wanglab/gogpt-training-data huggingface dataset:
Protein: Kinetochore protein mis13 (NMS complex subunit mis13) (Q9UUB5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Required for correct segregation of chromosomes and for maintaining the inner centromere structure.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Kinetochore protein mis14
- Kinetochore protein spc24
- Kinetochore protein spc25
- Outer kinetochore KNL1 complex subunit spc7
- Kinetochore protein nuf2
- Inner kinetochore subunit mal2
- Kinetochore protein ndc80
- Inner kinetochore subunit mis15
- Inner kinetochore subunit cnl2
- Centromere protein mis12
Sequence:
MKRKPEEQEGFVFVRKGKEKAGSKRRKSSVEDDPDTSQTDGLVELPVSDTPIVKRNKELRKGKGRRSSLDQRGKRASSIGTGFEALPHADVPSHEYYRHISKDLSEPLRIKQLLLWASSKALEEQRKKYGETEEASEAAIARSIVQEVLNELLANKVSVSWYQRPPDAVIPNKPHPQNLKNAQLVDELSAKLTQLHNEEAAWRAVAANSVSSDKSILSFKKAVESIDSKQDLDKQDSPLPPDDAPELPNISKLKPKFHTLLDMLAENIHTLHSLTNAGPEVRSSYGRLAAQDFIAHRKSLLSFSKYVDTMNLLRLLSEASYKSSSNESV
Protein: Thioredoxin-related transmembrane protein 2 (Cell proliferation-inducing gene 26 protein) (Thioredoxin domain-containing protein 14) (Q9Y320)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:31735293}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:31735293}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria. {ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:31735293}.
Interaction partners:
- Thioredoxin-related transmembrane protein 1
- Calnexin
Sequence:
MAVLAPLIALVYSVPRLSRWLAQPYYLLSALLSAAFLLVRKLPPLCHGLPTQREDGNPCDFDWREVEILMFLSAIVMMKNRRSITVEQHIGNIFMFSKVANTILFFRLDIRMGLLYITLCIVFLMTCKPPLYMGPEYIKYFNDKTIDEELERDKRVTWIVEFFANWSNDCQSFAPIYADLSLKYNCTGLNFGKVDVGRYTDVSTRYKVSTSPLTKQLPTLILFQGGKEAMRRPQIDKKGRAVSWTFSEENVIREFNLNELYQRAKKLSKAGDNIPEEQPVASTPTTVSDGENKKDK
Protein: Transferrin (O97355)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMSPHKTHTWLPLAVAALLLILGPQSSLAEEPIYRLCVPQIYLAECQQLLADPSEAGIRMECVAGRDRVDCLELIEQRKADVLATEPEDMYIAYHRKNEDYRVISEIRTQQDKNAAFRYEGIILVKKDSPIRTLQQLRGAKSCHTGFGRNVGYKIPITKLKNTHVLKVSADPQISATERELKSLSEFFTQSCLVGTYSTHPETDRLLKKKYANLCALCEKPEQCNYPDKFSGYDGAIRCLDKGQGEVAFSKVQYIKKYFGLPGAGPDAPPAEGNPENFEYLCEDGTRRPVTGPACSWAQRPWSGYISNEQAVHNSEQLHQLQSRLERFFANGLQAQNKDAAAHLLIQPNAVYHSKDAAIDPKVYLERAGYKDVIERDGSAIRKIRLCAQNDDEFAKCQALHQAAYARDARPELECVQSTDCVVALTKKEADLTIVRATGYADARSNQLQPIVYEQRAQDDVLVAVAAPGVTREALQKASIKFNENCERSRAAAALLNKRRGLDACRVSSSDDGEVQIVPASELEKHKDAQLVCPSLERRPVTDFRDCNVDVQLPRAIFIRSDTTSVEQETVKHLFSLISDKFGARGKLVDVFALFGEFQKGKKNVYFNDKAVQLTTELKNEIQNEQIYTDLQCNANKIAKQ
Protein: Zyxin (A5H447)
Organism: Xenopus laevis (African clawed frog)
Function: Adhesion plaque protein. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). Suppresses the transcription-repressing activity of hesx1/anf1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cell junction, focal adhesion {ECO:0000250}. Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of hesx1. {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}.
Interaction partners:
Sequence:
MDPAAPATRMTSSFTINISTPSFYNPPKKFAPVVPPKPKINPFKAPEEPQSLVPQENSAGPGLHQAFVGKVGEMPPGVDHDDFVLPPPPPSEESISPPSSSFPPPPPSFGDEGLGSPSGGSFPPPPPPEFSEPFPPPIEEFFPSPPPLEECVSDTQDLPVPVPPPPPPPLPSPPAAPPPKPSAPCEAPKPAPVFPKSSPPPAFPKPEPPSVAPKAASSIFIPKPSAPMAVAPKPLAPPPVAAKPSGPVSFAPPSPAPHTFSPDPSAPAHTFSPKTVTFSPKSAPHTFMPKPSAPVTYPQKTTEPPAEASQSSPKVTPAAKHEAPPPTVPSGGRAPGFSFAQQRERPRVLEKPRANLQGSEPEHEPTVEVQVERTRSLGPQTESGRSPGAQSTGGKDMKPLPEGLRSQKPMSDGIHRTGGQHSGHKVTGQQDQTLGSQGLNMKEVEELEMLTQQLMREMDKPPTAEAHSMELCGFCGRGLSRTETVVRAGEHLYHVACFTCSRCDQQLQGQQYYESAGKPLCDECYQDTLECCAVCDKKITERLLKAIGKSYHPSCFTCAVCKCSLQGEPFIVDDNKLPHCVNDYHRRYAPRCCVCGDPIAPEPGRDETVRVVALEKNFHMMCYKCEDCGCPLSIEADDAGCFPLDGHVLCKKCHTVRARAALG
Protein: CUB-like domain-containing protein (V6CJ59)
Organism: Caenorhabditis elegans
Interaction partners:
- CUB-like domain-containing protein
- VWFA domain-containing protein
- CUB-like domain-containing protein
Sequence:
MIYSSTMSATPLIISLGLLVGVTAALDCTQIPNNAIIPLSYTTIPAGATGLVEIPPNFNCVYNVKVPKMVYARVRLENGLKGYNDLITVQDQQGTYTRVSSRSPSVLNFYVFPNTTTTFQVVTKSVDMHSSFRMIVFYQPMYTETVTHLGNPDMKYFMLNDLQENSYKTPQTIISNEKISVSMASSGWDADIFENYFIIKGDLNNTKSVSRLSRFVGQGYISTGSSLTVVGLDNRVSESSVTFVPFSQAQQYDSYTTFSTYFEANQLKIDATVGNKKKKAVTVISMKNIVTVLDVQRTNSPNCVLKAVQSPPTPSSEIYLDFTTVTDFPRNITHKSFCIIAENCGATFNLVSPFPLR
Protein: UDP-glucuronate decarboxylase (EC 4.1.1.35) (C0Z2I3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}.
Interaction partners:
Sequence:
MASELTNRRHEIEQPEAESYYPKPIKPWFVAIRPIRYMLREQRLVFVLVGIAIATLGFTIFSKSSNHQPIPYDVDPLSGYGMRSESSYLPATIHKKPSIEYMSRIGSAGGKIPLGLKRKVLRVVVTGGAGFVGSHLVDRLMARGDNVIVVDNFFTGRKENVMHHFNNPNFEMIRHDVVEPILLEVDQIYHLACPASPVHYKFNPVKTIKTNVVGTLNMLGLAKRVGARFLLTSTSEVYGDPLQHPQVETYWGNVNPIGVRSCYDEGKRTAETLTMDYHRGANVEVRIARIFNTYGPRMCIDDGRVVSNFVAQALRKEPLTVYGDGKQTRSFQFVSDLVEGLMRLMEGEHVGPFNLGNPGEFTMLELAKWMVGEQVVQETIDPNAKIEFRPNTEDDPHKRKPDITKAKELLGWEPKVALRQGLPLMVKDFRQRVFGDQKQDSSTTSSSTE
Protein: Capricious, isoform D (Q0E8F0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRRRAITMSLAPHLGQAFSLCLCLCLCLVLATLPVALGLANCPNGCECDDDTLMVNCGEGTLDVLPIALNPAIQRLVIKNNKLKTIDSSMQFYAQLTFLDLSFNDMLTIPERSFAYHAKLQELHLDHNKIGQVSNKTFLGLSTISVLNLRGNLIAELEYRTFSPMVKLAELNLGQNRISHIDPHALDGLDNLRVLYLDDNTLTTVPGELTFQALHSLAELYLGTNSFMTIPGGAFQDLKGLTRLDLRGAGLHNISGDALKGLVSLRFLDLSDNRLPAIPTAAFQRLGRLEQLNIGQNDFEVISSGAFSGLRELRHLELTGAQRLRRVESGAFSGNTNLEHLNLSSNKQLNELSSIALGGLPHLSTVVLKANQLSSLDEGLVPWADLQTLDLSENPFECDCRLLWLRHLLVSRNASGQYAPVICAYPTALRDLPLAHLAEPLLGCAHGAASKQAIIGILVVACAALITTLALVLYTCRHRIREMLKGHSALGRKEREYQKTFSDEEYMSRPPPGGGGVHPAAGGYPYIAGNSRMIPVTELXLEAPPPPQLRGRGGGGGASTASGAVQQLQVPSAVDQASNSFAQLSHIHYMTNNGQQQQAQQQQSTSKMHHSQQDMRLLACNGGKPLNATSLPRHRPPVVQESTLSHYSQPLANGIRLTQDHFNHNQNQSHNQHYGGVYAKPCDAMSEPGYIHNNSHYSLPLDHDLPPSPTPTPPPPALPLRNGVGMALIHGNTTGRRSFNNNNNVSTLSNNNHHGIGGGVGVAVGGTVGNNNGSLRRYH
Protein: RB binding protein 4, chromatin remodeling factor (H0YF10)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XNPCIIATKTPSSDVLVFDYTKHPSKPGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQM
Protein: Uncharacterized protein Rv0875c (P9WKR7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0876c
- Uncharacterized protein Rv0877
- Integral membrane protein
- Uncharacterized protein Rv0048c
- Probable conserved transmembrane protein alanine and leucine rich
- Sensor-type histidine kinase PrrB
- HTH-type transcriptional repressor Rv1353c
- Uncharacterized protein Rv2079
- Possible transcriptional regulatory protein
- DNA 3'-5' helicase
Sequence:
MKRGVATLPVILVILLSVAAGAGAWLLVRGHGPQQPEISAYSHGHLTRVGPYLYCNVVDLDDCQTPQAQGELPVSERYPVQLSVPEVISRAPWRLLQVYQDPANTTSTLFRPDTRLAVTIPTVDPQRGRLTGIVVQLLTLVVDHSGELRDVPHAEWSVRLIF
Protein: Gap junction epsilon-1 protein (Connexin-23) (Cx23) (Q9CX92)
Organism: Mus musculus (Mouse)
Function: Mediates calcium-independent ATP release, suggesting activity as a hemichannel. Does not form functional gap junctions. May play a non-essential role in eye lens development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18849090}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gap junction beta-4 protein
- Gap junction delta-2 protein
Sequence:
MSLNYIKNFYEGCVKPPTVIGQFHTLFFGSVRMFFLGVLGFAVYGNEALHFSCDPDKREINLFCYNQFRPITPQVFWALQLVIVLLPGAIFHLYAACKSINQDCILQKPVYTVIYVLSVLLRISLEVFAFWLQIHLFGFQVKPIYLCDTESLGKKPNILKCMVPEHFEKTIFLIAMYTFTVITMVLCVAEVFEIIFRRSCFLFKR
Protein: Proton myo-inositol cotransporter hmit-1.3 (H(+)-myo-inositol cotransporter hmit-1.3) (H(+)-myo-inositol symporter hmit-1.3) (Q21455)
Organism: Caenorhabditis elegans
Function: H(+)-myo-inositol cotransporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21679696}; Multi-pass membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:21679696}. Note=Localizes to the endfoot region of glial cells where the cilia of sensory neurons are embedded. {ECO:0000269|PubMed:21679696}.
Interaction partners:
Sequence:
MVQVAPVAAGAGSGQTRPSSDPKTGWFVYMLAFSAVIGGFLFGYDTGIVSAAMLYVPNASGIKPLDSVWQEIIVSITPGVAAIGSLCSGPGSDFLGRKKIIIGASVTFTIGAIICAAAWTKIILLIGRILLGLAIGFASMIVPIYVSEASPSHIRGKLVTGFQLMITVGLVIANIIGGAFSYVDPDQVGWRLMFAFAAVPAIIQFVCFLFLPESPRWLYEHGRTVEAREVLTRIYNGHTEWVDYEINEISFSYEEELRAKAEHAGNGPTIIRILKTPHVRKAMIIGSLLQMFQQLSGINTVMYYTGNIIRSAGVKDNHTTIWISVGTSAINFLGTFIPIALVERVGRRVLLLVSMIGVILFLIAMGVSFLLINNDSLRTFDQQNYTLNYNPSVKHAAKCLKYSNCDFCVTDENCGFCESKVAKKGYCLPFPSDDSSDYSATGICEFSNLTNNGTDFEWEDTYCHTKFTVLPIIIMVFYLLSFSAGYAPLPWVLNAEFYPLWARSTAVSVSTACNWIFNLIVSLTFLSLSQAATKYGTFFIYCGCTMVALVFVFFFVPETKGYSIDEVEMLFMTKEERRKAQKVLDESKEGKHRNSVAMSFDTKF
Protein: Tea1p (A0A1D8PK74)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitochondrial outer membrane protein OM14 C-terminal domain-containing protein
- Uncharacterized protein
Sequence:
MSINSSTSTTNKRKRKNPSTTTPPPPTTPHPAPPRTEKRISCQRCRTRKIKCNYELPCFNCKRDGSQCIQPIDMRSKRLKATEVITLQKKLDLMIKFINDCKKLPNAEAKQQFISQTNLDELINDGSIVLDNGDSTNGDGDVLHVANHDEDVTHNNSAIYGPTSVYDDSLMHNHKPNTKHKQITIDKSNSNDDNNSKGEINKDENRNVGNNSSINYNNNINTLNNRIDNNSSNLINVINKMNKDPDILKCIQLFFIWQYPDHNMFIFREAFLIDFFNPKKNMLYCSKTLILSICSLGAKMSTEETIYNRSKEFYQESKYLLLNSLHQPSITSLQSFMLLAFYDICNGQNSSGWMLSGCAMRMGYDLGFQLNPELWFVKSKGENNTINNLSKLDVEIRSRIYWGCYMADHFISLLLGRPSILKISDASIPVTSDLPDLEWIDDFTYNGYIKKKKLHKRSKSKHRKDEHEDDKDDLKSPGKHKHQEVSYISDPLNQIINLINISDNILNDIFTKTDEEQPQEHQQEQQQQQQQQQQKSNEDLNLKSRWEKLSQYNSQIMAWKKNLPKDLRWNRTKLGKTGENPTYSGIRYYYYILLLCLNRPFVGIDQDNHNNHDTNNNDNNDNNDSDDSDDNLSPLSICLNAIDDLYESINRFQKKHGYRGGSIFIVYSSILSISILLLTNSRIQLASEQKNRLHFFMDVLYGCSKTWKLAEKSYNLITEKLKHLYEAGELKDVFEFIIEKKSSPSATNTSGNGLNEASGNNNNNNSQSIESNEFKLPINNKTLSKLKHNQQNTNNSLPTYDTTDTINSTSGATTTNNSTTFSMDQNLMEAPTPLSTISNGVNNNNNNGGGGGGRNSSSATDFLTDDNVDFLGGPPVLMTADLFNEDWEALFPDYIFNSKN
Protein: Uncharacterized protein C688.03c (Q9P6M2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MDKKEYCYYCFEVVAATLEHRKVRDKWNAKSWTRSIPLFVKFASGKGHDKQLRGCIGTFRARPLVTNLTYFSKQAAFCDERFRPISLGELALLECQIDLLVDFEPIDDPLDWEVGIHGVSIKFTANGIRYSSTYLPSVAAEQRWDQEETLESLIHKAGYYGSIRSLQITATRYKSLEIGCTYEEYLHNLELLG
Protein: Peroxidase 59 (Atperox P59) (EC 1.11.1.7) (ATPN) (Peroxidase N) (Q39034)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Probable pectinesterase/pectinesterase inhibitor 59
- Pathogenesis-related protein 1
- Transmembrane protein
- GDSL esterase/lipase At1g74460
- CASP-like protein 1A1
- GDSL esterase/lipase At1g28650
- Cytochrome b561 and DOMON domain-containing protein At4g17280
- GDSL esterase/lipase At2g30310
- Actin cytoskeleton-regulatory complex pan-like protein
- GDSL esterase/lipase At5g45960
Sequence:
MKTQTKVMGGHVLLTVFTLCMLCSGVRAQLSPDIYAKSCPNLVQIVRKQVAIALKAEIRMAASLIRLHFHDCFVNGCDASLLLDGADSEKLAIPNINSARGFEVIDTIKAAVENACPGVVSCADILTLAARDSVVLSGGPGWRVALGRKDGLVANQNSANNLPSPFEPLDAIIAKFVAVNLNITDVVALSGAHTFGQAKCAVFSNRLFNFTGLGNPDATLETSLLSNLQTVCPLGGNSNITAPLDRSTTDTFDNNYFKNLLEGKGLLSSDQILFSSDLAVNTTKKLVEAYSRSQSLFFRDFTCAMIRMGNISNGASGEVRTNCRVINN
Protein: Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (P69441)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
Interaction partners:
- Protein translocase subunit SecY
- Adenylosuccinate lyase
- Nucleoside diphosphate kinase
- Adenine phosphoribosyltransferase
- Adenylosuccinate synthetase
- Fumarate hydratase class II
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL5
- Hypoxanthine phosphoribosyltransferase
- Translation initiation factor IF-1
Sequence:
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVTDELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIGYYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG
Protein: Papillosin (P86416)
Organism: Halocynthia papillosa (Red sea-squirt)
Function: Has strong antibacterial activity against the Gram-positive bacteria M.luteus, S.aureus, B.megaterium, A.viridans and E.faecalis, and against the Gram-negative bacteria K.pneumoniae, E.coli DH5alpha, S.typhimurium, P.aeruginosa and E.aerogenes. Lacks hemolytic activity against sheep erythrocytes.
Interaction partners:
Sequence:
GFWKKVGSAAWGGVKAAAKGAAVGGLNALAKHIQ
Protein: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 2.3.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein biotinylase sirtuin-4) (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 2.3.1.286) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4) (Q9Y6E7)
Organism: Homo sapiens (Human)
Function: Acts as NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels. Down-regulates insulin secretion.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:17715127}.
Interaction partners:
- Nicotinamide phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Glutamate dehydrogenase 1, mitochondrial
- Glutamine-dependent NAD
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- NAD
- Nicotinamide N-methyltransferase
- Purine nucleoside phosphorylase
Sequence:
MKMSFALTFRSAKGRWIANPSQPCSKASIGLFVPASPPLDPEKVKELQRFITLSKRLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHGDFVRSAPIRQRYWARNFVGWPQFSSHQPNPAHWALSTWEKLGKLYWLVTQNVDALHTKAGSRRLTELHGCMDRVLCLDCGEQTPRGVLQERFQVLNPTWSAEAHGLAPDGDVFLSEEQVRSFQVPTCVQCGGHLKPDVVFFGDTVNPDKVDFVHKRVKEADSLLVVGSSLQVYSGYRFILTAWEKKLPIAILNIGPTRSDDLACLKLNSRCGELLPLIDPC
Protein: Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) (Q32PX2)
Organism: Rattus norvegicus (Rat)
Function: Required for assembly and stability of the aminoacyl-tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R010}. Nucleus {ECO:0000250|UniProtKB:Q8R010}. Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q8R010}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Lysine--tRNA ligase
- Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1
- Aspartate--tRNA ligase, cytoplasmic
- Eukaryotic translation elongation factor 1 epsilon-1
- Leucine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MPMYQVKPYHGGSAPLRVELPTCMYRLPNVHSKTTSPATDAGHVQEPSEPSLRALESRQDDILKRLYELKAAVDGLSKMIHTPDADLDVTNILQADEPTTLTTNALDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCERYRVLSTVHTHSSVKNVPENLLKCFGEQARKQSRHEYQLGFTLIWKNVPKTQMKFSVQTMCPIEGEGNIARFLFSLFGQKHNAVHLTLIDSWVDIAMFQLREGSSKEKAAVFRSMNSALGKSPWLVGNELTVADVVLWSVLQQTGGSSGAAPTNVQRWLKSCENLAPFSTALQLLK
Protein: Matrix protein (Membrane protein) (P16629)
Organism: Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5)
Function: The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MPSISIPADPTNPRQSIKAFPIVINSDGGEKGRLVKQLRTTYLNDLDTHEPLVTFINTYGFIYEQDRGNTIVGEDQLGKKREAVTAAMVTLGCGPNLPSLGNVLGQLREFQVTVRKTSSKAEEMVFEIVKYPRIFRGHTLIQKGLVCVSAEKFVKSPGKIQSGMDYLFIPTFLSVTYCPAAIKFQVPGPMLKMRSRYTQSLQLELMIRILCKPDSPLMKVHTPDKEGRGCLVSVWLHVCNIFKSGNKNGSEWQEYWMRKCANMQLEVSIADMWGPTIIIHARGHIPKSAKLFFGKGGWSCHPLHEVVPSVTKTLWSVGCEITKAKAIIQESSISLLVETTDIISPKVKISSKHRRFVKSNWGLFKKTKSLPNLTELE
Protein: Amino acid transporter (E7EV13)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
Sequence:
MSIDHEQPWQQPVPAGERPAAGPGGLAAAAAGKPAAESTAHAPAPADHDPRARAALPAPKRLHSADGQRRGHWGQPGLCPAPISAHLPPDQVLLFSWRASDEDAADAGVTSHCLQPGHRNMFPPNLVEACFKQFKTQYSTRVVTRTMVRTENGSEPGASMPPPFSVENGTSFLENVTRALGTLQEMLSFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGIVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESAM
Protein: F-box/kelch-repeat protein At3g06240 (Q8GXC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- T29M8.11
- At1g27330
- Large ribosomal subunit protein uL1c
- AT4g14420/dl3250c
- Probable pectinesterase/pectinesterase inhibitor 58
- Membrane protein of ER body 1
- S-protein homolog 12
- AP-5 complex subunit zeta-1
- Glycoprotein membrane GPI-anchored
- Autophagy-related protein 8b
Sequence:
MKAIQLLWEAIMEATKRERRREDDDGEKASPESLVLPPEIITEILLRLPAKSIGRFRCVSKLFCTLSSDPGFAKIHLDLILRNESVRSLHRKLIVSSHNLYSLDFNSIGDGIRDLAAVEHNYPLKDDPSIFSEMIRNYVGDHLYDDRRVMLKLNAKSYRRNWVEIVGSSNGLVCISPGEGAVFLYNPTTGDSKRLPENFRPKSVEYERDNFQTYGFGFDGLTDDYKLVKLVATSEDILDASVYSLKADSWRRICNLNYEHNDGSYTSGVHFNGAIHWVFTESRHNQRVVVAFDIQTEEFREMPVPDEAEDCSHRFSNFVVGSLNGRLCVVNSCYDVHDDIWVMSEYGEAKSWSRIRINLLYRSMKPLCSTKNDEEVLLELDGDLVLYNFETNASSNLGICGVKLSDGFEANTYVESLISPNSYGIES
Protein: GEO10302p1 (TA01267p) (Q9VB29)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO10195p1
- trypsin
Sequence:
MKLLIWLCLLGFLASAYGIFLDKITGRGDSSGNGLLDDIFGLEDSDNSSHNKTSQHALPASGIFTPVKVAVDVIQNIWDEFSKGVLGLMGSFGTGDDGGESPPSGNTAPVTTESSLPSQETTTTRTTPFTTTESRTESVLETTTTDSSTSTLPP
Protein: Protein DipZ (P9WG63)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Immunogenic protein MPT70
- Possible cytochrome C-type biogenesis protein CcsA
- Peptide methionine sulfoxide reductase MsrA
- Alkyl hydroperoxide reductase C
- Probable conserved integral membrane protein
- Uncharacterized protein
- Cell surface glycolipoprotein MPT83
- Dihydrolipoyl dehydrogenase
- peptide-methionine
- Probable arsenic-transport integral membrane protein ArsC
Sequence:
MVESRRAAAAASAYASRCGIAPATSQRSLATPPTISVPSGEGRCRCHVARGAGRDPRRRLRRRRWCGRCGYHSHLTGGEFDVNRLCQQRSRERSCQLVAVPADPRPKRQRITDVLTLALVGFLGGLITGISPCILPVLPVIFFSGAQSVDAAQVAKPEGAVAVRRKRALSATLRPYRVIGGLVLSFGMVTLLGSALLSVLHLPQDAIRWAALVALVAIGAGLIFPRFEQLLEKPFSRIPQKQIVTRSNGFGLGLALGVLYVPCAGPILAAIVVAGATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAFRRRQREIRIATGSVTILLAVALVFDLPAALQRAIPDYTASLQQQISTGTEIREQLNLGGIVNAQNAQLSNCSDGAAQLESCGTAPDLKGITGWLNTPGNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEYAFEKVPGNVAKGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEGDYNVTETLVRQLLNDAKPGVKLPQPSSTTTPDLTPRAALTPETYFGVGKVVNYGGGGAYDEGSAVFDYPPSLAANSFALRGRWALDYQGATSDGNDAAIKLNYHAKDVYIVVGGTGTLTVVRDGKPATLPISGPPTTHQVVAGYRLASETLEVRPSKGLQVFSFTYG
Protein: TBC1 domain family member 23 (E9PGE5)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MGWYFRLARTEHYSQRLPAVYWDCSQKGRPFHLFRLLIQYHEPELCSYLDTKKITPDSYALNWLGSLFACYCSTEVTQAIWDGYLQQADPFFIYFLMLIILVNAKEVILTQESDSKEEVIKFLENTPSSLNIEDIEDLFSLAQYYCSKTPASFRKDNHHLFGSTLLGIKDDDADLSQALCLAISVSEILQANQLQGEGVRFFVVDCRPAEQYNAGHLSTAFHLDSDLMLQNPSEFAQSVKSLLEAQKQSIESGSIAGGEHLCFMGSGREEEDMYMNMVLAHFLQKNKEYVSIASGGFMALQQHLADINVDGPENGYGHWIASTSGSRSSINSVDGESPNGSSDRGMKSLVNKMTVALKTKSVNVREKVISFIENTSTPVDRMSFNLPWPDRSCTERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSMSDDDRKEVVNIQTWINKPDVKHHFPCKEVKESGHMFPSHLLVTATHMYCLREIVSRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGNSSASGIEILAIERYLIPNAGDATKAIKQQIMKVLDALES
Protein: Microfibril-associated glycoprotein 4 (36 kDa microfibril-associated glycoprotein) (36 kDa MAP) (P55918)
Organism: Bos taurus (Bovine)
Function: Could be involved in calcium-dependent cell adhesion or intercellular interactions. May contribute to the elastic fiber assembly and/or maintenance.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P55083}.
Interaction partners:
- Elastin
- Microfibrillar-associated protein 2
- Fibrillin-1
- Fibulin-5
- Microfibrillar-associated protein 5
Sequence:
MEALLVLPLLLLLSAGPCAPQLLGIRGDALEKSCLQLPLDCDDIYAQGYQADGVYLIYPSGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWNDYKLGFGRADGEYWLGLQNMHLLTLKQKYELRVDLEDFENNTAFAKYADFSISPNAVSAEEDGYTLYVSGFEDGGAGDSLTYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSHLSYANGINWAQWKGFYYSLKRTEMKIRRA