wanglab/gogpt-training-data huggingface dataset:
Protein: TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta) (Q80UF7)
Organism: Mus musculus (Mouse)
Function: Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively. Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8IUC6}. Mitochondrion {ECO:0000269|PubMed:21703541}. Note=Colocalizes with UBQLN1 in the autophagosome. Colocalizes in the cytosol with DDX1, DDX21 and DHX36 (PubMed:21703541). Colocalizes in the mitochondria with DDX1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q8IUC6, ECO:0000269|PubMed:21703541}.
Interaction partners:
- Toll-like receptor 4
- Toll-like receptor 3
- TNF receptor-associated factor 6
- TNF receptor-associated factor 3
- Interferon regulatory factor 3
- Receptor-interacting serine/threonine-protein kinase 1
- Toll-like receptor 2
- Interferon regulatory factor 7
- Receptor-interacting serine/threonine-protein kinase 3
- Interleukin-1 receptor-associated kinase 4
Sequence:
MDNPGPSLRGAFGILGALERDRLTHLKHKLGSLCSGSQESKLLHAMVLLALGQDTEARVSLESLKMNTVAQLVAHQWADMETTEGPEEPPDLSWTVARLYHLLAEENLCPASTRDMAYQVALRDFASQGDHQLGQLQNEAWDRCSSDIKGDPSGFQPLHSHQGSLQPPSASPAVTRSQPRPIDTPDWSWGHTLHSTNSTASLASHLEISQSPTLAFLSSHHGTHGPSKLCNTPLDTQEPQLVPEGCQEPEEISWPPSVETSVSLGLPHEISVPEVSPEEASPILPDALAAPDTSVHCPIECTELSTNSRSPLTSTTESVGKQWPITSQRSPQVPVGDDSLQNTTSSSPPAQPPSLQASPKLPPSPLSSASSPSSYPAPPTSTSPVLDHSETSDQKFYNFVVIHARADEQVALRIREKLETLGVPDGATFCEEFQVPGRGELHCLQDAIDHSGFTILLLTASFDCSLSLHQINHALMNSLTQSGRQDCVIPLLPLECSQAQLSPDTTRLLHSIVWLDEHSPIFARKVANTFKTQKLQAQRVRWKKAQEARTLKEQSIQLEAERQNVAAISAAYTAYVHSYRAWQAEMNKLGVAFGKNLSLGTPTPSWPGCPQPIPSHPQGGTPVFPYSPQPPSFPQPPCFPQPPSFPQPPSFPLPPVSSPQSQSFPSASSPAPQTPGPQPLIIHHAQMVQLGVNNHMWGHTGAQSSDDKTECSENPCMGPLTDQGEPLLETPE
Protein: Lipoate-protein ligase LplJ (EC 6.3.1.20) (Lipoate--protein ligase) (O07608)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Lipoyl synthase
- Octanoyl-[GcvH]:protein N-octanoyltransferase
- Glycine cleavage system H protein
- Probable metallo-hydrolase YhfI
- Lipoprotein LipO
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase
- Dihydrolipoyl dehydrogenase
- Protein LplB
- Dihydrolipoyl dehydrogenase
Sequence:
MLFIDNQNINDPRINLAIEEYCVKHLDPEQQYLLFYVNQPSIIIGKNQNTIEEINTKYVEENGIIVVRRLSGGGAVYHDLGNLNFSFITKDDGDSFHNFKKFTEPVIQALHQLGVEAELSGRNDIVVDGRKISGNAQFATKGRIFSHGTLMFDSAIDHVVSALKVKKDKIESKGIKSIRSRVANISEFLDDKMTTEEFRSHLLRHIFNTNDVGNVPEYKLTEKDWETIHQISKERYQNWDWNYGRSPKFNLNHSKRYPVGSIDLHLEVKKGKIEDCKIFGDFFGVGDVSEIENLLVGKQYERSVIADVLEGVNLKHYFGNITKEDFLDLIY
Protein: Chromatin structure-remodeling complex subunit SFH1 (A0A1D8PEB6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Chromatin structure-remodeling complex protein RSC8
- Uncharacterized protein
- Bromo domain-containing protein
- RSC chromatin remodeling complex ATPase subunit
- Npl6p
- Uncharacterized protein
- RFX-type winged-helix domain-containing protein
- Chromatin structure-remodeling complex subunit RSC1
- Arp9p
- Chromatin structure-remodeling complex protein RSC58
Sequence:
MATSQELTADIQALATSFPKRLANDSDNSLLINVAPTGRQAKRHIQQINYSEEFGDDLDFDEFPSSTPGTRSLNENKAQIEAQRYSLAKNTPTPKRILEKPVLSELVEKPVVLIPIKIMIENLNTNQKLIDSFMWNLNESLITPTEFAEIVCSDLDLPFSMAAQIADSINQQIEEYSYASNLQLPNKGPYNVTIDLSVNLNKQLYQDRFEWDMNQNEVTPEIFAEIVVADLGLSLEFKNAISHALHEIIIRVKKEVIDGTFNNEMHNLHLVKGIMFEQGIRIFTENSVQNGNDRWEPLVEVLTSSEIERRENERVRNLRRLKRENMRRDYDDHSRRRQAGKRRYDELEGAWV
Protein: Dal81p (Q5A876)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glutamyl-tRNA
Sequence:
MDNQSPNFMDQNWTPHMLPQTASYLANLDLPNIPTTHSNNHYNNNNNSGLNPSYNTSSIMQTIQNQHNVHDDQENQQQQHHHHQYINSNSPSSSSHQVTPNPTISSSSSSSKSNKQKRPCDQCRKRKIKCVLVPNTNNCVQCEAKQVTCTYTDQAPKRKLAETTTPANNDQLLKRGRIMDTSLLSNGSTIVPPDVAIREVSPIQDYSAMNNSLLKRTLSLQFPRSSFYVGPTSSVFDINLLNSIIKSHEHQMANGNESTTTARNNNSNNKIEQVSLNNLVSLRKVSDTVQFILKEDQSPQSYQTMSNDVDTIEKFISPHGQILVDLYFRIIHPSYPIIHKKVFIEKYSRTHREFSAPLLAAVYVLAIQWWDYDPQLNRFPKPNVEMILKIGLNNYMLEILKRPKLSAVQAGLLLLQCKHIINCKSSNDGSRQQGGGSSNSNHSNSVATGDADYSEWILCSQIVSLAEELGLGLDCNDWKLPKWERGLRKRLAWAVYLEDKWLSLKLARPSHINESNWMVLPLYDQDFPEKHGDGDLKEGSSDIDNGKKIFIHLIELSKILSDILNQFYSMKAMKEITEIDQVLKLAKPLQLRLRDWFRSLPIELQMSSVQPRKLCSNGFLQLAYFATELTLHRKITTIIFNQTKAGNPPSPELVGVCRSAAKTRLMASIEFVRDLKQEHIHSFWHCSATSNFTLIGTFAAILLMSSSTKEETDFYRDQILNYRWILKISSKGFDQAAEALADLDLVLTNIPGLIYDNINVPSLLPNVSDSLSSIQHFQMSHSPAGASPPQNSTSTITTTTTATATTQQRIRAPIRESPLSSPQNMYTPPLNNNNNNNSNVGNSNKGSPMSNAQGLSPKNKNMSGTTSKSPVKSPELTK
Protein: Signal-induced proliferation-associated 1-like protein 2 (SIPA1-like protein 2) (Q9P2F8)
Organism: Homo sapiens (Human)
Interaction partners:
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
Sequence:
MSDPRQSQEEKHKLGRASSKFKDPPRIMQSDDYFARKFKAINGNMGPTTSLNASNSNETGGGGPANGTPAVPKMGVRARVSEWPPKKDCSKELTCKALWESRSQTSYESITSVLQNGQSDQSEGQQDEQLDLDFVEAKYTIGDIFVHSPQRGLHPIRQRSNSDVTISDIDAEDVLDQNAVNPNTGAALHREYGSTSSIDRQGLSGENFFAMLRGYRVENYDHKAMVPFGFPEFFRCDPAISPSLHAAAQISRGEFVRISGLDYVDSALLMGRDRDKPFKRRLKSESVETSLFRKLRTVKSEHETFKFTSELEESRLERGIRPWNCQRCFAHYDVQSILFNINEAMATRANVGKRKNITTGASAASQTQMPTGQTGNCESPLGSKEDLNSKENLDADEGDGKSNDLVLSCPYFRNETGGEGDRRIALSRANSSSFSSGESCSFESSLSSHCTNAGVSVLEVPRENQPIHREKVKRYIIEHIDLGAYYYRKFFYGKEHQNYFGIDENLGPVAVSIRREKVEDAKEKEGSQFNYRVAFRTSELTTLRGAILEDAIPSTARHGTARGLPLKEVLEYVIPELSIQCLRQASNSPKVSEQLLKLDEQGLSFQHKIGILYCKAGQSTEEEMYNNETAGPAFEEFLDLLGQRVRLKGFSKYRAQLDNKTDSTGTHSLYTTYKDYELMFHVSTLLPYMPNNRQQLLRKRHIGNDIVTIVFQEPGALPFTPKSIRSHFQHVFVIVKVHNPCTENVCYSVGVSRSKDVPPFGPPIPKGVTFPKSAVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAENFVTTATVDTSVKFSFITLGAKKKEKVKPRKDAHLFSIGAIMWHVIARDFGQSADIECLLGISNEFIMLIEKDSKNVVFNCSCRDVIGWTSGLVSIKVFYERGECVLLSSVDNCAEDIREIVQRLVIVTRGCETVEMTLRRNGLGQLGFHVNFEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSVTVKVVIIQPHDDGSPRRGCSELCRIPMVEYKLDSEGTPCEYKTPFRRNTTWHRVPTPALQPLSRASPIPGTPDRLPCQQLLQQAQAAIPRSTSFDRKLPDGTRSSPSNQSSSSDPGPGGSGPWRPQVGYDGCQSPLLLEHQGSGPLECDGAREREDTMEASRHPETKWHGPPSKVLGSYKERALQKDGSCKDSPNKLSHIGDKSCSSHSSSNTLSSNTSSNSDDKHFGSGDLMDPELLGLTYIKGASTDSGIDTAPCMPATILGPVHLAGSRSLIHSRAEQWADAADVSGPDDEPAKLYSVHGYASTISAGSAAEGSMGDLSEISSHSSGSHHSGSPSAHCSKSSGSLDSSKVYIVSHSSGQQVPGSMSKPYHRQGAVNKYVIGWKKSEGSPPPEEPEVTECPGMYSEMDVMSTATQHQTVVGDAVAETQHVLSKEDFLKLMLPDSPLVEEGRRKFSFYGNLSPRRSLYRTLSDESICSNRRGSSFGSSRSSVLDQALPNDILFSTTPPYHSTLPPRAHPAPSMGSLRNEFWFSDGSLSDKSKCADPGLMPLPDTATGLDWTHLVDAARAFEGLDSDEELGLLCHHTSYLDQRVASFCTLTDMQHGQDLEGAQELPLCVDPGSGKEFMDTTGERSPSPLTGKVNQLELILRQLQTDLRKEKQDKAVLQAEVQHLRQDNMRLQEESQTATAQLRKFTEWFFTTIDKKS
Protein: Nuclear receptor subfamily 1 group H member 3 (C9JCS0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLPPRASSPPQILPQ
Protein: Uncharacterized protein M85 (D3XDR2)
Organism: Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus)
Interaction partners:
Sequence:
METTVLVTFEQRLTTGDVGKLSRLIGAVIPIPYRHHLLGSSQVGLDAVVKDKTRDYSRMRARMREMTLTIMRRVEGNQMILGVPTHGQCYTIRNTGPVSWEKGDVLTTLPPVFSGEVTGLVSVSDWDLVLPWIVPMALATEINQRMMMLALLSLDRSHEEVRAATAQLRVVRYRDATLTLPEITIDDTVLIDMRNVCISLSMIANLSSEVTLAYVRKLALEDSNMLLMKCQEILGRRMPQVGVGAGSSGDRNDPPARSRTNYNITPTEELNKLTALFVMIRQITDVISEQPAFLVCDVSPDDKSALCIYKG
Protein: Uncharacterized protein ycf76 (ORF85) (Q32766)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MKKILFSMFYSILVGEEPDSVFLKKEGKQNQVKMIWVAPSSCAKDLTISEGTGATFLFNFHSRVSYLFPRPFLRPRNMKWTNSFS
Protein: Fgr39p (A0A1D8PF33)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MFRVTSRAALPCLRILSQLNVLSPVRSFKLPSIFSAVKRANEIDERFTKLAERPVDYKVMEIIKQIDTEPELLFQLGFFFYECKRIGITQDLVNNRKRGVLYWPIFLGNLIPLNRAFWETMHLMNKAQHSHRLNPFKINEIGLLDPKNFPPDFYKQLLTGKYNGIDFRDTKAFSMSRPQWEESKDTV
Protein: Calcium-transporting ATPase type 2C member 1 (ATPase 2C1) (EC 7.2.2.10) (ATP-dependent Ca(2+) pump PMR1) (Ca(2+)/Mn(2+)-ATPase 2C1) (Secretory pathway Ca(2+)-transporting ATPase type 1) (SPCA1) (Q64566)
Organism: Rattus norvegicus (Rat)
Function: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway (By similarity). Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (By similarity). Plays a primary role in the maintenance of Ca(2+) homeostasis in the trans-Golgi compartment with a functional impact on Golgi and post-Golgi protein sorting as well as a structural impact on cisternae morphology. Responsible for loading the Golgi stores with Ca(2+) ions in keratinocytes, contributing to keratinocyte differentiation and epidermis integrity (By similarity). Participates in Ca(2+) and Mn(2+) ions uptake into the Golgi store of hippocampal neurons and regulates protein trafficking required for neural polarity (By similarity). May also play a role in the maintenance of Ca(2+) and Mn(2+) homeostasis and signaling in the cytosol while preventing cytotoxicity (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P98194}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P98194}; Multi-pass membrane protein {ECO:0000255}. Note=During neuron differentiation, shifts from juxtanuclear Golgi position to multiple Golgi structures distributed over the neural soma with a predominance in the apical dendritic trunk. {ECO:0000250|UniProtKB:Q80XR2}.
Interaction partners:
Sequence:
MKVARFQKIPNVENETMIPVLTSKRASELAVSEVAGLLQADLQNGLNKSEVSHRRAFHGWNEFDISEDEPLWKKYISQFKNPLIMLLLASAVISVLMRQFDDAVSITVAILIVVTVAFVQEYRSEKSLEELSKLVPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVDLSIDESSLTGETTPCSKVTAPQPAATNGDLASRSNIAFMGTLVRCGKAKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVSLAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEMTVTHILTSDGLHAEVTGVGYNQFGEVIVDGDVVHGFYNPAVSRIVEAGCVCNDAVIRNNTLMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMKGAYEQVIKYCTTYNSKGQTLALTQQQRDLYQQEKAQMGSAGLRVLALASGPDLGQLTLLGLVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAIAIASRLGLYSKTSQSVSGEEVDTMEVQHLSQIVPKVAVFYRASPRHKMKIIKSLQKNGSVVAMTGDGVNDAVALKAADIGVAMGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLATLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKILVSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCSNKMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVSEIIKKVERSREKTQKNTTSTPSSFLEV
Protein: Protein kinase C-like 3 (EC 2.7.11.13) (Atypical protein kinase C-3) (aPKC3) (Q19266)
Organism: Caenorhabditis elegans
Function: Required for the normal progression of embryogenesis and viability of the organism. Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3. Required for epithelial cell polarity in the distal spermatheca. Phosphorylates serine residues of num-1. Required for the expression of antimicrobial peptide nlp-29 in response in response to fungal infection or physical injury.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9422779, ECO:0000269|PubMed:9716526}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9422779}. Note=Targeted and anchored at the apical surface (villi) of intestinal and pharyngeal cells, and in proximity with the cortical actin cytoskeleton that lies under the plasma membrane. Tightly bound to organelles/cytoskeleton in six of the seven developmental stages. Accumulation in cytoplasm is restricted to L1 larvae and adults. Colocalized with par-3 at the anterior cortex of the 1-cell embryo. {ECO:0000269|PubMed:9422779, ECO:0000269|PubMed:9716526}.
Interaction partners:
- Partitioning defective protein 6
- Partitioning defective protein 3
- Cell division control protein 42 homolog
- LGL-1
- Numb-related protein 1
- Ras-like GTP-binding protein rhoA
- Protein Scribble homolog let-413
- Actin
- RING-type domain-containing protein
- Spindle apparatus protein lin-5
Sequence:
MSSPTSLEEDGDIKLKTRFQGQVVVLYARPPLILDDFFALLKDACKQHKKQDITVKWIDEDGDPISIDSQMELDEAVRCLNSSQEAELNIHVFVGKPELPGLPCQGEDKTVYRRGARRWKKIYLYNGHRFQAKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHCGQALQGPNIIPMAPASGSLKGARSNTSSSTTRSGGGIDNGAFHEHEIESPGSTSHDASRAMNGNGSSKWAVSLNDFRLLTVIGRGSYAKVVQAEHVSTRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSCFQTESRLFFVIEFVPGGDLMFHMQQQRKLPEEHARFYSGEIILALHFLHSRGIIYRDLKLDNVLIDAEGHIKLTDYGMCKENIKDGDLTSTFCGTPNYIAPEILRGDEYGFSVDWWALGVLMFEMMAGRSPFDIVGMQNSEENTEDYLFQIILERQIRIPRSLSVRASGILKGFLNKDPTERLGCKLDINEGLRDMKEHQFFRGFIDWEALEQKAVAPPYHPAVESDRDLTHFDHQFTDELPQLSPDNPDVIARIDQSEFDGFEYVNPLQMSREDSV
Protein: Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 2.1.3.15) (P0A9Q5)
Organism: Escherichia coli (strain K12)
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Subcellular location: Cytoplasm.
Interaction partners:
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- Biotin carboxylase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Malonyl CoA-acyl carrier protein transacylase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Dihydrofolate synthase/folylpolyglutamate synthase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Phosphate acetyltransferase
Sequence:
MSWIERIKSNITPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMTARNRLHSLLDEGSLVELGSELEPKDVLKFRDSKKYKDRLASAQKETGEKDALVVMKGTLYGMPVVAAAFEFAFMGGSMGSVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALAKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPPGFQRSEFLIEKGAIDMIVRRPEMRLKLASILAKLMNLPAPNPEAPREGVVVPPVPDQEPEA
Protein: 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC 3.1.2.4) (3-hydroxyisobutyryl-coenzyme A hydrolase) (HIB-CoA hydrolase) (HIBYL-CoA-H) (Q6NVY1)
Organism: Homo sapiens (Human)
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS35
- Large ribosomal subunit protein mL46
- Peroxisomal bifunctional enzyme
- Small ribosomal subunit protein uS10m
Sequence:
MGQREMWRLMSRFNAFKRTNTILHHLRMSKHTDAAEEVLLEKKGCTGVITLNRPKFLNALTLNMIRQIYPQLKKWEQDPETFLIIIKGAGGKAFCAGGDIRVISEAEKAKQKIAPVFFREEYMLNNAVGSCQKPYVALIHGITMGGGVGLSVHGQFRVATEKCLFAMPETAIGLFPDVGGGYFLPRLQGKLGYFLALTGFRLKGRDVYRAGIATHFVDSEKLAMLEEDLLALKSPSKENIASVLENYHTESKIDRDKSFILEEHMDKINSCFSANTVEEIIENLQQDGSSFALEQLKVINKMSPTSLKITLRQLMEGSSKTLQEVLTMEYRLSQACMRGHDFHEGVRAVLIDKDQSPKWKPADLKEVTEEDLNNHFKSLGSSDLKF
Protein: Heptose kinase (G3XD48)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Lipopolysaccharide kinase
- Serine/threonine protein kinase
- UDP-glucose:
- Lipopolysaccharide core heptose
- lipopolysaccharide heptosyltransferase II
- Lipopolysaccharide heptosyltransferase 1
- Probable carbamoyl transferase
- Uncharacterized protein
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Small ribosomal subunit protein uS3
Sequence:
MAGWTLEPDYRHLAADFGSLDSVFALEGERLTRDPLSEVIRIERDGVRYYVKRYRSAGKGLRRYLARPRIKAEWQNLKRFEKWGIPTAEVVAWGLERKAGAFQRGAMITRELPGTEDLSVLACNRDPRLKDPRWVDGVSRQIAKATRLMHDQHFTHNDLKWRNLLVDDQPLVYFIDCPNGAFWWSFMLRYRITKDLACLDKVAKYHLSRTQRLRFYLQYRRRRHLNESDKKRIRQVVAFFEGRE
Protein: Protein phosphatase 2A catalytic subunit B (EC 3.1.3.16) (PP2A-C2) (Q54RD6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay. The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells where it regulates F-actin dynamics and signal relay by controlling the activation of rasC and the downstream target of rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20493808}. Note=The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells (PubMed:20493808). Membrane localization of the Sca1 complex is regulated by scaA phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
Interaction partners:
- Protein phosphatase 2A scaffold subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Uncharacterized protein
- Suppressor of Mek1
- TAP42-like family protein
- Ras guanine nucleotide exchange factor H
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase qkgA
Sequence:
MNTSTFNLDHCIEKLQKCEILPESTIKEITDKMKELLISESNVQEIRSPVTVVGDVHGQFYDVLEIFKIGGQCPDTNYLFLGDYVDRGYHSVETISLLTCLKLRYPSRITLLRGNHESRQITQVYGFYGECMRKYGNPTVWKYFTEMFDYLSVAAIIDEAIYCVHGGLSPSALSIDQIKVLDRFQEVPNEGALSDILWSDPDPDREGFVESQRGAGYSYGKDVTLRFLQNNKMQHIIRAHQLCMDGYQTLFDNKLSTVWSAPNYCNRCGNMASIVEVNEKLERYFNTYAAAPQSLSNKPTLDTNKELPDYFL
Protein: ATP-sensitive inward rectifier potassium channel 10 (ATP-dependent inwardly rectifying potassium channel Kir4.1) (Inward rectifier K(+) channel Kir1.2) (Potassium channel, inwardly rectifying subfamily J member 10) (P78508)
Organism: Homo sapiens (Human)
Function: May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules.
Subcellular location: Membrane {ECO:0000269|PubMed:24561201}; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:24561201}. Note=In kidney distal convoluted tubules, located in the basolateral membrane where it colocalizes with KCNJ16. {ECO:0000269|PubMed:24561201}.
Interaction partners:
- Inward rectifier potassium channel 16
- Pendrin
- Dystrophin
- Caveolin-1
- Forkhead box protein I1
- Excitatory amino acid transporter 2
- Inward rectifier potassium channel 4
- Dystroglycan 1
- Gap junction beta-2 protein
- Hepatic and glial cell adhesion molecule
Sequence:
MTSVAKVYYSQTTQTESRPLMGPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELDPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV
Protein: Interferon regulatory factor 2-binding protein 1 (IRF-2-binding protein 1) (IRF-2BP1) (Probable E3 ubiquitin-protein ligase IRF2BP1) (EC 2.3.2.27) (Probable RING-type E3 ubiquitin transferase IRF2BP1) (Q8IU81)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12799427}.
Interaction partners:
- Interferon regulatory factor 2
- Interferon regulatory factor 2-binding protein 2
- Probable E3 ubiquitin-protein ligase IRF2BPL
- Transcription cofactor vestigial-like protein 4
- TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
Sequence:
MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPPALKHPATKDLAAAAAQGPQLPPPQAQPQPSGTGGGVSGQDRYDRATSSGRLPLPSPALEYTLGSRLANGLGREEAVAEGARRALLGSMPGLMPPGLLAAAVSGLGSRGLTLAPGLSPARPLFGSDFEKEKQQRNADCLAELNEAMRGRAEEWHGRPKAVREQLLALSACAPFNVRFKKDHGLVGRVFAFDATARPPGYEFELKLFTEYPCGSGNVYAGVLAVARQMFHDALREPGKALASSGFKYLEYERRHGSGEWRQLGELLTDGVRSFREPAPAEALPQQYPEPAPAALCGPPPRAPSRNLAPTPRRRKASPEPEGEAAGKMTTEEQQQRHWVAPGGPYSAETPGVPSPIAALKNVAEALGHSPKDPGGGGGPVRAGGASPAASSTAQPPTQHRLVARNGEAEVSPTAGAEAVSGGGSGTGATPGAPLCCTLCRERLEDTHFVQCPSVPGHKFCFPCSREFIKAQGPAGEVYCPSGDKCPLVGSSVPWAFMQGEIATILAGDIKVKKERDP
Protein: Serine/threonine-protein kinase RIO1 (EC 2.7.11.1) (Q9VTL5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein LTV1 homolog
- RNA-binding protein NOB1
- Pre-rRNA-processing protein TSR1 homolog
- Serine/threonine-protein kinase RIO2
- Protein arginine N-methyltransferase 5
- Protein valois
- Bystin
- Small ribosomal subunit protein uS5
- Probable RNA-binding protein EIF1AD
- U3 small nucleolar ribonucleoprotein protein MPP10
Sequence:
MNNDSHKYSDAEEDEEDLRSSEWTNDFKNLTLKHEIFKDIKLTPKEDCDDLAQVIATANEEDEPEDEEPEEYDEDDYDDIGDDYDTYEEAYTGFNKLHVQPQLTNASGGGSGGGAGGASGGSQRVSSYQPNEKLLRRYSARINVEKYDPTTNMSAQAANRLVNFDRRDRTQVRDKHDRATAEQVMDPRTRMILFKLLNRGMIQEINGCISTGKEANVYHAVSKNGEEEFAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRKRAVATMTVKELFDFITDQTITTENMEECLERISERIKDRDFDAISAQEKIDEAVWQNTYIPKRLDEVRHFERDVAKAKQGVQQNLIYGKITGLTSDLDVQQKPDVLQSSTAKEDDGSEAQTSGSEDEDNSQDNDNDEDAKKFKNSARPREESPESKKARKKAVKDAKAEQRKVKVKKHVKKRKEKMGSMKK