wanglab/gogpt-training-data huggingface dataset:
Protein: Paraspeckle component 1 (Paraspeckle protein 1) (Q8WXF1)
Organism: Homo sapiens (Human)
Function: Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line (By similarity). Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity). Together with NONO, required for the formation of nuclear paraspeckles. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:11790299, ECO:0000269|PubMed:16148043, ECO:0000269|PubMed:28712728}. Nucleus, nucleolus {ECO:0000269|PubMed:11790299}. Nucleus matrix {ECO:0000250|UniProtKB:Q8R326}. Cytoplasm {ECO:0000250|UniProtKB:Q8R326}. Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles (PubMed:11790299, PubMed:16148043). Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps in an RNA-dependent manner (PubMed:11790299, PubMed:16148043). May cycle between paraspeckles and nucleolus (PubMed:11790299). In telophase, when daughter nuclei form, localizes to perinucleolar caps (PubMed:11790299). {ECO:0000269|PubMed:11790299, ECO:0000269|PubMed:16148043}.
Interaction partners:
- Non-POU domain-containing octamer-binding protein
- Splicing factor, proline- and glutamine-rich
- RNA-binding protein 14
- RNA-binding protein 14
- Matrin-3
- RNA-binding protein FUS
- Cleavage and polyadenylation specificity factor subunit 6
- TAR DNA-binding protein 43
Sequence:
MMLRGNLKQVRIEKNPARLRALESAVGESEPAAAAAMALALAGEPAPPAPAPPEDHPDEEMGFTIDIKSFLKPGEKTYTQRCRLFVGNLPTDITEEDFKRLFERYGEPSEVFINRDRGFGFIRLESRTLAEIAKAELDGTILKSRPLRIRFATHGAALTVKNLSPVVSNELLEQAFSQFGPVEKAVVVVDDRGRATGKGFVEFAAKPPARKALERCGDGAFLLTTTPRPVIVEPMEQFDDEDGLPEKLMQKTQQYHKEREQPPRFAQPGTFEFEYASRWKALDEMEKQQREQVDRNIREAKEKLEAEMEAARHEHQLMLMRQDLMRRQEELRRLEELRNQELQKRKQIQLRHEEEHRRREEEMIRHREQEELRRQQEGFKPNYMENREQEMRMGDMGPRGAINMGDAFSPAPAGNQGPPPMMGMNMNNRATIPGPPMGPGPAMGPEGAANMGTPMMPDNGAVHNDRFPQGPPSQMGSPMGSRTGSETPQAPMSGVGPVSGGPGGFGRGSQGGNFEGPNKRRRY
Protein: Serine/threonine-protein kinase ULK2 (EC 2.7.11.1) (Unc-51-like kinase 2) (Q8IYT8)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18936157}; Peripheral membrane protein {ECO:0000269|PubMed:18936157}. Note=Localizes to pre-autophagosomal membrane.
Interaction partners:
- RB1-inducible coiled-coil protein 1
- Autophagy-related protein 101
- Autophagy-related protein 13
- Beclin-1
- Serine/threonine-protein kinase ULK1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphoinositide 3-kinase regulatory subunit 4
- Autophagy-related protein 2 homolog B
- Autophagy-related protein 2 homolog A
- Serine/threonine-protein kinase mTOR
Sequence:
MEVVGDFEYSKRDLVGHGAFAVVFRGRHRQKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQELPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLHQIAAAMRILHSKGIIHRDLKPQNILLSYANRRKSSVSGIRIKIADFGFARYLHSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNRSLMPSIPRETSPYLANLLLGLLQRNQKDRMDFEAFFSHPFLEQGPVKKSCPVPVPMYSGSVSGSSCGSSPSCRFASPPSLPDMQHIQEENLSSPPLGPPNYLQVSKDSASTSSKNSSCDTDDFVLVPHNISSDHSCDMPVGTAGRRASNEFLVCGGQCQPTVSPHSETAPIPVPTQIRNYQRIEQNLTSTASSGTNVHGSPRSAVVRRSNTSPMGFLRPGSCSPVPADTAQTVGRRLSTGSSRPYSPSPLVGTIPEQFSQCCCGHPQGHDSRSRNSSGSPVPQAQSPQSLLSGARLQSAPTLTDIYQNKQKLRKQHSDPVCPSHTGAGYSYSPQPSRPGSLGTSPTKHLGSSPRSSDWFFKTPLPTIIGSPTKTTAPFKIPKTQASSNLLALVTRHGPAEEQSKDGNEPRECAHCLLVQGSERQRAEQQSKAVFGRSVSTGKLSDQQGKTPICRHQGSTDSLNTERPMDIAPAGACGGVLAPPAGTAASSKAVLFTVGSPPHSAAAPTCTHMFLRTRTTSVGPSNSGGSLCAMSGRVCVGSPPGPGFGSSPPGAEAAPSLRYVPYGASPPSLEGLITFEAPELPEETLMEREHTDTLRHLNVMLMFTECVLDLTAMRGGNPELCTSAVSLYQIQESVVVDQISQLSKDWGRVEQLVLYMKAAQLLAASLHLAKAQIKSGKLSPSTAVKQVVKNLNERYKFCITMCKKLTEKLNRFFSDKQRFIDEINSVTAEKLIYNCAVEMVQSAALDEMFQQTEDIVYRYHKAALLLEGLSRILQDPADIENVHKYKCSIERRLSALCHSTATV
Protein: Tubby-related protein 1 (Tubby-like protein 1) (O00294)
Organism: Homo sapiens (Human)
Function: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells (By similarity). Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16303976}. Cell membrane {ECO:0000269|PubMed:16303976}; Peripheral membrane protein {ECO:0000269|PubMed:16303976}; Cytoplasmic side {ECO:0000269|PubMed:16303976}. Secreted {ECO:0000250}. Synapse {ECO:0000250}. Note=Detected at synapses between photoreceptor cells and second-order neurons. Does not have a cleavable signal peptide and is secreted by an alternative pathway (By similarity). {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase Mer
- Aryl-hydrocarbon-interacting protein-like 1
- Retinoid isomerohydrolase
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 12
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Retinal guanylyl cyclase 1
- Cone-rod homeobox protein
- Spermatogenesis-associated protein 7
- Ceramide kinase-like protein
Sequence:
MPLRDETLREVWASDSGHEEESLSPEAPRRPKQRPAPAQRLRKKRTEAPESPCPTGSKPRKPGAGRTGRPREEPSPDPAQARAPQTVYARFLRDPEAKKRDPRETFLVARAPDAEDEEEEEEEDEEDEEEEAEEKKEKILLPPKKPLREKSSADLKERRAKAQGPRGDLGSPDPPPKPLRVRNKEAPAGEGTKMRKTKKKGSGEADKDPSGSPASARKSPAAMFLVGEGSPDKKALKKKGTPKGARKEEEEEEEAATVIKKSNQKGKAKGKGKKKAKEERAPSPPVEVDEPREFVLRPAPQGRTVRCRLTRDKKGMDRGMYPSYFLHLDTEKKVFLLAGRKRKRSKTANYLISIDPTNLSRGGENFIGKLRSNLLGNRFTVFDNGQNPQRGYSTNVASLRQELAAVIYETNVLGFRGPRRMTVIIPGMSAENERVPIRPRNASDGLLVRWQNKTLESLIELHNKPPVWNDDSGSYTLNFQGRVTQASVKNFQIVHADDPDYIVLQFGRVAEDAFTLDYRYPLCALQAFAIALSSFDGKLACE
Protein: Pre-mRNA-splicing factor ISY1 (Interactor of SYF1) (PRP19-associated complex protein 30) (P21374)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing and cell cycle control. As a component of the NTC complex (or PRP19-associated complex), associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. The cell cycle arrest of SYF2 defective cells may be due to the inefficient splicing of TUB1. Also involved in DNA repair.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor BUD31
- Splicing factor YJU2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor NTC20
- Pre-mRNA-splicing factor PRP46
- Pre-mRNA-splicing factor SNT309
Sequence:
MSRNVDKANSVLVRFQEQQAESAGGYKDYSRYQRPRNVSKVKSIKEANEWKRQVSKEIKQKSTRIYDPSLNEMQIAELNDELNNLFKEWKRWQWHIDHTLMEKKTKRKRLEDSHVLMNSGKLINGKRYFGRALELPEVKEWLKQSQRQNDGGSINTKCIPKDRNDFYYHGKVTAALTEFEANWTSILKAHYNVPVNEDEEEMSRQTQEIHVPTLADMEHWLVQRRKKKLMDELNL
Protein: Phosducin-like protein 3 (Viral IAP-associated factor 1) (VIAF-1) (Q8BVF2)
Organism: Mus musculus (Mouse)
Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation. Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27496612}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta
Sequence:
MQDPNADTEWNDILRKKGILPPKESLKELEEEEAEKEEQLLQQSVVKTYEDMTLEELEENEDEFSEEDERAIEMYRQQRLAEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCSLINHHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTVFVYREGDIKAQFIGPLVFGGMNLTIDELEWKLSESGAIKTALEENPKKPIQDLLLSSVRGPVPMRRDSDSEDD
Protein: ADP-ribosylation factor-like protein 4D (ADP-ribosylation factor-like protein 4L) (ADP-ribosylation factor-like protein 5) (Q99PE9)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:12414990}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Cytohesin-2
Sequence:
MGNHLTEMAPTASSFLPHFQALHVVVIGLDSAGKTSLLYRLKFKEFVQSVPTKGFNTEKIRVPLGGSRGITFQVWDVGGQEKLRPLWRSYTRRTDGLVFVVDSAETERLEEARMELHRISKASDNQGVPVLVLANKQDQPGALSAAEVEKRLAVRELAAATLTHVQGCSAVDGLGLQPGLEHLYEMILKRKKAPRSSKKRR
Protein: Mhp1p (A0A1D8PT36)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MTSTDEDSGKNQFSTPKAQQLSTNGSFPLIDQKTKPQLDMEKMRDILAEETCLYTKGVQDTDVDWFITDSSIDPNADVQPSVSSPRETNLNSQATIPTSHLTSAISNSNENYTNKTKPSIAPIQEENIASDTSPRHHRHEIEQQQPRRRSSVSVSTSGGFLSKLKSKFHKESPTPPGNHQDGLFKSGYSVNPDKKSNDSSNSSIASLSSSPKLVSGSNLQRTMSTPAYTHDTCDPRLEEYIKFYRKSDRRASVASSSHSAKDECLPSVLVNASEPTNYNKTKDEVNASRVSGFFKRKNSVAMKNGETSSPRSSVSVSVTPQSQVKNGLENNPSFQGLKPLKRVAFHSSTFLIDPPQQIPSRTPRKGNVEVLPNGTVNIRPLTDEERLEIEKSQKGLGGGIVVGGTGALGYIKKDSDPPKPGENNLNAQDDDNNDDGSNQSSESSQLESEPSVDKHAKSFTIDTPMARHQAVNYSVPIKKMALDTMYARCCHLREILPIPAILKQIPKGSIAPIPVLQLRNPTPTMIEIQSFADFLRIAPVICVSLDGVNFSVEQFKILLSAMSAKKQLEKLSLRNTPIDQKGWSLLCWFLSRNTVLNRLDITQCPSLSVNTLKKKKKKTDSKFDETLVRMVSNKDNRSDVDWELFVATLVARGGIEELILTGCCITDIEIFEKLISLAVSKKTSRLGLAFNQLTSRHMKIIVDEWLFKDFARGIDFGYNDFSSVHMLKILVDYSKRPDFDQILSKSTLSFVSLNSTNVSLGDIFKESFERVLMKLPNLKYVDFSNNQRLFGTFGKSDNEEADANEVASVNYFISKLPLFPKLVRLHLENENFSKSSVLQIAEILPFCKSLGYFSILGSKLDFTCGSALVNAVKNSQSLINVDADSDNFPDIFKERMGLYTMRNMERLLYSAKKADVKTPLLSEDSAGNVSMTEQLHEILRLKSQQKLDLQSPEITKFIERAKSISHGLRQTINELLRMQLKNRLDLDGKETLIRLIFIDSSIEKGLMLIDPSLVDDNNKNAGYLTSMIGTREGNEETQQFEQSDHLDPQPAASVLANKSPSVMSRSDSRTSLNNLNKEEGSVLKLAKLRDFHSPNSPYPESTGEELRNKLMSVELADLDKVIDFLSDLKKKGVSLEKVFQCHENQGANDHEEGLLDIEHIKSRLQKLSVEQMDGVSKDVDTDADEINTGTDKTHALNNTYDEVLKNLFK
Protein: Hexosyltransferase (EC 2.4.1.-) (Q580N7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MRFVSKGVRRIWRTEDYLVVAGIHSIDNDERFIRRNLQRETCWSYHEVSRKSNNFTGKLLIVYALSAHTNNNCVLRDIVEEEAKLNQDVIIFPVCDVNPTTSKKVGDAGNWGWEAELTMSRKTYLWFKLAVETFKSTNPYIMKADDDIFMRAPLYLKYLEVLPRGKLNMGRALGELDEYIDKMTWYVVGYANTISRDVVKEIVGFLEISKLLVRKISFRNFEKYIDYAASNEDIMVGEVLRHKMKLDSLLTVDIQDCHYVMHVKRPLHKFVRENPNLIVFHHIAEEEYA
Protein: Variant surface glycoprotein (VSG), putative (Q57TR6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MKAITTTIGTLWILSAHWTKADTNAADNEPDFTVLCSVLDVATGKPALNDIPTKWRNLRQQLTDINISLSTGDWTKHLLDTDGNVQEWTKAQQAGKLPEDWATEWPAWAAAAKRSAKGGETHDKLQASGIPSLDAEQRKEAAQLIKHLLNSTQPLMDALQGVETAEAATTAAALAATLDQSVYGDKPEAHPGKQASAAVRRTATRGICASGAKIGTSQALADALLCLCWTDTGSPPQGQGSVCRKNLGNTLTSTWDTASATVNAAYAQIKGACKLQTGHTITAANIAEALAAVKHKIAQHKEGGYLGKYEGDFSCDGKNANGVCIKYADFSDKGNKAFEEIEWVKKLRSVETALRKREAAVARVDTLTTALETQTAAAWLIPQRAKSSQQKREGVSPKQHTSTGNGNKQQADQCEAIKKATECKEKQPNCEWQGKNDEDGPHCKVNKTHITKEAAQTGTNRGNEETTTDKCSQAKTSDECAAVKGDIPKDKKSVCGWIEGKCQNSRFPVNKKLTLMVSAFVSIAAF
Protein: Protein kinase C (PKC) (EC 2.7.11.13) (dPKC98F) (P13678)
Organism: Drosophila melanogaster (Fruit fly)
Function: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.
Interaction partners:
- Ras-like GTP-binding protein Rho1
- LD29223p
- 3-phosphoinositide-dependent protein kinase 1
- Putative protein kinase C delta type homolog
- Cdc42 homolog
Sequence:
MFTGKLQIKVCEASGLRPTDFQKRHNLTFGKLADEQLIDPYVSIDVDESHFDRATTRPKTFDPVWNEQFVHDVTNVSNINLTVFHDAALPPDDFVANCIISFEDLMQSETAVQDLWVNLEPQGKIHVIIELKNRTDKAKAEAVVEHTVAVNKEFKERAGFNRRRGAMRRRVHQVNGHKFMATFLRQPTFCSHCREFIWGIGKQGYQCQVCTLVVHKKCHLSVVSKCPGMRDEQPAKVEMVPAGQRFNVNLPHRFVVHSYKRFTFCDHCGSLLYGLIKQGLQCETCGMNVHKRCQKNVANTCGINTKQMAEILSSLGISPDKQQPRRSKYLNQQGGEDNYGASLGADGDGAPGQSFRSCALSVDSLATSTTTMTSGYNSSSCMSLAVTGSGGVGATGETRPGKCSLLDFNFIKVLGKGSFGKVMLAEKKGTDEIYAIKVLKKDAIIQDDDVDCTMTEKRILALAANHPFLTALHSCFQTPDRLFFVMEYVNGGDLMFQIQKARRFEASRAAFYAAEVTLALQFLHTHGVIYRDLKLDNILLDQEGHCKLADFGMCKEGIMNGMLTTTFCGTPDYIAPEILKEQEYGASVDWWALGVLMYEMMAGQPPFEADNEDELFDSIMHDDVLYPVWLSREAVSILKGFLTKNPEQRLGCTGDENEIRKHPFFAKLDWKELEKRNIKPPFRPKMKNPRDANNFDAEFTKEDPVLTPIGNEVVRCINQDEFAGFSFVNPKFGPERKVY
Protein: GTPase-binding protein rid1 (O74737)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes at the cell tip and the barrier septum.
Interaction partners:
Sequence:
MNSLRSVKRLLGARSLSSDGLSESVNSSDREDSLSFQTPSTPSEDEMPQCFEDLIKPQVLSSEASKSLLSLNEGIKMEIVSSLQQKDQKKRNKLIAWMRKKPCYEQPDDFISYIVNTKIDSIDESIIHKLALLLRNEQVIWVEKFIHNGGFGVVFCTIDKISRLEWREELHDSILEQLLLCVKAMCTVQRGLECLSQSTYNVERLISLLLSKKQPCDFVVREVLVQIVHSFYKAHLDKEEGAMQVFSLFSIKDDKDEEVEFLKNVRVDRPFRRWIIELEDVSRNVFWVWNHDSNVIDLEKQYNQVYEAPLGFIGGIETEATSYVAAHIHLINELLEGLPLEKRQRKRLELQLSGLERIMGLRFRKSSQKFHKKLHEALREWIVAAKIDDWPYKLVQTGST
Protein: Probable cyclic di-GMP phosphodiesterase PdeA (EC 3.1.4.52) (P23842)
Organism: Escherichia coli (strain K12)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable diguanylate cyclase DgcJ
- Probable diguanylate cyclase CdgI
- Diguanylate cyclase DgcP
- Cyclic di-GMP phosphodiesterase PdeH
- Probable diguanylate cyclase DgcC
- HTH-type transcriptional regulator XapR
- Diguanylate cyclase DgcN
- Probable diguanylate cyclase DgcF
- Probable diguanylate cyclase DgcI
- Diguanylate cyclase DgcM
Sequence:
MFVEHNLIKNIKIFTLAFTLTVVLIQLSRFISPLAIIHSSYIFLAWMPLCVMLSILFIFGWRGVVPVLCGMFCTNLWNFHLSFLQTAVMLGSQTFVVLCACAILRWQLGTRWRYGLTSRYVWQRLFWLGLVTPIGIKCSMYLVGSFFDFPLKISTFFGDADAIFTVVDLLSLFTAVLIYNMLFYYLTRMIVSPHFAQILWRRDIAPSLGKEKRAFTLSWLAALSVLLLLLCTPYENDFIAGYLVPVFFIIFTLGVGKLRYPFLNLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRIYHRSEWLNRRWHLQALTDPLTLLPNFRALEQAPEQEAGKSFCCLRIDNLEFMSRHYGLMMRVHCIRSICRTLLPLMQENEKLYQLPGSELLLVLSGPETEGRLQHMVNILNSRQIHWNNTGLDMGYGAAWGRFDGNQETLQPLLGQLSWLAEQSCAHHHVLALDSREEMVSGQTTKQVLLLNTIRTALDQGDLLLYAQPIRNKEGEGYDEILARLKYDGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLAD
Protein: Protein IQ-DOMAIN 30 (AtIQD30) (Q501D2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
Interaction partners:
- Protein IQ-DOMAIN 9
- Protein IQ-DOMAIN 33
- At1g23060/T26J12_16
- Protein IQ-DOMAIN 10
- Pyridoxal 5'-phosphate synthase subunit PDX1.1
- 187-kDa microtubule-associated protein AIR9
Sequence:
MGKPARWLKSVLLGKKPSKSSGSKDKERIVNGKEVVVISKIEESDVVSDLSSIGNAAVYTSGIVETQNLKHEDVSDDEIQVSEVQPTDSQDVASVPDDSLSESEKIQQEIAAVTVQAAYRGYLARRAFKILKGIIRLQALIRGHMVRRQAVSTLCCVMGIVRLQALARGREIRHSDIGVEVQRKCHLHHQPLENKANSVVDTHSYLGINKLTGNAFAQKLLASSPNVLPLSLDNDSSNSIWLENWSASCFWKPVPQPKKASLRKSQKKFASNPQIVEAEFARPKKSVRKVPSSNLDNSSVAQTSSELEKPKRSFRKVSTSQSVEPLPSMDNPQVDLEKVKRGLRKVHNPVVENSIQPQLVPQIAVEKPNGSLEESVNAFDEEKEDEVAETVVQQPEELIQTHTPLGTNESLDSTLVNQIEESEENVMAEEKEDVKEERTPKQNHKENSAGKENQKSGKKASSVTATQTAEFQESGNGNQTSSPGIPSYMQATKSAKAKLRLQGSSSPRQLGTTEKASRRYSLPSSGNSAKITSHSPKTRVSNSSGKSGNKTEKTLLSSREGNGKATPVEWKR
Protein: Low-density lipoprotein receptor-related protein 3 (LRP-3) (105 kDa low-density lipoprotein receptor-related protein) (hLRp105) (O75074)
Organism: Homo sapiens (Human)
Function: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. Its precise role is however unclear, since it does not bind to very low density lipoprotein (VLDL) or to LRPAP1 in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Membrane, coated pit {ECO:0000250}.
Interaction partners:
- Alpha-2-macroglobulin receptor-associated protein
Sequence:
MEKRAAAGLEGAPGARAQLAVVCLVNIFLTGRLSSAVPALAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQASCQADEFRCDNGKCLPGPWQCNTVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGLQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDSRRVLLQLELRLGYDDYVQVYEGLGERGDRLLQTLSYRSNHRPVSLEAAQGRLTVAYHARARSAGHGFNATYQVKGYCLPWEQPCGSSSDSDGGSLGDQGCFSEPQRCDGWWHCASGRDEQGCPACPPDQYPCEGGSGLCYTPADRCNNQKSCPDGADEKNCFSCQPGTFHCGTNLCIFETWRCDGQEDCQDGSDEHGCLAAVPRKVITAALIGSLVCGLLLVIALGCAFKLYSLRTQEYRAFETQMTRLEAEFVRREAPPSYGQLIAQGLIPPVEDFPVYSASQASVLQNLRTAMRRQMRRHASRRGPSRRRLGRLWNRLFHRPRAPRGQIPLLTAARPSQTVLGDGFLQPAPGAAPDPPAPLMDTGSTRAAGDRPPSAPGRAPEVGPSGPPLPSGLRDPECRPVDKDRKVCREPLVDGPAPADAPREPCSAQDPHPQVSTASSTLGPHSPEPLGVCRNPPPPCSPMLEASDDEALLVC
Protein: ATP-binding cassette sub-family D member 3 (EC 3.1.2.-) (EC 7.6.2.-) (68 kDa peroxisomal membrane protein) (PMP68) (70 kDa peroxisomal membrane protein) (PMP70) (P55096)
Organism: Mus musculus (Mouse)
Function: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation. Has fatty acyl-CoA thioesterase and ATPase activities (By similarity). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation.
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P28288}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family D member 1
- Peroxisomal biogenesis factor 19
- ATP-binding cassette sub-family D member 2
- DNA repair protein RAD51 homolog 1
- Peroxisomal membrane protein PEX16
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein 11B
- Peroxisome assembly protein 12
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX14
Sequence:
MAAFSKYLTARNTSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSIIAKYVATVVGYLVVSRPFLDLAHPRHLHSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGRYERTMVSQQEKGIEGAQASPLVPGAGEIINTDNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKITEDTVEFGS
Protein: Retroelement silencing factor 1 (Q9HCM1)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of imprinted gene expression, regulates repressive epigenetic modifications associated with SETDB1. Required for the recruitment or accumulation of SETDB1 to the endogenous retroviruses (ERVs) and maintenance of repressive chromatin configuration, contributing to a subset of the SETDB1-dependent ERV silencing in embryonic stem cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5DTW7}. Note=Localizes around gamma-tubulin during M phase. {ECO:0000250|UniProtKB:Q5DTW7}.
Interaction partners:
Sequence:
MNWNEKPKSATLPPLYPKSQPPFLHQSLINQITTTSQSSFSYPGSNQEACMYPGNSNPISQPLLNIQNYPQQISVSDMHNGTVVASHTSVERITYANVNGPKQLTHNLQMSSGVTQNVWLNSPMRNPVHSHIGATVSHQTDFGANVPNMPALQSQLITSDTYSMQMQMIPSNSTRLPVAYQGNQGLNQSFSEQQVDWTQQCISKGLTYPDYRPPPKLYRYSPQSFLPDSTIQKQNFIPHTSLQVKNSQLLNSVLTLPSRQTSAVPSQQYATQTDKRPPPPPYNCRYGSQPLQSTQHITKHLSMEVPQSREMLSSEIRTSFQQQWQNPNENVSTIGNFTNLKVNTNSKQPFNSPIRSSVDGVQTLAQTNEEKIMDSCNPTSNQVLDTSVAKEKLVRDIKTLVEIKQKFSELARKIKINKDLLMAAGCIKMTNTSYSEPAQNSKLSLKQTAKIQSGPQITPVMPENAERQTPTVVESAETNKTQCMLNSDIQEVNCRRFNQVDSVLPNPVYSEKRPMPDSSHDVKVLTSKTSAVEMTQAVLNTQLSSENVTKVEQNSPAVCETISVPKSMSTEEYKSKIQNENMLLLALLSQARKTQKTVLKDANQTIQDSKPDSCEMNPNTQMTGNQLNLKNMETPSTSNVSGRVLDNSFCSGQESSTKGMPAKSDSSCSMEVLATCLSLWKKQPSDTAKEKECDKLRTNTTAVGISKPANIHVKSPCSVVGNSNSQNKISNPSQQTALSMVMHNYESSGINITKGTELQIAVVSPLVLSEVKTLSVKGITPAVLPETVYPVIKEGSVCSLQNQLAENAKATAALKVDVSGPVASTATSTKIFPLTQKEKQNESTNGNSEVTPNVNQGKHNKLESAIHSPMNDQQISQESRNSTVVSSDTLQIDNICSLVEGDTSYNSQIAKIFSSLPLKMVEPQKPSLPNQQGIGSREPEKQLDNTTENKDFGFQKDKPVQCTDVSHKICDQSKSEPPLESSFNNLETNRVILEKSSLEHATEKSTANDTCSSAAIQEDIYPQEIDASSNYTPQDPARNEIHSDKAPVLYLHDQLSELLKEFPYGIEAVNTREGSVGQQTTYQTSEDQTADKTSSDSKDPADQIQITILSSEQMKEIFPEQDDQPYVVDKLAEPQKEEPITEVVSQCDLQAPAAGQSRDSVILDSEKDDIHCCALGWLSMVYEGVPQCQCNSIKNSSSEEEKQKEQCSPLDTNSCKQGERTSDRDVTVVQFKSLVNNPKTPPDGKSHFPELQDDSRKDTPKTKHKSLPRTEQELVAGQFSSKCDKLNPLQNHKRKKLRFHEVTFHSSNKMTASYEQASQETRQKKHVTQNSRPLKTKTAFLPNKDVYKKHSSLGQSLSPEKIKLKLKSVSFKQKRKLDQGNVLDMEVKKKKHDKQEQKGSVGATFKLGDSLSNPNERAIVKEKMVSNTKSVDTKASSSKFSRILTPKEYLQRQKHKEALSNKASKKICVKNVPCDSEHMRPSKLAVQVESCGKSNEKHSSGVQTSKESLNGLTSHGKNLKIHHSQESKTYNILRNVKEKVGGKQPDKIWIDKTKLDKLTNISNEAQFSQMPPQVKDQKKLYLNRVGFKCTERESISLTKLESSPRKLHKDKRQENKHKTFLPVKGNTEKSNMLEFKLCPDILLKNTNSVEERKDVKPHPRKEQAPLQVSGIKSTKEDWLKFVATKKRTQKDSQERDNVNSRLSKRSFSADGFEMLQNPVKDSKEMFQTYKQMYLEKRSRSLGSSPVK