wanglab/gogpt-training-data huggingface dataset:
Protein: TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) (O46680)
Organism: Bos taurus (Bovine)
Function: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight junction {ECO:0000250|UniProtKB:P36897}. Membrane raft {ECO:0000250|UniProtKB:P36897}. Cell surface {ECO:0000250|UniProtKB:P36897}.
Interaction partners:
- TGF-beta receptor type-2
- Transforming growth factor beta-1 proprotein
- SMAD family member 7
- Mothers against decapentaplegic homolog
- Transforming growth factor beta
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 4
- E3 ubiquitin-protein ligase
- Growth/differentiation factor 11
- Growth/differentiation factor 8
Sequence:
MEAAAATPRPRLFLLMLAAAATLVPEATPLQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSITTTYCCNQDHCNKIELPTVGKPSSGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEVARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM
Protein: Seven TM Receptor (Q9N2S7)
Organism: Caenorhabditis elegans
Interaction partners:
- Serpentine Receptor, class T
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Serpentine Receptor, class D
- Serpentine Receptor, class AB
- Girdin homolog
Sequence:
MKKETTFDAMKATVQRISFAFSCFSNIILILLICTNSPKKIGSYKYLMIYFCVFAIFFSVLDIVIQPYILSAGPGFIVITEIKDTFLGPFGETCFLSSICGCFGVILATIAIHFIYRYFALERKGKLKYFQGGYLVVWLFVPLFVGTVWTIVTVYFCAPNDITLEYSRTLMKDHYEIDLENVTYIGSIYFVKDANGKSVMNKFALLGMAILFSIMGVSLSILAYFATKCYTRIKKLIYEGESSYTRNLQKQLYKALVAQASIPMFFIFTPIGLYLTLPLVGIELEISGEIATFVYALYPALDPLPIIFIIHNYRDAVLEFLGCCNVNNRIGAEDEPTSVTRHVSNCS
Protein: Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide) (Bicoid-interacting protein 1) (dSAP18) (Q9VEX9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the tethering of the SIN3 complex to core histone proteins. Interacts with bicoid (bcd) to repress transcription of bicoid target genes in the anterior tip of the embryo; a process known as retraction. Interacts with Trl and binds to Polycomb response elements at the bithorax complex. May contribute to the regulation of other homeotic gene expressions.
Subcellular location: Nucleus {ECO:0000269|PubMed:11256608, ECO:0000269|PubMed:11455422}. Cytoplasm {ECO:0000250|UniProtKB:O00422}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:O00422}.
Interaction partners:
- LD23870p
- Histone deacetylase complex subunit SAP30 homolog
- Acinus, isoform A
- FI07430p
- Pinin, isoform B
- Histone deacetylase HDAC1
- Paired amphipathic helix protein Sin3a
- LD24793p
- Chromatin assembly factor 1 p55 subunit
- RNA and export factor binding protein 2, isoform A
Sequence:
MANVESMIVEEKTQVKQIDREKTCPMLLRVFCSTGRHHSVSEYMFGNVPTNELQIYTWQDATLHELTSLVRDVNPDTRKKGTYFDFAVVYPNFRSNHFQMREIGVTCTGQKGIDDNKTLAQAKFSIGDFLDISITPPNRLPPTARRQRPY
Protein: Scavenger receptor (Q58SM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
TCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSMSASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTTMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSESTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: Transcriptional regulator (B1W457)
Organism: Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)
Interaction partners:
Sequence:
MSSEYAKQLGAKLRAIRTQQGLSLHGVEEKSQGRWKAVVVGSYERGDRAVTVQRLAELADFYGVPVQELLPGTTPGGAAEPPPKLVLDLERLAHVPPEKAGPLQRYAATIQSQRGDYNGKVLSIRQDDLRTLAVIYDQSPSVLTEQLISWGVLDADARRAVSHDEG
Protein: Rho-related protein racO (Q54Z85)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Mss4-like family protein
- Cofilin-1A
Sequence:
MKKEVKIVTVGDGLIGKTTLLMTYYTNEFNTRVYSSFDSEYLNPLTVIINDDVIEISLWENDGFDSDGVYKESPPFIKYQPNHINVFLLLFSISDRDSFNNCLTKWNFEIKQNYPSIPVVLCGIKTDLREEENLVYKNSIDNSHFISFSEGVNMANEIDAVGYYECSSLKKKGLSELFDVLAIVGYSNILTKKKDKIKFKNNNNNNNYNENNQNISDTENNDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNENNNNSYKNHNNKTTNKCKIS
Protein: S100 calcium binding protein, beta (neural) (A0A060YDS7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Protein S100
- F-actin-capping protein subunit alpha
- F-actin-capping protein subunit alpha
- F-actin-capping protein subunit alpha
- F-actin-capping protein subunit alpha
- F-actin-capping protein subunit alpha
- HhH-GPD domain-containing protein
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MTDLESSLATIMEVFHRYTEKEGDKHKLKKSELKDLINEELPALTGQVKDQATMDSLMESLDTDGDSELDFQEFMTFITMVTVCCHDFCEHHEDE
Protein: Phenylacetate-coenzyme A ligase (EC 6.2.1.30) (Phenylacetyl-CoA ligase) (PA-CoA ligase) (Q72K16)
Organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism.
Interaction partners:
Sequence:
MMYQPELETLPREKLRALQEERLKRLVAYVYERVPFYRRLLDEAGVDPKGFRGLEDLPRIPFTKKTDLRDHYPFGLFAVPREEVARVHASSGTTGKPTVVGYTKNDLKVFAEVVARSLAAAGARPGMMLHNAYGYGLFTGGLGLHGGAEALGMTVVPVSGGMTERQVMLIQDFRPEVISCTPSYAQTLAEEFRKRGVSPEELSLEYAVLGAEPWTEAIRKQVDEGLGVKSTNIYGLSEIIGPGVSNECVEERQGSHIWEDHFLPEVVDPDTGEPLPEGKVGVLVFTTLTKEAMPLLRYWTGDLTFLTYEACTCGRTHVRMGPILGRTDDMLIIRGVNVYPTQVEAVLLAIPEVVPHYQIVVRREGTLDEAELKVEVSEPFFREIGQEVLSDEVVEADHRLHALRERIARKIKDNVGVTLKVTLLPPGQAPRSEGGKLRRVLDLRK
Protein: cAMP-dependent protein kinase regulatory subunit (PKA regulatory subunit) (P36600)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit
- Adenylate cyclase
- 3',5'-cyclic-nucleotide phosphodiesterase
- Serine/threonine-protein kinase gad8
- Serine/threonine-protein kinase psk1
- Serine/threonine-protein kinase sck2
- Serine/threonine-protein kinase orb6
- Serine/threonine-protein kinase ppk33
- Aurora kinase
- Zinc finger protein rst2
Sequence:
MSFEEVYEELKALVDEQNPSDVLQFCYDFFGEKLKAERSVFRRGDTITESFSDGDESDFLSELNDMVAGPEAIGPDAKYVPELGGLKEMNVSYPQNYNLLRRQSVSTESMNPSAFALETKRTFPPKDPEDLKRLKRSVAGNFLFKNLDEEHYNEVLNAMTEKRIGEAGVAVIVQGAVGDYFYIVEQGEFDVYKRPELNITPEEVLSSGYGNYITTISPGEYFGELALMYNAPRAASVVSKTPNNVIYALDRTSFRRIVFENAYRQRMLYESLLEEVPILSSLDKYQRQKIADALQTVVYQAGSIVIRQGDIGNQFYLIEDGEAEVVKNGKGVVVTLTKGDYFGELALIHETVRNATVQAKTRLKLATFDKPTFNRLLGNAIDLMRNQPRARMGMDNEYGDQSLHRSPPSTKA
Protein: Dihydrofolate reductase (EC 1.5.1.3) (P04382)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Interaction partners:
Sequence:
MIKLVFRYSPTKTVDGFNELAFGLGDGLPWGRVKKDLQNFKARTEGTIMIMGAKTFQSLPTLLPGRSHIVVCDLARDYPVTKDGDLAHFYITWEQYITYISGGEIQVSSPNAPFETMLDQNSKVSVIGGPALLYAALPYADEVVVSRIVKRHRVNSTVQLDASFLDDISKREMVETHWYKIDEVTTLTESVYK
Protein: Protein XRP2 (A0A1B2JLU2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
Protein: Auracyanin-A (Q8RMH6)
Organism: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Function: Probably a soluble electron acceptor for the integral membrane protein electron transfer alternative complex III (ACIII).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Possibly located on the extracellular face of the cell membrane.
Interaction partners:
- Blue
Sequence:
MKITLRMMVLAVLTAMAMVLAACGGGGSSGGSTGGGSGSGPVTIEIGSKGEELAFDKTELTVSAGQTVTIRFKNNSAVQQHNWILVKGGEAEAANIANAGLSAGPAANYLPADKSNIIAESPLANGNETVEVTFTAPAAGTYLYICTVPGHYPLMQGKLVVN
Protein: Protein patched homolog 2 (PTC2) (Q9Y6C5)
Organism: Homo sapiens (Human)
Function: Plays a role in the control of cellular growth. May have a role in epidermal development. May act as a receptor for Sonic hedgehog (SHH).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Indian hedgehog protein
- Sonic hedgehog protein
- Desert hedgehog protein
- Protein smoothened
- Brother of CDO
- Cell adhesion molecule-related/down-regulated by oncogenes
- Growth arrest-specific protein 1
- Suppressor of fused homolog
- Protein patched homolog 1
- Low-density lipoprotein receptor-related protein 2
Sequence:
MTRSPPLRELPPSYTPPARTAAPQILAGSLKAPLWLRAYFQGLLFSLGCGIQRHCGKVLFLGLLAFGALALGLRMAIIETNLEQLWVEVGSRVSQELHYTKEKLGEEAAYTSQMLIQTARQEGENILTPEALGLHLQAALTASKVQVSLYGKSWDLNKICYKSGVPLIENGMIERMIEKLFPCVILTPLDCFWEGAKLQGGSAYLPGRPDIQWTNLDPEQLLEELGPFASLEGFRELLDKAQVGQAYVGRPCLHPDDLHCPPSAPNHHSRQAPNVAHELSGGCHGFSHKFMHWQEELLLGGMARDPQGELLRAEALQSTFLLMSPRQLYEHFRGDYQTHDIGWSEEQASTVLQAWQRRFVQLAQEALPENASQQIHAFSSTTLDDILHAFSEVSAARVVGGYLLMLAYACVTMLRWDCAQSQGSVGLAGVLLVALAVASGLGLCALLGITFNAATTQVLPFLALGIGVDDVFLLAHAFTEALPGTPLQERMGECLQRTGTSVVLTSINNMAAFLMAALVPIPALRAFSLQAAIVVGCTFVAVMLVFPAILSLDLRRRHCQRLDVLCCFSSPCSAQVIQILPQELGDGTVPVGIAHLTATVQAFTHCEASSQHVVTILPPQAHLVPPPSDPLGSELFSPGGSTRDLLGQEEETRQKAACKSLPCARWNLAHFARYQFAPLLLQSHAKAIVLVLFGALLGLSLYGATLVQDGLALTDVVPRGTKEHAFLSAQLRYFSLYEVALVTQGGFDYAHSQRALFDLHQRFSSLKAVLPPPATQAPRTWLHYYRNWLQGIQAAFDQDWASGRITRHSYRNGSEDGALAYKLLIQTGDAQEPLDFSQLTTRKLVDREGLIPPELFYMGLTVWVSSDPLGLAASQANFYPPPPEWLHDKYDTTGENLRIPPAQPLEFAQFPFLLRGLQKTADFVEAIEGARAACAEAGQAGVHAYPSGSPFLFWEQYLGLRRCFLLAVCILLVCTFLVCALLLLNPWTAGLIVLVLAMMTVELFGIMGFLGIKLSAIPVVILVASVGIGVEFTVHVALGFLTTQGSRNLRAAHALEHTFAPVTDGAISTLLGLLMLAGSHFDFIVRYFFAALTVLTLLGLLHGLVLLPVLLSILGPPPEVIQMYKESPEILSPPAPQGGGLRWGASSSLPQSFARVTTSMTVAIHPPPLPGAYIHPAPDEPPWSPAATSSGNLSSRGPGPATG
Protein: Kallikrein-11 (hK11) (EC 3.4.21.-) (Hippostasin) (Serine protease 20) (Trypsin-like protease) [Cleaved into: Kallikrein-11 inactive chain 1; Kallikrein-11 inactive chain 2] (Q9UBX7)
Organism: Homo sapiens (Human)
Function: Possible multifunctional protease. Efficiently cleaves 'bz-Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly cleaves other substrates for kallikrein and trypsin. Cleaves synthetic peptides after arginine but not lysine residues.
Subcellular location: [Isoform 1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus {ECO:0000269|PubMed:36689511}. Secreted {ECO:0000269|PubMed:36689511}.
Interaction partners:
- Thymic stromal lymphopoietin
- Cytokine receptor-like factor 2
- Kallikrein-10
- Interleukin-7 receptor subunit alpha
Sequence:
MQRLRWLRDWKSSGRGLTAAKEPGARSSPLQAMRILQLILLALATGLVGGETRIIKGFECKPHSQPWQAALFEKTRLLCGATLIAPRWLLTAAHCLKPRYIVHLGQHNLQKEEGCEQTRTATESFPHPGFNNSLPNKDHRNDIMLVKMASPVSITWAVRPLTLSSRCVTAGTSCLISGWGSTSSPQLRLPHTLRCANITIIEHQKCENAYPGNITDTMVCASVQEGGKDSCQGDSGGPLVCNQSLQGIISWGQDPCAITRKPGVYTKVCKYVDWIQETMKNN
Protein: ATPase inhibitor B, mitochondrial (ATP synthase F1 subunit epsilon B) (Inhibitor of F(1)F(o)-ATPase B) (IF(1) B) (IF1 B) (Q1LYB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing fech to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
Sequence:
MARFLNSNIRKFLTTQIRMSSDQLGELGKGAGKGGGGGGAVRQAGGAFGKKQAAEEEMYFKRKEQEQLSALRRHHQEEIDHHKKEIERLQHEITRHESKIKKLKHDD
Protein: Probable palmitoyltransferase AKR2 (EC 2.3.1.225) (Ankyrin repeat-containing protein AKR2) (Q12013)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in constitutive endocytosis of a-factor receptor STE3.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Palmitoyltransferase PFA3
- Palmitoyltransferase PFA5
- Palmitoyltransferase SWF1
- Palmitoyltransferase PFA4
- Sphingoid long chain base kinase 4
Sequence:
MTSMSIIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKDGDLKVVKDVVESGAVDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNQAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNNDNVDIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLFKKSSHAQFTIFLSPFLLMVYIYLISLVLSPVLAIMLSLLVTVVMVNTLKKFVLPCLPRKNTYKVSLTRTPFFSGLFLSTFCFLIYIWTKKLYPYSVSDYTMKNVQFLVTSFLTVVLFLRLVRSDPGCLKTDDSLTSIQETIKQLIDLGKFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVTVQYHMFLFMWLCLAYFKKTNYIYEQVEEYARCALLKNETLCKGSNYDPSTFFLFIWISVNFIWLGAMLIVQFFQILKGITTPELFILIKEEHKAKFINLIPFENSIYTSESKGVEDSDMIPEGPSATTITHTISIDGLEPRNRRRAILSACFSMMGINQWLVTIKEIVGITHILHGQVPQQHHSSLLRSFLVTNHWKTNLTDFWLNSDVTAPLWQRFFYSSDTSKAMLGGTEVDYYELYEYPAREGEVLRPN
Protein: LD21346p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9VXS3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- RE31221p
- RE03883p
- CG4570 protein
- Osiris 20
Sequence:
MLKWAVNQPRPSYLARDEVMATSSEAVGSSYSEFHALRGKLKRKSIGVAPGKENQLTSTPLPASSLSLHARTPLLKDLSNILATPPSGGASGANGATGGVTAVPLKFACTLPTFEAEYSPNAAIIPGSLIALRGMGIPDSYFEKPRYLEQKPLPHPHPHPAPPTGEQNTLSSSQMGDVTLERMIDAILESNRKVLPNARQQQHQHQHRQPRQHLRQRHRLRQQVLRSSHGHGHGPTQTPSPTYRPAFDPASDLCEYWKSPSRRDSLPAEGFEEREVRSPVPTVSESQDAKRHSLQLRRQRVVRRKRKITTKISSSVRQSAQKLLAAARSGSIAAPAQKMRHISPDSGHNSTSDCELEEEHCQLSRGLELGGEELEDACQLDAMWLQVQARDATKRRLSFSLVEES
Protein: Kappa-type opioid receptor (K-OR-1) (KOR-1) (MSL-1) (P33534)
Organism: Mus musculus (Mouse)
Function: G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}; Multi-pass membrane protein {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}.
Interaction partners:
- Pro-opiomelanocortin
- Proenkephalin-B
- Proenkephalin-A
- Prepronociceptin
- Methyl-CpG-binding protein 2
- Mu-type opioid receptor
Sequence:
MESPIQIFRGDPGPTCSPSACLLPNSSSWFPNWAESDSNGSVGSEDQQLESAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSAVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLASSVGISAIVLGGTKVREDVDVIECSLQFPDDEYSWWDLFMKICVFVFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITKLVLVVVAVFIICWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPVLYAFLDENFKRCFRDFCFPIKMRMERQSTNRVRNTVQDPASMRDVGGMNKPV
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)] At3g07690, cytosolic (G3Pdh(At3g07690)) (EC 1.1.1.8) (Q9S785)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for glycerol-3-phosphate (G3P) accumulation during systemic acquired resistance (SAR) establishment.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N335}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- Glycerol kinase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Dihydroxyacetone kinase
- Lipid phosphate phosphatase 1
- Probable lipid phosphate phosphatase 4
- Putative lipid phosphate phosphatase 3, chloroplastic
- Lipid phosphate phosphatase 2
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
Sequence:
MMDHLVETNSVPSRLVEERLDEIRRVMGKADDDPLRIVGVGAGAWGSVFIAMLQENYGKFRGKVSVRIWRRGGRAIDKATAEHLFEVINSREELLRRLIRRCAYLKYVEARLGDRVLYADEILKDGFCLNMIETPLCPLKVVTNLQEAVWDADIVINGLPSTETFQVFNEISKYWKERVNAPVIISLAKGVEAEFEPHPRIVTPTQMIHRATGIPLENILYLGGPNIASEVYNKEYANARICGSEKWRKPLGKFLRQSHFIVWDNSDLITHEVMGGLKNVYAIGAGMVATLTKESATSKSVYFAHCTSEMIFITHLLAKEPEKLAGPLLADTYVTLLKGRNAWYGQKLAKGELSLEMGDSIKGKGMIQGVSAVKAFFELLNQSSLSLQHPEEGKPVTPAELCPILKMLYRILITREFSCEAILEALRDETMNDPRELIEIAHSHLFFQPWLLGQKP
Protein: Integral membrane protein 2A (Protein E25) (O43736)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVKIAFNTPTAVQKEEARQDVEALLSRTVRTQILTGKELRVATQEKEGSSGRCMLTLLGLSFILAGLIVGGACIYKYFMPKSTIYRGEMCFFDSEDPANSLRGGEPNFLPVTEEADIREDDNIAIIDVPVPSFSDSDPAAIIHDFEKGMTAYLDLLLGNCYLMPLNTSIVMPPKNLVELFGKLASGRYLPQTYVVREDLVAVEEIRDVSNLGIFIYQLCNNRKSFRLRRRDLLLGFNKRAIDKCWKIRHFPNEFIVETKICQE
Protein: La protein 1 (AtLa1) (Q93ZV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17459889}. Nucleus, nucleolus {ECO:0000269|PubMed:17459889}.
Interaction partners:
- Protein EMBRYO DEFECTIVE 514
- At5g12410
- AT3g07170/T1B9_17
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- DEAD-box ATP-dependent RNA helicase 46
- THO complex subunit 4C
- Pre-mRNA cleavage factor Im 25 kDa subunit 2
- Alba DNA/RNA-binding protein
- Uncharacterized protein At2g34160
- ARM repeat superfamily protein
Sequence:
MSIPCLTEETAKTVLRQVEFYFSDSNLPIDDFLKKTVTESEDGLVSLALICSFSKMRGYLKLGDSKGDDIPEDTIKAVADTLRTSSALKISDDGKKVGRSTELLKLEDLIEQLNARTVAASPFSYDVKREDVESFFSQYGKVNSVRMPRHVAESRIFSGVALVEFPTEEDAQNVMKQNLVFAGQELELKPKKEFDNEREKDEVKFANYQPQKGSANQKNGSDHKNNSAYEPDYPKGLIISFTLKRSAEEGTTEQKSSEEPTDKTMEESETKPADTPDADKENTGEVQAEGAEDEDDEKEEKGALATHKDNKDVVLREDLKAVFGKFGDVKFVDFKMGSETGYLRFDEPEASQKARAAAVLANEGGLAVKNFIAVLEPVIGEAEKEYWTLLRSKDRFDKGGRGGRGGRRGGRFGRKRGSDSPGGRWNKSQKVEA
Protein: Boron transporter 1 (P53838)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in boric acid/borate export across the plasma membrane, and thereby protects yeast cells from boron toxicity. Involved in the trafficking of proteins to the vacuole.
Subcellular location: Cell membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSNESTRVTVSRGCTASDECAQALERTNDELDRESSVSESRSDEESHEKLSRRRFPTLGIGIWLDLKDRIPYYKSDWVDAFNYRVIPSIVDTYFNNLLPAIAFAQDMFDRTDNSYGVNEVLLSSAMAGIVFGVLGGQPLCIVGVTGPISIFNYTVYEIIKPLNTSYFGFMFWICMWSMIFHLVLAFTNAVCLLQYVTTFPCDIFGLFINVVYIQKGIQILTRQFSAKSGEKSVQDGFASVVVALVMTAFGLFFKLFHYYPLFSHRIRTFISDYSTALSVLFWSSFTHFGGYLHDVKFKKLPITKAFFPTSKVNRPQNTWLAYEPIPVKDVFIALPFGIFLTILFYFDHNVSSLMAQRHQYKLKKPSSFHYDFALLGLTTCISGVLGIPAPNGLIPQAPLHTETLLVRDSNQKVISCVEQRFTNTFQGLMILGTMTRPLLVCLGEIPQAVLSGLFFIMGINGLMTNSIIQRLVFLFSDPNRRDNTSPLMKVSKKSMLIFLSFSLTGFAGEFAITNTIAAIGFPLVLLLSVLVSFSFAYIFPTEELKILDTNVAQKFTIKNLLLENIRDAKFCDKHED
Protein: U6 snRNA-associated Sm-like protein LSm1 (P87173)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. The LSM1-LSM7 complex binds RNA with a preference for poly-U ends.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P47017}. Cytoplasm {ECO:0000250|UniProtKB:P47017}. Cytoplasm, P-body {ECO:0000250|UniProtKB:P47017}.
Interaction partners:
- LSM complex subunit lsm4
- LSM complex subunit lsm7
- LSM complex subunit lsm2
- Putative ATP-dependent RNA helicase ste13
- LSM complex subunit lsm5
- LSM complex subunit lsm3
- LSM complex subunit lsm6
- Deadenylation-dependent mRNA-decapping factor pdc2
- mRNA decapping complex subunit 2
- mRNA-decapping enzyme subunit 1
Sequence:
MNQATQIIPFTTSGSLVDYVDRKVIVVLRDGKKLIGILRSFDQFANLMLQYTIERIYVDDMYGDIDRGVYIVRGENVVLLGELDLDKEYDAVKQLRRMPAEELYPLAKLHEEEKKKNIREKGKYLHSVGFSVDGGHDDLY
Protein: Guanosine-diphosphatase (GDPase) (EC 3.6.1.42) (Q9UT35)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14612233}; Single-pass type II membrane protein {ECO:0000269|PubMed:14612233}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase [NAD
- Golgi apyrase
Sequence:
MTPTMKSIARRKALLIALSIFAVTFILWNGFPGSSNRPLPSSNDEFHYEDIELPSGYRSEGEVVDLLNPKDELEEPLFSEEPLFPVTTSIPTKTAVSKPKIAPTSAAKDVTFSSSIDSDDCSVAYDNSKPVRQYVLMIDAGSTGSRVHVYQFNNCNPSPKLEEEFFKMIEPGLSSFAGDPEGAAASLDPLLDYAMENVPEEYRRCSPIAVKATAGLRLTGESEAKAILKSVRQHLENDYPFPIVKDGVSILEGSMEGIYAWITINYLLGTLGGKATHSTVAVMDLGGASTQLVFEPRFASDGESLVDGDHKYVLDYNGEQYELYQHSHLGYGLKEARKLIHKFVLNNAEALKESLELLGDSTSIIHPCLHLNASLTHPDSKSEASEVVFVGPSLAHLSLQCRGIAEKALYKDKNCPVRPCSFNGVHQPKFTETFTDSPIYLISYFYDRMISLGMPSTFTIEDMKYLANSVCSGPTYWQDAFSLTDALKELKEEPEWCLDLNYMISLLSVGYEIPNNRQLHTAKKIDNKELGWCLGASLSMLSEQNNGWNCNVKEEI