wanglab/gogpt-training-data huggingface dataset:
Protein: FERM domain containing kindlin 2 (H0YJ34)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
SDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLITPGSGTDVLYIGPLKGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPITSPEILAKMFKPQALLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPEQITTDITPECLVSPRYLKKYKNKQPGYIRDLITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKKEELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV
Protein: cAMP-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) (F1SD45)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHFAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Protein: Calcineurin subunit B type 2 (Calcineurin B-like protein) (CBLP) (Protein phosphatase 2B regulatory subunit 2) (Protein phosphatase 3 regulatory subunit B beta isoform) (P28470)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q63811}. Note=Localizes in the mitochondria in a SPATA33-dependent manner. {ECO:0000250|UniProtKB:Q63811}.
Interaction partners:
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Nuclear factor of activated T-cells 1
- Nuclear factor of activated T-cells, cytoplasmic 3
- Calmodulin-like protein 4
- Nuclear factor of activated T-cells 2
- Nuclear factor of activated T-cells, cytoplasmic 4
- Calmodulin-1
- Calmodulin-like protein 3
Sequence:
MGNEASYHSEMGTHFDHDEIKRLGRSFKKMDLDKSGSLSVDEFMSLPELQQNPLVGRVIDIFDTDGNGEVDFREFIVGTSQFSVKGDEEQKLRFAFRIYDMDNDGFISNGELFQVLKMMVGNNLKDWQLQQLVDKSILVLDKDGDGRISFEEFRDVVRTMEIHKKLVVFVDHGQED
Protein: AT3g51510/F26O13_150 (Transmembrane protein) (Q9SCZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAASLTSLPTGFCLSHGDECCNRSPTKSPFPGHHPLAGRRKGHLLHYERSTVRRLVVTAATEGSKKSKESEPSWANPDSDEPPPWARNEGRSSTSQESFEVPFFVYLLASAITAIAAIGSVFEYTSKNPVFGILESDSIFYTPVLGFFALTGIPTSVFLWFKSVEAANKEAQEQDKRDGFL
Protein: Down syndrome cell adhesion molecule 1, isoform BY (A0A0B4K7H7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQHYEEDIHKAFVIRGNSAILKCDIPSFVADFVNVISWHSDEKENFYPGTEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVGPRLTSGDKTRNVDISLAGSGTLLCPAQAYPVPFFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVLPQIVPFAYEDLINMGDSIDLFCQIQKGDRPIKVHWSFERSAGDYGFDQVQPQMRTNRISEKTSMISIPSASPAHTGRDTCIASNKAGTTTYSVDLTVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: NADH-quinone oxidoreductase subunit L (EC 7.1.1.-) (NADH dehydrogenase I subunit L) (NDH-1 subunit L) (NUO12) (P33607)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit H
Sequence:
MNMLALTIILPLIGFVLLAFSRGRWSENVSAIVGVGSVGLAALVTAFIGVDFFANGEQTYSQPLWTWMSVGDFNIGFNLVLDGLSLTMLSVVTGVGFLIHMYASWYMRGEEGYSRFFAYTNLFIASMVVLVLADNLLLMYLGWEGVGLCSYLLIGFYYTDPKNGAAAMKAFVVTRVGDVFLAFALFILYNELGTLNFREMVELAPAHFADGNNMLMWATLMLLGGAVGKSAQLPLQTWLADAMAGPTPVSALIHAATMVTAGVYLIARTHGLFLMTPEVLHLVGIVGAVTLLLAGFAALVQTDIKRVLAYSTMSQIGYMFLALGVQAWDAAIFHLMTHAFFKALLFLASGSVILACHHEQNIFKMGGLRKSIPLVYLCFLVGGAALSALPLVTAGFFSKDEILAGAMANGHINLMVAGLVGAFMTSLYTFRMIFIVFHGKEQIHAHAVKGVTHSLPLIVLLILSTFVGALIVPPLQGVLPQTTELAHGSMLTLEITSGVVAVVGILLAAWLWLGKRTLVTSIANSAPGRLLGTWWYNAWGFDWLYDKVFVKPFLGIAWLLKRDPLNSMMNIPAVLSRFAGKGLLLSENGYLRWYVASMSIGAVVVLALLMVLR
Protein: AT4g17250/dl4660w (Transmembrane protein) (Q93ZA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGCDSHGNLSDTEFSKPLPSIGVYVAAASLICGVAMFSDLLHGFRHRKFWFPCKFFSLNATTLTFISVCVKLSLDLNTSMPSRQDQLAKLSSSVFVCTVMANSMPSLGYMVTQDLLMNLTALGILVITDVVNICIQLGTGAIYVFPQEHALVIILMLLMFMILSFSAITVPATKRFLELKYKKRYEFALKQCPSYTERRRGVPKLKEDLMKFWMMAHTSSPQFVMARSVTCTTTGFLCFLIAITLAEAMVRSYFLQPRSLGFCNGDSDYKWSTTLVLVSQTAAVAIGTVAPASRWLKAVNFRCPFRNKKSLKDELRVESYWVECLAEKKERPLNFWMLHGRCSRKLAHDLNRLMLDICIATQYGIVLASKFLRFITVYCSSRILLCCFHFTFKSDSVANAESSGSNPSTRQFVLHLEGEEEMVDYMARSNRVATDHLIQKGRKKQPVNLIELLEATTFISKGFEGIRDFDSDEVSSLASGEPPNSWALPLVTLTSIAVALPNIKPCSLKKLVKAVNEALVYVNKFEEVLDIEGELANSRKAAEVVWLGVDLYHKWLNVDLRKLSKQHSKTPQEVLKELVDIAQKEFTESWEKNRILCMKHKPSHWPIKTQAANSMYRISQTLLMKYESRNIETEETLLKDVEKMVSDIVSGCFCNTAQVIGMKCLVTAVEVREASVREAAMHLGRTEKILEIVDRRCMPALSHHKVAKIDEWREFYRTNKSITFTHPSSQCTTRELIINLE
Protein: Nuclear transition protein 2 (TP-2) (TP2) (Q05952)
Organism: Homo sapiens (Human)
Function: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P11101}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11101}. Chromosome {ECO:0000250|UniProtKB:P11101}. Note=Loaded onto the nucleosomes of condensing spermatids (By similarity). Nuclear import is mediated by IPO4. Nucleolar localization requires the protein to be phosphorylated (By similarity). {ECO:0000250|UniProtKB:P11101, ECO:0000250|UniProtKB:P11378}.
Interaction partners:
- Protamine-2
- Spermatid nuclear transition protein 1
- Sperm protamine P1
- Protamine-3
- Importin subunit alpha-4
Sequence:
MDTQTHSLPITHTQLHSNSQPQSRTCTRHCQTFSQSCRQSHRGSRSQSSSQSPASHRNPTGAHSSSGHQSQSPNTSPPPKRHKKTMNSHHSPMRPTILHCRCPKNRKNLEGKLKKKKMAKRIQQVYKTKTRSSGWKSN
Protein: Sphingosine-1-phosphate lyase (S1P lyase) (S1PL) (SP-lyase) (SPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase) (Q54RV9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine (By similarity). Sphingosine-1-phosphate (S1P) probably acts intracellularly as a second messenger perhaps by promoting cell proliferation; the absence of S1P lyase increases its concentration. This leads to increased lateral pseudopod formation as well as defects in the efficiency of chemotaxis. Overexpression of S1P lyase causes decreased growth rates, entry into stationary phase at lower cell density and increased sensitivity to the antitumor agents cisplatin and carboplatin; these effects are more pronounced in cells that express more enzyme.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sphingosine kinase B
- Sphingosine kinase A
- Probable sphingosine-1-phosphate phosphatase
- sphinganine-1-phosphate aldolase
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 1
- Ethanolamine-phosphate cytidylyltransferase
- sphingolipid 4-desaturase
- Ceramide synthase
Sequence:
MDKANDYLKDYQPAKLVLATAGITAASILAYQAITDRDFKDKLNKKIFRSIKSMPGVSDIVKKERAKAKVELKKMFKTDVRNAHYTLPLKGIKHEDLIEEMKALAKVDESHWVDSKVSGCVYLGEKEHTKLLNEAYSLFSLSNPLHPSVFPSIRKFETESISMVSNMLNAHSKVVGSLTSGGTESIFMAVKAYRDFYKDRTDRPEIVVPVTIHAAFDKACEYLKIRIVHIDVDPVSYKVDMAAMKKAINKDTILVAGSAVNFPHGIIDPIDEIAKLAQQYDIGCHVDACLGGFILPFAEKLDYDIPVFDFRIPGVTSMSVDTHKFGYAAKGTSVVLFGNKKLRRAMYFVAPNWPGGIYASPTLPGSRPGGLVAACWASLVSMGNDGFLEKAKGVMETTKKIIKGLQSINGVKIIGDPKAMVVAFTCDNIFYVNDYMSKKGWHLNALQRPNSLHVCVTAKMIGMESLFIEDLKDSIKLVKDNSGSLPKDGTAPIYGSAHSVPDREMVGTILSDFIDELITPDYKPSQST
Protein: Protein windpipe (Q9W266)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in negative regulation of the JAK/STAT pathway by binding to the receptor dome and promoting its internalization for subsequent lysosomal degradation, thereby reducing JAK/STAT signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25923769}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Pre-mod
Sequence:
MERVHLTAWLALFLIVVANATPTPARTPTGCPADCTCSLSQHTHKPLYHLKCNSTRGLRLTEKTFQSTVPVHSIDLSHLNLTRLSHLLDKLPELTSADLSHNQLKDLGHLGKGLKRLNLKHNQLTSDKLRKLPQHLQVLNLQHNNITHLPLELTHMHQLHQLELSHNAINCSCQTLEVRNWLVERIVYMEHPVVCSYPLEFRGRSWLQLKQDEICKKEKYQWFDTEENELMMGDQPAAVSAEREDEEELGKDFLPIVGNPAATAKKVRSPQIPLPSDQVEGSGDLSETNMELKLPEETVAEPEAAESQLVDAAASPSVLEEHIVKDEDEDDEGSGSGGGLLIIPDPSKVKITSEDDIDSDGKPEESDVRPLENPENSENPDTVFSNKIGIYEGDQEEKKPVEEDNIVPVVMTNLDTGLESDVVTDGPLDSSKESEDILTAKIGKPKDDSSAIYYLLAVIGLIVVGLVLFVAIKRCKYDSNAAARDAEAQRQTELLDMDKKQLGKPLHKNGHGNGQEHSPLIGEKTKLDEAQIVKKPYENGEAKDGAGQQPLLNGNGSANGGTKEAPETGEPAAHEYYPITPRYPTPQSPRASKYAQQQQLAEQNNNEPDGAYLPSSPKSGRYSPVYSPETGRVKIKLTETPKPKTPMLVTRSKSNAGDIITTPVRPIEPTHQVINGH
Protein: Uncharacterized protein YecA (P0AD05)
Organism: Escherichia coli (strain K12)
Interaction partners:
- UPF0225 protein YchJ
- Sugar phosphatase YidA
- Probable cyclic di-GMP phosphodiesterase PdeA
Sequence:
MKTGPLNESELEWLDDILTKYNTDHAILDVAELDGLLTAVLSSPQEIEPEQWLVAVWGGADYVPRWASEKEMTRFMNLAFQHMADTAERLNEFPEQFEPLFGLREVDGSELTIVEEWCFGYMRGVALSDWSTLPDSLKPALEAIALHGTEENFERVEKMSPEAFEESVDAIRLAALDLHAYWMAHPQEKAVQQPIKAEEKPGRNDPCPCGSGKKFKQCCLH
Protein: Coiled-coil domain-containing protein (Q7YWU3)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein hal-3
- Synaptonemal complex protein 3
- Serine/threonine-protein kinase plk-2
- C2H2-type domain-containing protein
- HORMA domain-containing protein
- C2H2-type domain-containing protein
- HORMA domain-containing protein
- HORMA domain-containing protein
- C2H2-type domain-containing protein
- Sun domain-containing protein 1
Sequence:
MNTPVKAKRQRQQMPGTPIPMGRQTHRAHSASGFYTPHVSKLKTNYDREFQKFLRSAKTAIDHLDKIEMQILCPLKKKIKRFHKESNTLDVYFRSQTYWRSFYKELMNRSDDVMDCFRFEDLRDVAAVVESHRLPDVLVSFVTQQLMEWRELFKDVEWMRKFRELSHNMDSLKTKRIEHVLRQDIIREIGVAIDVHNLKIDDFRSHSNNTERVAEGIAHAIEESKNKQDAGNQLKHVPVLSKQMSVRRWYREHYGDPQALSDESDEESLSDGDNSSLFVGTADSSSRDASDISTEEVVTENEFDEFFN
Protein: p53 apoptosis effector related to PMP-22 (Keratinocyte-associated protein 1) (KCP-1) (Q9JK95)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Plays a role in stratified epithelial integrity and cell-cell adhesion by promoting desmosome assembly. Plays a role as an effector in the TP53-dependent apoptotic pathway.
Subcellular location: Cell junction, desmosome {ECO:0000269|PubMed:15797384, ECO:0000269|PubMed:22515648}. Cell membrane {ECO:0000269|PubMed:15797384, ECO:0000269|PubMed:21285247, ECO:0000269|PubMed:22515648, ECO:0000269|PubMed:25486861, ECO:0000269|PubMed:27834691}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25486861, ECO:0000269|PubMed:27834691}. Note=Associated with desmosomes (PubMed:15797384). May translocate to the intestinal apical epithelial cell surface via sipA and sctB1/sipC-promoted exocytic translocation following infection by S. Typhimurium (By similarity). {ECO:0000250|UniProtKB:Q96FX8, ECO:0000269|PubMed:15797384}.
Interaction partners:
- Desmoplakin
- Plakophilin-1
- Plakophilin-3
- Desmocollin-2
- Cellular tumor antigen p53
- Desmoglein-2
Sequence:
MLRCGLACERCRWILPLLLLSAIAFDIIALAGRGWLQSSNHIQTSSLWWRCFDEGGGSGSYDDGCQSLMEYAWGRAAAATLFCGFIILCICFILSFFALCGPQMLVFLRVIGGLLALAAIFQIISLVIYPVKYTQTFRLHDNPAVNYIYNWAYGFGWAATIILIGCSFFFCCLPNYEDDLLGAAKPRYFYPPA
Protein: Guanylate cyclase soluble subunit alpha-1 (GCS-alpha-1) (EC 4.6.1.2) (Guanylate cyclase soluble subunit alpha-3) (GCS-alpha-3) (Soluble guanylate cyclase large subunit) (P19686)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit beta-2
- cGMP-dependent protein kinase 2
- Nitric oxide synthase 1
- Inosine triphosphate pyrophosphatase
- cGMP-specific 3',5'-cyclic phosphodiesterase
- Guanylate cyclase soluble subunit alpha-2
- High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
- GTP cyclohydrolase 1
- cGMP-dependent 3',5'-cyclic phosphodiesterase
Sequence:
MFCRKFKDLKITGECPFSLLAPGQVPTEPIEEVAGVSESCQATLPTCQEFAENAEGSHPQRKTSRNRVYLHTLAESIGKLIFPEFERLNLALQRTLAKHKIKENRNSSEKEDLERIIAEEAIAAGVPVEVLKDSLGEELFKICYEEDEHILGVVGGTLKDFLNSFSTLLKQSSHCQEAERRGRLEDASILCLDKDQDFLNVYYFFPKRTTALLLPGIIKAAARILYESHVEVSLMPPCFRSECTEFVNQPYLLYSVHVKSTKPSLSPGKPQSSLVIPTSLFCKTFPFHFMLDRDLAILQLGNGIRRLVNKRDFQGKPNFEEFFEILTPKINQTFSGIMTMLNMQFVIRVRRWDNLVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVLIGEQARAQDGLKKRLGKLKATLEHAHQALEEEKKKTVDLLCSIFPSEVAQQLWQGQIVQAKKFNEVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHRESDTHAVQIALMALKMMELSNEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDCPGFVFTPRSREELPPNFPSDIPGICHFLDAYQHQGPNSKPWFQQKDAEDGNANFLGKASGVD
Protein: 18S rRNA (guanine-N(7))-methyltransferase (EC 2.1.1.-) (Bud site selection protein 23 homolog) (Metastasis-related methyltransferase 1) (Williams-Beuren syndrome chromosomal region 22 protein) (rRNA methyltransferase and ribosome maturation factor) (O43709)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:34948388}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25851604}. Cytoplasm {ECO:0000269|PubMed:24488492}. Note=Localized diffusely throughout the nucleus and the cytoplasm (PubMed:24488492). Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604). Localization is not affected by glucocorticoid treatment (PubMed:24488492). {ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Protein LTV1 homolog
- Small ribosomal subunit protein uS5
- Bystin
- Dimethyladenosine transferase
- Pre-rRNA-processing protein TSR1 homolog
- RNA-binding protein NOB1
- Small ribosomal subunit protein uS15
- RNA-binding protein PNO1
- Small ribosomal subunit protein uS12
Sequence:
MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVGLDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAVLQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMSRRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF
Protein: Translation initiation factor IF3-4, chloroplastic (AtIF3-4) (AtINFC-4) (Protein SVR9-LIKE 1) (Q94B52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chloroplast translation initiation factor that is essential for the coordination of leaf and chloroplast development. IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25630975, ECO:0000269|PubMed:27535792}.
Interaction partners:
- Translation initiation factor IF-2
- Peptide chain release factor 1
- Class I peptide chain release factor
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Probable mitochondrial import receptor subunit TOM40-2
- Large ribosomal subunit protein mL45
- 50S ribosomal protein L33
- Small ribosomal subunit protein uS14c
- Large ribosomal subunit protein uL3c
- Small ribosomal subunit protein uS14m
Sequence:
MAGITSTVGFNAILAGATKTVSHPVKSKLFGLRLCVPEFSIVSLSPYHHRRCPAITCRYGGGGGGGSRFPGDRRGRQKESEDDDSLDISAIRSATVRLIDDQQNMIGLVSKEEAVRRAEDAELDLVILSPDADPPVVRMMDYSKYRYEQQKRKKEQQKKTTRMDLKELKMGYNIDQHDYSVRMRAARKFLQDGDKVKVIVNMKGRENEFRNIAIELLRRFQTEIGELGTEESKNFRDRNLFIVLVPNKEVIRKVQEPPPKKKKKPADDKVSAANITATQDI
Protein: feruloyl esterase (EC 3.1.1.73) (Ferulic acid esterase A) (A2R709)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MFSGRFGVLLTALAALSAAAPTPLDVRSVSTSTLDELQLFSQWSAAAYCSNNIDSDDSNVTCTADACPSVEEASTKMLLEFDLTNNFGGTAGFLAADNTNKRLVVAFRGSSTIKNWIADLDFILQDNDDLCTGCKVHTGFWKAWEAAADNLTSKIKSAMSTYSGYTLYFTGHSLGGALATLGATVLRNDGYSVELYTYGCPRVGNYALAEHITSQGSGANFRVTHLNDIVPRLPPMDFGFSQPSPEYWITSGTGASVTASDIELIEGINSTAGNAGEATVDVLAHLWYFFAISECLL
Protein: K Homology domain-containing protein (H2L067)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pumilio domain-containing protein 5
- RNA-binding protein pos-1
- PIP-1
- Zinc finger protein mex-5
- Zinc finger protein mex-6
- Pharynx and intestine in excess protein 1
- CCCH-type zinc finger protein oma-1
- Female germline-specific tumor suppressor gld-1
- CCCH-type zinc finger protein oma-2
- C3H1-type domain-containing protein
Sequence:
MPVVSVRPFSMRNEGFSNGHNTWNDAEFWKPMKEEQIAYKLPGAWYYEEDTASCSPVSDPEDIAQFLNYRTSIGVQNVTESVEVPTSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEDPIFVVTGRLEDVNEAKREIDCAAEHFTQIRASRRHTQGAHAPGQITSYVRVPLRVVGLVVGPKGATIKRIQQDTHTYIITPSREREPVFEVTGLPHNVEAARKEIETHIFQRTGNLPETDNDFAGQLAGVSLMVQKQQQAQQQMQEAQQQSMFYRRAFGNSNPFNQKEMSSSPFGMESSLGLDALLRSFPSMRSSLTPESLSGTGLSSRPSLGGGQSAKQDLPTYDYWGTNNSLNDIMENEILSRKYDALSAWSSMGLEKREESPTNGLMSSLKGTSAGFGLLSTIWSGGNMNLSPGSLASASASPTSSTCDHNDHTLVPING
Protein: Carboxysome assembly protein CcmO (Carbon dioxide concentrating mechanism protein CcmO) (ORF II) (P46205)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Required for formation of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Required for recruitment of major shell protein CcmK2 to the pre-carboxysome. Suggested to be a carboxysome shell protein, but it is not detected in gels, mass spectrometry or by protein sequencing (Probable).
Subcellular location: Carboxysome {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:31048338}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000269|PubMed:22928045}.
Interaction partners:
- Carboxysome shell vertex protein CcmL
- Carboxysome assembly protein CcmM
- Ribulose bisphosphate carboxylase large chain
- Carboxysome shell protein CcmP
- Carboxysome assembly protein CcmN
Sequence:
MSASLPAYSQPRNAGALGVICTRSFPAVVGTADMMLKSADVTLIGYEKTGSGFCTAIIRGGYADIKLALEAGVATARQFEQYVSSTILPRPQGNLEAVLPISRRLSQEAMATRSHQNVGAIGLIETNGFPALVGAADAMLKSANVKLICYEKTGSGLCTAIVQGTVSNVTVAVEAGMYAAERIGQLNAIMVIPRPLDDLMDSLPEPQSDSEAAQPLQLPLRVREKQPLLELPELERQPIAIEAPRLLAEERQSALELAQETPLAEPLELPNPRDDQ
Protein: Hsp90 co-chaperone HCH1 (High-copy Hsp90 suppressor protein 1) (P53834)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ATP-dependent molecular chaperone HSP82
- Hsp90 co-chaperone AHA1
- ATP-dependent molecular chaperone HSC82
- Co-chaperone protein SBA1
- Peptidyl-prolyl cis-trans isomerase CPR6
- Peptidyl-prolyl cis-trans isomerase CYP7
- Hsp90 co-chaperone Cdc37
- Heat shock protein STI1
- Serine/threonine-protein phosphatase T
- TPR repeat-containing protein associated with Hsp90
Sequence:
MVVLNPNNWHWVDKNTLPWSKDYLNGKLTSLSTVSSDGKSKIELTQVSSITGDSNVSQRKGKPICYFDLQLSMNVKVTNLDTNKDDEDDDGILADGKLEIPEFMHDESDIPILSQGFDAFDGLVRSEFVPKVVETLLKYQDDLIKEHSKDIQV
Protein: Tetratricopeptide repeat protein (Q389Z5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSSSSSANDSSSANMDAASGKGIINSPPPGESPDDNSETTAKCSNASDLNSYREFRDQLLSFSLGESAYDYAETLFAKNPSSPEVMALLAETTVLYDKTKNKYARDHWCDRLDLLQRGVDVSRKCINENPEYGPCYRTYVLSATREAEALYYMKSLMGFGLLENYNAIMRRGEKGMELLPTDADIPNALGALSARCAYVWYNPTRLYARWCGVPGWKELWAKSVQLHKRAVENDPANLEFACRLAQAYFHSGDYQNARRWYGKVRDEMPPQDLKDERWQAIAHTHLSTAFVKTSWNVPFA