYIWIIGMIYAYFHPTVERWMEKLEECDAKRRMSIKTSIIGISSFAGYLWYEYIYKLDKVTYNKYHPYTSWIPITVYICLRNCTQQLRRFSLTLFAWLGKITLETYISQFHIWLRSSVPNGQPKLLLSIIPEYPMLNFMLTTAIYVLVSVRLFELTNTLKSVFIPTKDDKRLLHNVIAMAAISFCLYIIGLILLLIPH
Protein: ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Caseinolytic protease) (Endopeptidase Clp) (Stress protein G7) (P80244)
Organism: Bacillus subtilis (strain 168)
Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades proteins tagged by trans-translation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
Interaction partners:
- ATP-dependent Clp protease ATP-binding subunit ClpX
- ATP-dependent Clp protease ATP-binding subunit ClpE
- Negative regulator of genetic competence ClpC/MecB
- Adapter protein MecA 1
- ATP-dependent protease ATPase subunit ClpY
- Chaperone protein DnaK
- Heat-inducible transcription repressor HrcA
- Chaperonin GroEL
- ATP-dependent protease subunit ClpQ
- Protein-arginine kinase
Sequence:
MNLIPTVIEQTNRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDRDNFKSAEEALEYGLIDKILTHTEDKK
Protein: E3 SUMO-protein ligase K-bZIP (EC 2.3.2.-) (E3 SUMO-protein transferase K-bZIP) (Q2HR82)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Plays a role in viral gene regulation and seems to be essential for KSHV reactivation. Disrupts host G1 cell cycle control thus allowing viral transcription and translation to proceed at the early stages of infection. Catalyzes its own SUMO modification as well as that of its interacting partners such as host TP53 and RB1.
Interaction partners:
Sequence:
MPRMKDIPTKSSPGTDNSEKDEAVIEEDLSLNGQPFFTDNTDGGENEVSWTSSLLSTYVGCQPPAIPVCETVIDLTAPSQSGAPGDEHLPCSLNAETKFHIPDPSWTLSHTPPRGPHISQQLPTRRSKRRLHRKFEEERLCTKAKQGAGRPVPASVVKVGNITPHYGEELTRGDAVPAAPITPPYPRVQRPAQPTHVLFSPVFVSLKAEVCDQSHSPTRKQGRYGRVSSKAYTRQLQQALEEKDAQLCFLAARLEAHKEQIIFLRDMLMRMCQQPASPTDAPLPPC
Protein: Virulence-associated membrane protein 2 (VMP2) (A0A0D1CVX2)
Organism: Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)
Function: During infection, may play a role in establishing and maintaining biotrophy; the formation of a tight interaction zone between the host and the pathogen.
Subcellular location: Membrane {ECO:0000269|PubMed:34093627}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAGKRRVASLVLLMIIWWSIVSAAESQCEERNDYSRKRPSHKPFTSHQNKQDRSCSSPLPSESCSTSAITPSDSAVRDTSLSRRGLPGMPGDIEWMGFYGSLLAVPTMLSILGIITNYNLGKSYYNSELNAQYYKQSREMLRAHTAKLIQDQEKKFANAGVSWNGMVYGKDGQVNPGAKLPEWNGRVLGGTVANPKSQPVPGSGGAVQGAAAGVGGGTTAGVAAGAGAASAGTGPAQVGGATAGGAGAEAQTGTGAIATGTGTGGAGDAGGSAPVSSGAEQGDAEAGDEARGSEERGDDGTEDRRGGQSEGDDDSDSDGNDEGDAGDAGDAGDA
Protein: Mitoguardin 1 (A0A2R8YGK2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MSEETIKFSPVAKKLFVVTAVSAISVIFLAHHFKRKRGKKKGKILPWEPEHLILEYTKRAASDKGSSCSSSRQNLTLSLSSTKDKGSQVCNYANGGLFSKYSGSAQSLASVQSVNSCHSCACGNSNSWDKADEDDIKLVNIPVTTPENLYLMGMELFEEALRRWEQALTFRNRQAEDEACGSIKLGAGDAIAEENVDDIISTEFIHKLEALLQRAYRLQEEFEATLGASDPNSLADDIDKDTDITMKGNVEDFGLRDTLSIASTDSFASAAELAEHREVRHTYSLESLCHCPFYEEAMHLVEEGKIYSRVLRTEMLECLGDSDFLAKLHCIRQAFQVILSESANRIFLAESGRKILSALIVKARKNPKKFEDVFDEMIYFLEQTDHWGSTEMELAARGVKNLNFYDVVLDFILMDSFEDLENPPTSIQNVVNNRWLNSSFKETAVASSCWSVLKQKRQQMKIPDGFFAHFYAICEHISPVLAWGFLGPRNSLYDLCCFFKNQVLLFLKDIFDFEKVRYSSTETLAEDLMQLLIRRTELLMAYLEADALRHTSSCLSSHGHVMSTGLLEAKVQ
Protein: Free fatty acid receptor 1 (G-protein coupled receptor 40) (Q8K3T4)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose-stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation. Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. Mediates the anti-inflammatory effects of omega-3 polyunsaturated fatty acids (PUFAs) via inhibition of NLRP3 inflammasome activation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O14842}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14842}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Free fatty acid receptor 4
- Pro-glucagon
- Guanine nucleotide-binding protein subunit alpha-11
- Gastric inhibitory polypeptide
- G protein-coupled receptor 84
- Glucose-dependent insulinotropic receptor
- G-protein coupled receptor 142
- Peroxisome proliferator-activated receptor gamma
Sequence:
MDLPPQLSFALYVSAFALGFPLNLLAIRGAVSHAKLRLTPSLVYTLHLACSDLLLAITLPLKAVEALASGVWPLPLPFCPVFALAHFAPLYAGGGFLAALSAGRYLGAAFPFGYQAIRRPCYSWGVCVAIWALVLCHLGLALGLEAPRGWVDNTTSSLGINIPVNGSPVCLEAWDPDSARPARLSFSILLFFLPLVITAFCYVGCLRALVHSGLSHKRKLRAAWVAGGALLTLLLCLGPYNASNVASFINPDLEGSWRKLGLITGAWSVVLNPLVTGYLGTGPGQGTICVTRTPRGTIQK
Protein: Up-regulator of cell proliferation (HBV X protein up-regulated gene 4 protein) (HBxAg up-regulated gene 4 protein) (Q8TCY9)
Organism: Homo sapiens (Human)
Function: May be involved in cell cycle progression through the regulation of cyclin D1 expression. May participate in the development of hepatocellular carcinoma (HCC) by promoting hepatocellular growth and survival. May play an important role in development of gastric cancer.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}. Nucleus {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}. Note=In epithelial cells localized predominantly in the cytoplasm and occasionally in nuclei.
Interaction partners:
Sequence:
MASPGIEVELLGKGHSDLGEVAPEIKASERRTAVAIADLEWREMEGDDCEFRYGDGTNEAQDNDFPTVERSRLQEMLSLLGLETYQVQKLSLQDSLQISFDSMKNWAPQVPKDLPWNFLRKLQALNADARNTTMVLDVLPDARPVEKESQMEEEIIYWDPADDLAADIYSFSELPTPDTPVNPLDLLCALLLSSDSFLQQEIALKMALCQFALPLVLPDSENHYHTFLLWAMRGIVRTWWSQPPRGMGSFREDSVVLSRAPAFAFVRMDVSSNSKSQLLNAVLSPGHRQWDCFWHRDLNLGTNAREISDGLVEISWFFPSGREDLDIFPEPVAFLNLRGDIGSHWLQFKLLTEISSAVFILTDNISKKEYKLLYSMKESTTKYYFILSPYRGKRNTNLRFLNKLIPVLKIDHSHVLVKVSSTDSDSFVKRIRAIVGNVLRAPCRRVSVEDMAHAARKLGLKVDEDCEECQKAKDRMERITRKIKDSDAYRRDELRLQGDPWRKAAQVEKEFCQLQWAVDPPEKHRAELRRRLLELRMQQNGHDPSSGVQEFISGISSPSLSEKQYFLRWMEWGLARVAQPRLRQPPETLLTLRPKHGGTTDVGEPLWPEPLGVEHFLREMGQFYEAESCLVEAGRLPAGQRRFAHFPGLASELLLTGLPLELIDGSTLSMPVRWVTGLLKELHVRLERRSRLVVLSTVGVPGTGKSTLLNTMFGLRFATGKSCGPRGAFMQLITVAEGFSQDLGCDHILVIDSGGLIGGALTSAGDRFELEASLATLLMGLSNVTVISLAETKDIPAAILHAFLRLEKTGHMPNYQFVYQNLHDVSVPGPRPRDKRQLLDPPGDLSRAAAQMEKQGDGFRALAGLAFCDPEKQHIWHIPGLWHGAPPMAAVSLAYSEAIFELKRCLLENIRNGLSNQNKNIQQLIELVRRL
Protein: Pantothenate kinase 3 (mPanK3) (EC 2.7.1.33) (Pantothenic acid kinase 3) (Q8R2W9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16040613, ECO:0000269|PubMed:23152917, ECO:0000305}.
Interaction partners:
- Bifunctional coenzyme A synthase
- Phosphopantothenoylcysteine decarboxylase
- Phosphopantothenate--cysteine ligase
- Pantothenate kinase 2
- Pantetheinase
- Vascular non-inflammatory molecule 3
- Pantothenate kinase 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MKIKDAKKPSFPWFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTFIQMGRDKNFSTLQTVLSATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADRLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRETVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAVGALLGLPNFS
Protein: Zinc finger MYND-type containing 11 (E7EV75)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MARLTKRRQADTKAIQHLWAAIEIIRNQKQIANIDRITKYMSRVHGMHPKETTRQLSLAVKDGLIVETLTVGCKGSKAGIEQEGYWLPGDEIAYSMQPFSRTAAPNKDWETENHDWYCFECHLPGEVLICDLCFRVYHSKCLSDEFRLRDSSSPWQCPVCRSIKKKNTNKQEMGTYLRFIVSRMKERAIDLNKKGKDNKHPMYRRLVHSAVDVPTIQEKVNEGKYRSYEEFKADAQLLLHNTVIFYGADSEQADIARMLYKDTCHELDELQLCKNCFYLSNARPDNWFCYPCIPNHELVWAKMKGFGFWPAKVMQKEDNQVDVRFFGHHHQRAWIPSENIQDITVNIHRLHVKRSMGWKKACDELELHQRFLREGRFWKSKNEDRGEEEAESSISSTSNEQLKVTQEPRAKKGRRNQSVEPKKEEPEPETEAVSSSQEIPTMPQPIEKVSVSTQTKKLSASSPRMLHRSTQTTNDGVCQSMCHDKYTKIFNDFKDRMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFVEEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR