wanglab/gogpt-training-data huggingface dataset:
Protein: ADAM metallopeptidase domain 22 (M0R5P8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Leucine-rich glioma-inactivated protein 1
- Disks large homolog 4
- 14-3-3 protein zeta/delta
- Leucine-rich repeat LGI family, member 4
- Leucine-rich repeat LGI family, member 2.
- ADAM metallopeptidase domain 23
- Leucine-rich repeat LGI family, member 3
- Disks large homolog 2
- Potassium voltage-gated channel subfamily A member 1
- Contactin-2
Sequence:
MEAWHEIPSVETVWPRVPGWPHSSLSFSFQGGEHCYYQGQIRGNPASFVALSTCHGLHEFSTPQRNTHIQESQFHSVYKSRLLEFPLDDLPSEFQRINITAPQFTLKPRLKRRKRQLLRFPRNVEEETKYIELMIVNDHLMFKKHRLSVVYTNTYAKSVVNMADVIYKDQLKTRIVLVAMETWAADNKFAISENPLVTLREFMKYRRDFIKEKADAVHLFSGSQFESSRSGAAYIGGICSLLRGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECALEGAECCKKCTLTQDSQCSDGLCCKKCKFQPLGTVCREAVNDCDIREICSGNSSQCAPNVHKMDGYSCDGTQGICFGGRCKTRDRQCKYIWGQKVTASDRYCYEKLNIEGTEKGNCGKDKDTWTQCNKRDVLCGFLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPMASFNFSTCLSNKAGTVCSGNGVCSNELKCVCNRHWTGADCGTHFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKQLPQGDYVKKPGDGDSFYSDFPPGGSADSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGSEQSSKSKTCILGTYKKVFFPISSSALLPSPSSSTGSIASSRKYPYPMPPLPDEEKTVNRQSARVYSNSARFILGCCWHLELTFCPFLRFLFVWFF
Protein: Inorganic phosphate transporter PHO84 (P25297)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity transporter for external inorganic phosphate. Is not an essential protein, since a constitutive, low affinity pI transporter exists in yeast.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10518922, ECO:0000269|PubMed:11779791, ECO:0000269|PubMed:19348508, ECO:0000269|PubMed:2038328}; Multi-pass membrane protein {ECO:0000255}. Vacuole {ECO:0000269|PubMed:11779791}. Note=Accumulates at the plasma membrane in cells starved for phosphate (PubMed:11779791). At high external phosphate concentrations, removed from the cell membrane via endocytosis and internalized in PKA/TPK3-dependent manner (PubMed:19348508). {ECO:0000269|PubMed:11779791, ECO:0000269|PubMed:19348508}.
Interaction partners:
- Low-affinity phosphate transporter PHO90
- Inorganic phosphate transporter PHO87
- Low-affinity phosphate transporter PHO91
- Phosphate permease PHO89
- Putative cyclin-dependent kinase inhibitor SPL2
- Acid phosphatase PHO11
- Phosphate system positive regulatory protein PHO81
- Vacuolar transporter chaperone 3 complex subunit 3
- Acid phosphatase PHO12
- Vacuolar transporter chaperone complex subunit 4
Sequence:
MSSVNKDTIHVAERSLHKEHLTEGGNMAFHNHLNDFAHIEDPLERRRLALESIDDEGFGWQQVKTISIAGVGFLTDSYDIFAINLGITMMSYVYWHGSMPGPSQTLLKVSTSVGTVIGQFGFGTLADIVGRKRIYGMELIIMIVCTILQTTVAHSPAINFVAVLTFYRIVMGIGIGGDYPLSSIITSEFATTKWRGAIMGAVFANQAWGQISGGIIALILVAAYKGELEYANSGAECDARCQKACDQMWRILIGLGTVLGLACLYFRLTIPESPRYQLDVNAKLELAAAAQEQDGEKKIHDTSDEDMAINGLERASTAVESLDNHPPKASFKDFCRHFGQWKYGKILLGTAGSWFTLDVAFYGLSLNSAVILQTIGYAGSKNVYKKLYDTAVGNLILICAGSLPGYWVSVFTVDIIGRKPIQLAGFIILTALFCVIGFAYHKLGDHGLLALYVICQFFQNFGPNTTTFIVPGECFPTRYRSTAHGISAASGKVGAIIAQTALGTLIDHNCARDGKPTNCWLPHVMEIFALFMLLGIFTTLLIPETKRKTLEEINELYHDEIDPATLNFRNKNNDIESSSPSQLQHEA
Protein: Protein COS1 (P53822)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MKENELKNEKSVDVLSFKQLESQKIVLPQDLFRSSFTWFCYEIYKSLAFRIWMLLWLPLSVWWKLSNNCIYPLIVSLLVLFLGPIFVLVICGLSRKRSLSKQLIQFCKEVTENTPSSDPHDWEVVAANLNSYLYENKAWNTKYFFFNAMVCQEAFRTTLLEPFSLKKDEAAKVKSFKDSVPYIEEALGVYFREVEKQWKLFNSEKSWSPVGLEDAKLPKEAYRFKLTWFLKRISNIFMLIPFLNFLCCIYVSRGMCLLLRTFYLGWILFMLVQGFQNMRMIVLSVKMEHKMQFLSTIINEQESGANGWDEIAKKMNRYLFEKKVWKNEEFFFDGIDCEWFFSHFFYRVLSAKKSMRALSLNVELWPYIKEAQLSCSEESLA
Protein: Ribosome-binding protein 1 (Ribosome receptor protein) (RRp) (mRRp) (Q99PL5)
Organism: Mus musculus (Mouse)
Function: Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Synaptojanin-2-binding protein
- Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial
Sequence:
MDIYDTQTLGVVVFGGFMVVSAIGIFLVSTFSMKETSYEEALANQRKEMAKTHHQKGEKKKKEKTVEKKGKTKKKEEKPNGKIPEHDLDPNVTIILKEPVRVSAVAVAPTSVHSSVGHTPIATVPAMPQEKLASSPKDRKKKEKKVAKVEPAVSSIVNSIQVLASKSAILEATPKEVPMVAVPPVGSKASSPATSSQGKKGQGAQNQAKKGEGAQNQGKKGEGAQNQAKKGEGAQNQAKKGEGAQNQGKKGEGAQNQAKKGEGGQNQAKKGEGAQNQGKKGEGAQNQGKKGEGAQNQAKKGEGAQNQAKKGEGAQNQGKKGEGAQNQSKKGEGAQNQAKKGEGGQNQAKKGEGAQNQAKKGEGAQNQAKKGEGVQNQAKKGVEGAQNQGKKGEANQNQAKKGEGGQNQTKKGEGPQNQGKKGEAAQKQDKKIEGAQNQGKKPEGTSNQGKKGEGAQNQGKKGEGAQNQSKKGEGAQNQAKKGEGGQNQAKKGEGAQNQAKKGEGAQNQAKKGEGVQNQAKKGVEGAQNQGKKGEANQNQAKKGEGGQNQTKKGEGPQNQGKKGEAAQKQDKKIEGAQNQGKKPEGTSNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGPQNQAKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKAEGVQSQSKKGEGTQNQGKKGDGNPNQGKKGEGASNQNRKTDTVANQGTKQEGVSNQVKKSEGSPNQGKKAEGAPNQGKKKDGSPSQAKKVDAAANQGKKSEMAPAQGQKASMVQSQEAPKQDAPAKKKSGSRKKGEPGPPDCDGPLFLPYKTLVSTVGSMVFSEGEAQRLIEILSEKTGVIQDTWHKATQKGDPVAILKRQLQEKEKLLATEQEDAAVAKSKLRELNKEMASEKAKAAAGEAKVKKQLVAREQEIAAVQARMQASYRDHVKEVQQLQGKIRTLQEQLENGPNTQLARLQQENSILRDALNQATSQVESKQNTELAKLRQELSKVNKELVEKSEASRQEEQQRKALEAKAATFEKQVLQLQASHKESEEALQKRLEEVTRELCRAQTSHANLRADAEKAQEQQQRVAELHSKLQSSEVEVKSKCEELSSLHGQLKEARAENSQLTERIRSIEALLEAGQAQDTQASHAEANQQQTRLKELESQVSCLEKETSELKEAMEQQKGKNNDLREKNWKAMEALALAERACEEKLRSLTQAKEESEKQLHLAEAQTKETLLALLPGLSISAHQNYAEWLQEFKEKGSELLKKPPTLEPSMDIVLKLREAEETQNSLQAECDQYRTILAETEGMLKDLQKSVEEEERVWKAKVGAAEEELHKSRVTVKHLEDIVEKLKGELESSDQVREHTSHLEAELEKHMAAASAECQNYAKEVAGLRQLLLESQSQLDEAKSEAQKQSDELALVRQQLSDMRSHVEDGDVAGSPAVPPAEQDPMKLKTQLERTEATLEAEQTRRQKLTAEFEEAQRTACRIQEELEKLRAAGPLESSGKEEITQLKERLEKEKRLTSDLGRAAIKLQELLKTTQEQLTKEKDTVKKLQEQLGKAEDGSSSKEGTSV
Protein: Kinesin-like protein (Q384B7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinesin-like protein, putative
- FG-GAP repeat protein, putative
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- FG-GAP repeat protein, putative
- Kinesin, putative
- Kinesin-like protein
- Kinesin, putative
Sequence:
MQRLAGKRQRQHEASDLVPKSAEPARSKNSRNTASEPGSGSLRHNSIGGGDMMWKRKTKELREQIVQLAALYATKERETEEVQDAIEEMVVSHEAELAGVVAGDESHRRRHVDALVHLRAREDGCHSERQRALDETVVLQQQRTELERAHDRLREDIVIQSDALEQLQREIEEQSEELLEEQRKLDAIVEHHNLMRDATYGFSGEVQEIMRELERIKVDKERVERAGKQTEILRRQLYSQCEEMKGTIRVYCRVKGGLNSESVAAGPVPDVRSGSSNPCGDPDLCLSETPREDSVSSRSTMQTTVSANPACIYASKEIGQIRRDAPVGRFIFPDGDATEKRSICVLLSRNNATSTGRQESKETFTFDRVFDGTASQEAVYADVEPLVNCAVDGYRVCVFAYGQTGSGKTYSMQGDQHDGQRCGITPRALRTVFKRREELEADGWKYQLSCYFVEIYNEVIRDLLQEASLYEPGGAAASQPNYHIIKQSNETGSTSISGVTEKRINSFEDFRRLYDIAMKNRSTAKTMINDRSSRSHCIFVLRIMGEHAGIRQRSEGSLCMVDLAGSERVHESGVQGKQFKEAVNINRSLLDLGKCISALNKSGSVAPWRNCKLTYLLQNYLGAKGGKMLMLVTVSDQEEHLTESINSLRFAKRVNQTAIGPSTKRVGNF
Protein: Free fatty acid receptor 2 (G-protein coupled receptor 43) (Leukocyte-specific STAT-induced GPCR) (Q8VCK6)
Organism: Mus musculus (Mouse)
Function: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Free fatty acid receptor 4
- Peptide YY
- G-protein coupled receptor 84
- G-protein coupled bile acid receptor 1
- Pro-neuropeptide Y
- Appetite-regulating hormone
- Olfactory receptor 51E2
- Delta-1-pyrroline-5-carboxylate synthase
- Glucose-dependent insulinotropic receptor
- Pro-glucagon
Sequence:
MTPDWHSSLILTAYILIFLTGLPANLLALRAFMGRVRQPQPAPVHILLLNLTLADLLLLLLLPFRIVEAASNFRWYLPKIVCALTGFGFYSSIYCSTWLLAGISMERYLGVAFPVQYKLSRRPLYGVIAALVAWIMSFGHCTIVIIVQYLNSTEQVGTENQITCYENFTQEQLDVVLPVRLELCLVLFFVPMAVTIFCYWRFVWIMLTQPHVGAQRRRRAVGLAVVTLLNFLVCFGPYNMSHLVGFYLRQSPSWRVEAVVFSSLNASLDPLLFYFSSSVVRRAFGKGLLLIRNPASSMLGRGAKETVEGTKMDRGGSQAEGVQSSEFVTE
Protein: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (EC 3.2.2.6) (ADP-ribosyl cyclase 2) (Bone marrow stromal cell antigen 1) (BST-1) (Cyclic ADP-ribose hydrolase 2) (cADPR hydrolase 2) (CD antigen CD157) (Q10588)
Organism: Homo sapiens (Human)
Function: Catalyzes both the synthesis of cyclic ADP-beta-D-ribose (cADPR) from NAD(+), and its hydrolysis to ADP-D-ribose (ADPR). Cyclic ADPR is known to serve as an endogenous second messenger that elicits calcium release from intracellular stores, and thus regulates the mobilization of intracellular calcium (Probable). May be involved in pre-B-cell growth (Probable).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:8202488}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD-dependent protein deacetylase sirtuin-1
- NAD-dependent protein deacetylase sirtuin-3, mitochondrial
- Nicotinamide N-methyltransferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Purine nucleoside phosphorylase
- NAD-dependent protein deacylase sirtuin-6
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
Sequence:
MAAQGCAASRLLQLLLQLLLLLLLLAAGGARARWRGEGTSAHLRDIFLGRCAEYRALLSPEQRNKNCTAIWEAFKVALDKDPCSVLPSDYDLFINLSRHSIPRDKSLFWENSHLLVNSFADNTRRFMPLSDVLYGRVADFLSWCRQKNDSGLDYQSCPTSEDCENNPVDSFWKRASIQYSKDSSGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGPNVESCGEGSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALKSAAAATQRKAPSLYTEQRAGLIIPLFLVLASRTQL
Protein: Aquaporin TIP1-2 (Gamma-tonoplast intrinsic protein 2) (Gamma-TIP2) (Salt stress-induced tonoplast intrinsic protein) (Tonoplast intrinsic protein 1-2) (AtTIP1;2) (Q41963)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Water channel required to facilitate the transport of water across cell membrane. May be involved in the osmoregulation in plants under high osmotic stress such as under a high salt condition. Transports urea in yeast cells in a pH-independent manner. Transports H(2)O(2) in yeast cells.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14576283}; Multi-pass membrane protein {ECO:0000269|PubMed:14576283}. Note=Tonoplast.
Interaction partners:
- Protein S-acyltransferase 24
- NAC domain-containing protein 91
- PAMP-induced secreted peptide 1
- Aquaporin SIP1-1
Sequence:
MPTRNIAIGGVQEEVYHPNALRAALAEFISTLIFVFAGSGSGIAFNKITDNGATTPSGLVAAALAHAFGLFVAVSVGANISGGHVNPAVTFGVLLGGNITLLRGILYWIAQLLGSVAACFLLSFATGGEPIPAFGLSAGVGSLNALVFEIVMTFGLVYTVYATAVDPKNGSLGTIAPIAIGFIVGANILAGGAFSGASMNPAVAFGPAVVSWTWTNHWVYWAGPLIGGGLAGIIYDFVFIDENAHEQLPTTDY
Protein: Homeotic protein empty spiracles (P18488)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a homeotic selector gene controlling antennal and mandibular segment identity.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor btd
- Fork head domain transcription factor slp1
- Fork head domain transcription factor slp2
Sequence:
MTKMIPPVPTAAAAVMMPTPKQKIGFSIESIVGNDVSTAGGNSTPDLSGPQSPPPGERNVPGSPPQTPPATLTLIPGSPPHHLMAPPAHGLPYPHPHAQQQQQQHLQAPHPHPHLSPAQQHVLHQHLLMQHQHPGTPKSHQDIQELLQRLHHNAAMASGLSPLQTRLSPETEQPQMAVSLKRERSPAPPAMEQAENPAQRIQPPHTPPKSVSPQSSQPSSSPTLLISSPHATPPQQQQQQPPPNYPKPAMMHPGGAGPMMMPGMPPAGLVRPFPMGPGGPPMPQGQPGLPDIKALPPYINAPPELPPQHNPHLIAAAQFQMAAALQAGHVLGPAAAAAAAAGLPPHAAQFMPNPGMARDSYQLYPWLLSRHGRIFPHRFPGSFLVPPFRKPKRIRTAFSPSQLLKLEHAFESNQYVVGAERKALAQNLNLSETQVKVWFQNRRTKHKRMQQEDEKGGEGGSQRNMHNGSGDEDDDELIDMEMDECPSDEEHELDASH
Protein: SKP1-like protein 5 (SKP1-like 5) (Q6H4D6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, a RING-box and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9FHW7}.
Interaction partners:
- Os01g0185400 protein
- F-box protein
- Os01g0106800 protein
- Os02g0708300 protein
- COP9 signalosome complex subunit 5
- Cyclin-dependent kinases regulatory subunit 1
- Calcyclin-binding protein
- Os07g0489500 protein
- Os09g0452700 protein.
- Ubiquitin-ribosomal protein eL40y fusion protein
Sequence:
MAAVKEGADAGDSKILLISSDGQHFQVTEAEASMSKLVSNMIEDGCTENGVPLPNVASNVLAKVLEYCKKHAAAAAAEDVAVKDQELKSFDASFIDVDNTMLFNLILAANYLNVPSLLDLACQHTADLIKGKTVQEIRDMFGIVNDFTPEEEEEIRKENEWAFEN
Protein: Metalloendopeptidase (EC 3.4.24.-) (B5XFY0)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MAPVFVLSIFIAVLCSVQGRSTGKVSFERSEEDMEIDGTSANSIEEDEYSASTLIEKANRNLGQRPDEPLVMFGDIAVYTGFMNADPCTARGCKWQKSSDGNVYVPFVISNEYSARERSVIEGGLRTFAASTCIRFFPRTNQRDFVDVQSQSGCFSFIGRRGNGQVVSLSRNGCVFLSVVQHELLHALGFNHEQTRSDRDSNVQILFQNIMPGMEFNFRKINTINLGTPYDYNSVMHYSRFAFSRNRQPTIFPIPDNNAVIGRATEMSPIDILRINRLYNCTGQQLD
Protein: Actin-like protein 9 (Q8TC94)
Organism: Homo sapiens (Human)
Function: Testis-specic protein that plays an important role in fusion of proacrosomal vesicles and perinuclear theca formation.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:33626338}. Cytoplasm, cytoskeleton, perinuclear theca {ECO:0000269|PubMed:33626338}. Note=Localizes predominantly in the equatorial segment of the sperm head and neck regions, with some localization in the acrosomal segment of the head. Colocalizes in the acrosomal and equatorial segments of sperm with ACTL7A. Colocalizes with PLCZ1 in the equatorial segment of the head of capacitated sperm. {ECO:0000269|PubMed:33626338}.
Interaction partners:
- Dynactin subunit 2
- Actin-related protein 10
Sequence:
MDASRPKSSESQSSLEAPRPGPNPSPNVVNKPLQRDSPGMVADRLPPKTGAVVIDMGTGTCKVGFAGQASPTYTVATILGCQPKKPATSGQSGLQTFIGEAARVLPELTLVQPLRSGIVVDWDAAELIWRHLLEHDLRVATHDHPLLFSDPPFSPATNREKLVEVAFESLRSPAMYVASQSVLSVYAHGRVSGLVVDTGHGVTYTVPVFQGYNLLHATERLDLAGNNLTAFLAEMLLQAGLPLGQQDLDLVENIKHHYCYVASDFQKEQARPEQEYKRTLKLPDGRTVTLGKELFQCPELLFNPPEVPGLSPVGLSTMAKQSLRKLSLEMRADLAQNVLLCGGSSLFTGFEGRFRAELLRALPAETHVVVAAQPTRNFSVWIGGSILASLRAFQSCWVLREQYEEQGPYIVYRKCY
Protein: Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.367) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Lysine N-methyltransferase 1C) (Protein G9a) (Q96KQ7)
Organism: Homo sapiens (Human)
Function: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.
Subcellular location: Nucleus {ECO:0000269|PubMed:11316813}. Chromosome {ECO:0000269|PubMed:11316813}. Note=Associates with euchromatic regions (PubMed:11316813). Does not associate with heterochromatin (PubMed:11316813). {ECO:0000269|PubMed:11316813}.
Interaction partners:
- Histone-lysine N-methyltransferase EHMT1
- Chromobox protein homolog 3
- Histone deacetylase 1
- Histone H3.3
- DNA
- Histone H3.2
- Histone H3.1
- E3 ubiquitin-protein ligase UHRF1
- Histone H3.1t
- Histone H3.3C
Sequence:
MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLEPAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPSKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPELGSLPPVNT
Protein: Cytochrome P450 4A10 (CYPIVA10) (Cytochrome P450-LA-omega 1) (Cytochrome P452) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) (P08516)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long-chain fatty acids. Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver. In kidney, may play an important role in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Also participates in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) in kidney by converting 8,9-epoxyeicosatrienoic acid (EET) to 20,8,9-HEET, an activator of PPARA. Displays substantially lower fatty acid omega-1 hydroxylase activity. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3027069}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:3027069}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 2E1
- Cytochrome P450 3A1
- UDP-glucuronosyltransferase 1A1
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Cytochrome P450 2U1
- Cytochrome P450 3A18
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase 2B1
Sequence:
MSVSALSSTRFTGSISGFLQVASVLGLLLLLVKAVQFYLQRQWLLKAFQQFPSPPFHWFFGHKQFQGDKELQQIMTCVENFPSAFPRWFWGSKAYLIVYDPDYMKVILGRSDPKANGVYRLLAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVKNMADSIRLMLDKWEQLAGQDSSIEIFQHISLMTLDTVMKCAFSHNGSVQVDGNYKSYIQAIGNLNDLFHSRVRNIFHQNDTIYNFSSNGHLFNRACQLAHDHTDGVIKLRKDQLQNAGELEKVKKKRRLDFLDILLLARMENGDSLSDKDLRAEVDTFMFEGHDTTASGVSWIFYALATHPEHQQRCREEVQSVLGDGSSITWDHLDQIPYTTMCIKEALRLYPPVPGIVRELSTSVTFPDGRSLPKGIQVTLSIYGLHHNPKVWPNPEVFDPSRFAPDSPRHSHSFLPFSGGARNCIGKQFAMSEMKVIVALTLLRFELLPDPTKVPIPLPRLVLKSKNGIYLYLKKLH
Protein: DNA damage-inducible transcript 4-like protein (HIF-1 responsive protein RTP801-like) (Protein regulated in development and DNA damage response 2) (REDD-2) (Q96D03)
Organism: Homo sapiens (Human)
Function: Inhibits cell growth by regulating the TOR signaling pathway upstream of the TSC1-TSC2 complex and downstream of AKT1.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small nuclear ribonucleoprotein G
Sequence:
MVATGSLSSKNPASISELLDCGYHPESLLSDFDYWDYVVPEPNLNEVIFEESTCQNLVKMLENCLSKSKQTKLGCSKVLVPEKLTQRIAQDVLRLSSTEPCGLRGCVMHVNLEIENVCKKLDRIVCDSSVVPTFELTLVFKQENCSWTSFRDFFFSRGRFSSGFRRTLILSSGFRLVKKKLYSLIGTTVIEGS
Protein: Interphotoreceptor matrix proteoglycan 1 (Sialoprotein associated with cones and rods) (SPACR) (Q8JIR8)
Organism: Gallus gallus (Chicken)
Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein. May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix (By similarity).
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q17R60}. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:11991949}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8R1W8}.
Interaction partners:
- Peripherin-2
- Elongation of very long chain fatty acids protein 4
- Kelch like family member 31.
Sequence:
MHLKTGLIFLAICLALQVQGSREIPSKTNHGEAKQLADASGSDKTERTTKRSRVSTIRRIFDMAKHRTKRSPFFSTGVKICPQESVKQILASHQAYYRLRVCQEAVWEAFRIFLDRIPDTSEYQNWVTACQRETFCIFDIGKNFSNSQEHLEIIQRRVKHRTFQERKDEISTDKTGGKKLEDIPSVSTGPPSASLSTYTLVPNGTLLNEIVNETKTPVKELGTNTVPELPAEQMVEFSVTLTDQEYTAELSDPNSPQYRQLAAKFQLQMQKIFEKLPGFKEIHVLGFKQKKEKDGSSSTIARYMVNFERDGSEIKSTADDISTIGSNKVENEKVPLSAKEEREISATKLTVTDLQQLVATALHEDRSLPVDLGTLRFTDEPIKPSSDFDNDIQGMVTIPLAGPDLDDTISAELPLVYPSPITVDQTRDIFVDEFTTGITDLSREIGGPEDFDSNFITSEPAFPTKPSREPPHDRSPDTEDITTDYQRFTVPFSALVSTDSPAKPEDSYLPPPADESDSNDLITDESPTEQVITPAVYTTGSFTLPTFLQATDKDTEAEMKKELVGVTEPLFKEADRDSLSGQAVKMMDELESSGDDILVTTSTYKTLPFLIGSSDLFATQPEVTFAAALPPDQTLLPTVTSPFYSHSVVIDQSPEVPDTLMPAAASALPDRASTGVQDIAAELDGAGVKSTAVLDEAEHGSGYISVQTTEPAEVTQAPTLKYVTTSSMTTAAKGKELVVFFSLRVTNMHFSDDLFNRSSQEYKALEQQFMQLLLPYLQSNLTGFKQLEILNFRNGSVIVNSKMKFARTVPYNITEAVHCVLEDFCDAAAQHLNLEIDSYSLDIEPADQADPCKFMACDEFSKCIMNEWTKEADCLCKPGYASQDGLPCRSLCEMEPHLCDNGGKCELVPGRGAVCRSPDQFTEPGLTS