wanglab/gogpt-training-data huggingface dataset:
Protein: Methylxanthine N3-demethylase NdmB (EC 1.14.13.179) (3-methylxanthine demethylase) (H9N290)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N3-demethylation of theobromine to produce 7-methylxanthine and formaldehyde. Also catalyzes the N3-demethylation of 3-methylxanthine, caffeine, and theophylline to xanthine, paraxanthine, and 1-methylxanthine, respectively. NADH is the preferred substrate.
Interaction partners:
Sequence:
MKEQLKPLLEDKTYLRHFWHPVCTLNEFERANASGHGPMGVTLLGEKLVLARLNSKIIAAADRCAHRSAQLSIGRVCSNAGKDYLECPYHGWRYDEAGACQLIPACPDKSISPRAKISSFDCEVKYDIVWVRLDNSFDCTQIPYLSDFDNPDMQVIVADSYIWETVAERRWENFTDFSHFAFVHPGTLYDPFFASHPTVYVNRVDGELQFKLAPPREMKGIPPEAPMGDFTYRCTMPYSVNLEIKLWKDDSRFVLWTTASPVDNKSCRNFMIIVREKDNQPDHMHLAFQKRVLDEDQPVIESQWPLEIQTSEVSVATDKISVQFRKWHKELSLSAVEGREAFRDSVLTNVIEEEQ
Protein: Spexin prohormone 1 (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1 (Spexin-14)] (F1QQI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in the regulation of food intake and energy metabolism. May also be involved in suppressing the anxiety response by promoting the expression of serotonin-related genes such as fev, tph2 and slc6a4a.
Subcellular location: [Spexin-1]: Secreted {ECO:0000250|UniProtKB:Q9BT56}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9BT56}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q9BT56}.
Interaction partners:
- Galanin receptor 2a
- Galanin receptor 2b
- Galanin receptor type 1
- Golgi transport 1Bb
- Agouti-related neuropeptide.
- FMRFamide related peptide 1
- Pleckstrin homology domain-containing, family A member 6.
- Prolactin-releasing hormone
- Insulin
- Galanin receptor type 1
Sequence:
MKDLRTLAAYALALLLLATFVSHSWSAPKGSFQRRNWTPQAMLYLKGTQGRRFVSEDRNEGDLYDTIRLESRSQNTENLSISKAAAFLLNILQQARDEDEPY
Protein: Alpha-conotoxin EI (P50982)
Organism: Conus ermineus (Agate cone) (Chelyconus ermineus)
Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Probable competitive antagonist of fish muscle acetylcholine receptor. Inhibits postsynaptic nicotinic acetylcholine receptors (nAChRs) from zebrafish (IC(50)=58-100 nM). Blocks mammalian nAChR composed of alpha-1/gamma and alpha-1/delta subunits. Blocks central nervous system nAChR composed of alpha-4-beta-2/CHRNA4-CHRNB2 subunits and peripheral nervous system nAChR composed of alpha-3-beta-4/CHRNA3-CHRNB4 subunits. Low toxin concentrations potentiate currents in muscle nAChR composed of alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHRND) subunits and central nervous system nAChR composed of alpha-4-beta-2/CHRNA4-CHRNB2 subunits, but not peripheral nervous system nAChR composed of alpha-3-beta-4 subunits. Also exhibits inhibition of D.melanogaster alpha-7/CHRNA7 nAChRs. Has possibly a distinct nAChR binding mode from other alpha-conotoxins, due to a different three residue motif (lacks the Ser-Xaa-Pro motif) (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:28238803, ECO:0000269|PubMed:7578057}.
Interaction partners:
Sequence:
MFTVFLLVVLATTVGSFTLDRASDGRDAAANDKASDLIALTARRDPCCYHPTCNMSNPQICG
Protein: Ras-specific guanine nucleotide-releasing factor 1 (Ras-GRF1) (Guanine nucleotide-releasing protein) (GNRP) (P140 Ras-GRF) (P28818)
Organism: Rattus norvegicus (Rat)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Interaction partners:
- GTPase HRas
- Glutamate receptor ionotropic, NMDA 2B
- GTPase NRas
- Calmodulin-like protein 3
- Calmodulin-1
- Calmodulin-like protein 4
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MQKAIRLNDGHVVSLGLLAQRDGTRKGYLSKRSSDNPKWQTKWFALLQNLLFYFESDSSSRPSGLYLLEGSICKRMPSPKRGTSSKESDKQHHYFTVNFSNDSQKSLELRTDDSKDCDEWVAAIARASYKILATEHEALMQKYLHLLQVVETEKTVAKQLRQQLEDGEVEIERLKAEIANLIKDNERIQSNQLVAPEDEDSDIKKIKKVQSFLRGWLCRRKWKNIIQDYIRSPHADSMRKRNQVVFSMLEAEAEYVQQLHILVNNFLRPLRMAASSKKPPITHDDVSSIFLNSETIMFLHQIFYQGLKARIASWPTLVLADLFDILLPMLNIYQEFVRNHQYSLQILAHCKQNRDFDKLLKQYEAKPDCEERTLETFLTYPMFQIPRYILTLHELLAHTPHEHVERNSLDYAKSKLEELSRVMHDEVSETENIRKNLAIERMITEGCEILLDTSQTFVRQGSLIQVPMSEKGKINKGRLGSLSLKKEGERQCFLFSKHLIICTRGSGSKLHLTKNGVISLIDCTLLDDPENMDDDGKGQEVDHLDFKIWVEPKDSPPFTVILVASSRQEKAAWTSDIIQCVDNIRCNGLMMNAFEENSKVTVPQMIKSDASLYCDDVDIRFSKTMNSCKVLQIRYASVERLLERLTDLRFLSIDFLNTFLHSYRVFTDAVVVLDKLISIYKKPITAIPARSLELLFSSSHNTKLLYGDAPKSPRASRKFSSPPPLAIGTSSPVRRRKLSLNIPIITGGKALELASLGCPSDGYTNIHSPISPFGKTTLDTSKLCVASSLTRTPEEIDMTTLEESSGFRKPTSDILKEESDDDQSDVDDTEVSPPTPKSFRNRITQEFPLFNYNSGIMMTCRDLMDSNRSPLSATSAFAIATAGANESPANKEIYRRMSLANTGYSSDQRNIDKEFVIRRAATNRVLNVLRHWVTKHSQDFETDDLLKYKVICFLEEVMHDPDLLPQERKAAANIMRTLTQEEITENHSMLDELLLMTEGVKTEPFENHSAMEIAEQLTLLDHLVFKSIPYEEFFGQGWMKADKNERTPYIMKTTRHFNHISNLIASEILRNEEVSARASTIEKWVAVADICRCLHNYNAVLEITSSINRSAIFRLKKTWLKVSKQTKSLFDKLQKLVSSDGRFKNLRETLRNCDPPCVPYLGMYLTDLAFLEEGTPNYTEDGLVNFSKMRMISHIIREIRQFQQTTYKIEPQPKVTQYLVDETFVLDDESLYEASLRIEPKLPT
Protein: Heavy metal-responsive transcription factor-1 (Q9NFS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNDQEKQHQQQQQHYFHSEWKTTANSHGNSLSDSRDYDTNSSRNSLSGSPPVTSNCSSSGSLDFDRPLAQLLEPKLEADGLGIIHGDNYSIYGSQTAESTSGEQQSSDEALSRYRCNYENCYRSYSTIGNLRTHLKTHTGDYSFKCPEDGCHKAFLTSYSLKIHVRVHTKVKPYECEVSGCDKAFNTRYRLHAHLRLHNGETFNCELCQKCFTTLSDLKKHMRTHTQERPYKCPEDDCGKAFTASHHLKTHRRTHTGEKPYPCQEDSCQKSFSTSHSLKSHKKTHQRQLQNKGRKKRPLKTQQTKCSDQEQKDPQQEEQEEEEFIKEDQPEMTLLNPGSHCSETTSTDSGVVLQTLTPQDHLSNVFILQGNEPLILPETSQAYQLSYAAEEEIPSPWIDAGVLVSKPIIPMAPLTDACVALPTEMPSFVNLKPTFGNAVSGNMGDPQPETMDVDPTVETSLPTPTLELNQPNIEELLKQDSFENEEDMETESLLNDILMTIDNNSALLQATLQQASQVPSDASGLVELDIRDNKPTLKQITADAGICNCTNCKCDQTKSCHGGDCGAAAAQQATRTGAPTTTTTTTTMNSSGGKRICGSVVPTKKVSKRETEMNQNIEDVALLLQNLASMSSGGSSGGGGGCCGGGAVKPAPSGGGCCGEPKAPKPVNNGCGCARPSAPSSAGCCGSGVASTPKPTGGCCSGNQKPAPTATTASSPSCCCSGKGEVQEPPVISSASSAPAAAVKGNACTCKSPAEGVANGCCVVICIKTLQALRKVLTRRNLNLMLCPQQN
Protein: Triacylglycerol lipase OBL1 (EC 3.1.1.-) (Oil body lipase 1) (AtOBL1) (F4JFU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acid lipase that can hydrolyze a range of triacylglycerols without a clear preference for acyl-chains. Can also cleave 1,2-diacylglycerol, 1,3-diacylglycerol and 1-monoacylglycerol, but not phospatidylcholine, phosphatidylethanolamine, or sterol esters. Required for pollen tube growth. Triacylglycerol hydrolysis by OBL1 may provide acyl groups for the synthesis of membrane lipids in growing pollen tubes (Probable).
Subcellular location: Lipid droplet {ECO:0000269|PubMed:29178188}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=Associates with the oil body membrane. {ECO:0000305|PubMed:29178188}.
Interaction partners:
- Triacylglycerol lipase SDP1L
- Triacylglycerol lipase 1
Sequence:
MHKDNDSGSGSNPGQVSNYLIVRPHRGGYIDLFRYGVRDDQTSKAKFLEMPDNREWSTITIDEEAEDHRWVIVVSILVRKIIRLLRTPMEFTGFVVDFFLNLFSANGGFFGLLLRLIQAKVVIPERGSVTFVSTIGQLDGRISLYKEWNFVEHLEGIDSVDSGRVKIELGSRGLMDLCVMASKLAYENAKVVENVVDLHWKMNLVEFLDCWNDYQKQMSTQVFVFTDKQKDANLIVISFRGTEPFDADDWGTDFDYSWYEVPNVGKLHMGFLEAMGLGNRDDTTTFHYNLFEQTSSEEENSKKNLLDMVERSAYYAVRVILKRLLSEHENARFVVTGHSLGGALAILFPTLLVLNEETEIMKRLLGVYTFGQPRIGNREVGLFMKAQLNQPVDRYFRVVYCNDIVPRLPYDDKTFLYKHFGLCLFYDSFYNETKAEDEPDPNPYGLRYKILGHVIAVWELVRGLTMGYTHGPDYKEGWFRILFRLMGLVIPGLSDHCMTDYVNSVRLGPDNELQMSSL
Protein: Regulator of nonsense transcripts 2 (Up-frameshift suppressor 2 homolog) (Upf2) (A2AT37)
Organism: Mus musculus (Mouse)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HAU5}. Cytoplasm {ECO:0000269|PubMed:27149095}.
Interaction partners:
- Serine/threonine-protein kinase SMG1
- UPF3 regulator of nonsense transcripts homolog A
- Regulator of nonsense transcripts 1
- UPF3 regulator of nonsense transcripts homolog B
- RNA-binding protein with serine-rich domain 1
- Telomerase-binding protein EST1A
- RNA-binding protein 8A
- Serine/arginine repetitive matrix protein 1
- Protein CASC3
- RNA-binding protein 8A
Sequence:
MPAERKKSASMEEKESLLNNKEKDCSERRPVSSKEKPRDDLKVTAKKEVSKVPEDKKKRLEEDKRKKEDKERKKKEEEKVKAEEELKKKEEEEKKKQEEEERKKQEEQAKRQQEEAAAQLKEKEESLQLHQEAWERHQLRKELRSKNQNAPDNRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKLSDVNCAAHLCSLFHQRYSDFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKSIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSQNKDSNKDDSKEAKEPKDNKEASSPDDLELELENLEINDDTLELEGADEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVRKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKESKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSEEEEEGEEEEEENTDYLTDSNKENETDEENAEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGETESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR
Protein: Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (Extracellular mutant protein 40) [Cleaved into: Arginine biosynthesis bifunctional protein ArgJ alpha chain; Arginine biosynthesis bifunctional protein ArgJ beta chain] [Includes: Glutamate N-acetyltransferase (GAT) (EC 2.3.1.35) (Ornithine acetyltransferase) (OATase) (Ornithine transacetylase); Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS)] (Q04728)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03124, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Protein ARG5,6
- Amino-acid acetyltransferase, mitochondrial
- Acetylornithine aminotransferase, mitochondrial
- Ornithine carbamoyltransferase
- Argininosuccinate synthase
- Argininosuccinate lyase
- Arginase
- Alanine aminotransferase, mitochondrial
- Inactive alanine aminotransferase
- NADP-specific glutamate dehydrogenase 1
Sequence:
MRISSTLLQRSKQLIDKYALYVPKTGSFPKGFEVGYTASGVKKNGSLDLGVILNTNKSRPSTAAAVFTTNKFKAAPVLTSKKVLETARGKNINAIVVNSGCANSVTGDLGMKDAQVMIDLVNDKIGQKNSTLVMSTGVIGQRLQMDKISTGINKIFGEEKFGSDFNSWLNVAKSICTTDTFPKLVTSRFKLPSGTEYTLTGMAKGAGMICPNMATLLGFIVTDLPIESKALQKMLTFATTRSFNCISVDGDMSTNDTICMLANGAIDTKEINEDSKDFEQVKLQVTEFAQRLAQLVVRDGEGSTKFVTVNVKNALHFEDAKIIAESISNSMLVKTALYGQDANWGRILCAIGYAKLNDLKSLDVNKINVSFIATDNSEPRELKLVANGVPQLEIDETRASEILALNDLEVSVDLGTGDQAAQFWTCDLSHEYVTINGDYRS
Protein: NAC domain-containing protein 69 (ANAC069) (Protein NAC WITH TRANSMEMBRANE MOTIF 2) (Protein NTM1-like 13) (Q9M126)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP). Involved in salt stress response during seed germination and seedling growth. Binds the auxin-responsive IAA30 gene promoter and may serve as a molecular link that interconnects a developmental feedback loop of auxin signaling with a salt signal transduction pathway during seed germination.
Subcellular location: Membrane {ECO:0000269|PubMed:21450938}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:21450938}. Note=Localized primarily in plasma membrane or endoplasmic reticulum membrane as dormant form and, upon specific stress or signal, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:21450938}.
Interaction partners:
- glucan endo-1,3-beta-D-glucosidase
- Auxin-responsive protein IAA30
- Dof zinc finger protein DOF5.8
Sequence:
MVKDLVGYRFYPTGEELINHYLKNKILGKTWLVDEAISEINICSYDPIYLPSLSKIKSDDPVWYFFCPKEYTSAKKKVTKRTTSSGYWKATGVDRKIKDKRGNRGEIGIKKTLVYYEGRVPKGVWTPWVMHEYHITCLPQDQRNYVICQVMYKGEDGDVPSGGNNSSEPSQSLVSDSNTVRATSPTALEFEKPGQENFFGMSVDDLGTPKNEQEDFSLWDVLDPDMLFSDNNNPTVHPQAPHLTPNDDEFLGGLRHVNREQVEYLFANEDFISRPTLSMTENRNDHRPKKALSGIIVDYSSDSNSDAESISATSYQGTSSPGDDSVGSSNRQFLQTGGDEILSSCNDLQTYGEPSISSSTRQSQLTRSIIRPKQEVKQDTSRAVDSDTSIDKESSMVKTEKKSWFITEEAMERNRNNPRYIYLMRMIIGFILLLALISNIISVLQNLNPAMKFDRER
Protein: RING-type domain-containing protein (Q38C61)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin, putative
- Cullin 1, putative
- Elongin-C
- DNA damage-binding protein 1
- Ubiquitin-conjugating enzyme E2, putative
- COP9 signalosome complex subunit 4
- S-phase kinase-associated protein, putative
- SKP1 component dimerisation domain-containing protein
- 50S ribosomal protein L2, putative
- TATA-binding protein interacting
Sequence:
MEEAAAEGMPLSQEQGEQKRFVLKRWNAVALWSWDIEVDTCAICRNHVMDLCIECQASSNGPRTNCNIAWGVCNHAFHTHCISRWLKTRNVCPLDNKEWSYQKLGV
Protein: Glycine cleavage system P protein (EC 1.4.4.2) (A0A8I6AP64)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
Interaction partners:
Sequence:
MSFSGQERLGLDTVFCFPSRVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRKRFFIDPRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCGCSLKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQAQGYQQLFQELEKDLCELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLVPFLPSHPIVCLKPNEDTWPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKEATEIAILNANYMAKRLERYYRVLFRGARGYVAHEFILDTRPFKKSANIEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSRWDRPYSREVAAFPLPFVKPENKFWPTIARIDDIYGDQHLVCTCPPMEVYESPFSEQKRASS
Protein: CD59B glycoprotein (Cocaine-and amphetamine-regulated transcript protein-like 2) (Lymphocyte antigen 97, tandem duplicate 2) (A0A0G2L893)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zinc finger Ran-binding domain-containing protein 2
- MAC-inhibitory protein
Sequence:
MMKVLLLALVLALVFADGSALKCYNCVPNVPGGSCVTKEETCGYKKDTCVSARFTSPPFGYFRRCISMADCMILQSSTSIKAKCCQTDLCNTPII
Protein: Oligopeptide transporter, putative (Q4WD14)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLDKMGRLSVFNRKRRAADGTTPSAGSNESLSPPATAAPLNDAEKIKPVSETAAIEQETEQDPEVAALPLEVRQLVSLTDDPTLPTITCRYFLLSLLFVVPGAFLSQMSHYRTTQAPYSVFFVQIACHYVGHFLARWLPAWTIRIPLTKWAFSLNPGPWSIKEHVLVTLTAASGATYNLGYAPISMAELFYGERVHPAVAIFFMFAIVWIGYAFAAIARQILLYDPAFIWPQALMQTTLFETFRKQDTSSPLAKRQMKIFFFSLLGMTLWQFLPEYVFPFTSSLAFLCWVAPRNPVANFIGSGMGGMGFLNLSLDWSNINWNGSSILLTPWWTQVVLFLAFAFNCWVLLPAAKWGNLGSYKHGLMSNSLLTTNGTKYPILDLLTPDFRLNQTAYEEIGPMYMGLQNVWATFFDYAKVTASVAWVATFGYSQVKGNLLKMFRSRDKTSQTKGEGINHQYTDRLNVLQRSYQEVPLWWYLVLFMAGFIILIVSIACGYLWIPIWTVFVALGSAAALVLPFAFLYAVSNYQLAVGSFNELIYGYMVHTKAGEGHRHPCGPSTYGSIAGDAWYRAQYMLQDQKIGHYMHIPPRTVFFSQVFGTVLGIPMNYAVMRWVLSTKRDVLTGAKPDPLHQWTGQSLISSNTLGVQYAVIGPAELFKQSEMRPLPWSFLLGALLPPVLYGLHRLLPRWRIDLWNVSIFFSGLAVFYGNLSTGYTSAIIGGYVVMYWAYRKRFEVWKRYSYMIAAAFDAGFNLNMLLIFLFFGSGKQISMPNWWGNNPDSVERCFALD
Protein: Calpain-2 catalytic subunit (EC 3.4.22.53) (80 kDa M-calpain subunit) (CALP80) (Calcium-activated neutral proteinase 2) (CANP 2) (Calpain M-type) (Calpain-2 large subunit) (Millimolar-calpain) (M-calpain) (O08529)
Organism: Mus musculus (Mouse)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (By similarity). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250}.
Interaction partners:
- Calpain small subunit 1
- Calpastatin
- Talin-1
- Calpain-1 catalytic subunit
- Talin-2
- Caspase-12
- BH3-interacting domain death agonist
- Apoptosis regulator BAX
- Bcl-2 homologous antagonist/killer
- Interleukin-1 alpha
Sequence:
MAGIAIKLAKDREAAEGLGSHERAIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGYKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPPDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPNLFKIIQKALEKGSLLGCSIDITSAADSEAVTYQKLVKGHAYSVTGAEEVESSGSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFWMSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGERGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLGKNFFLTTRARERSDTFINLREVLNRFKLPPGEYVLVPSTFEPHKDGDFCIRVFSEKKADYQAVDDEIEANIEEIDANEEDIDDGFRRLFVQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIQLNLASWLSFSVL
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Inositol polyphosphate 3-phosphatase) (Q9Y0B5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MANTISLMSNVIRNVVSKKRIRYKEKGYDLDLTYINDNIIAMGYPAPDKLEGLFRNRLEDVFKLLEENHAQHYKIYNLCSERSYDVAKFRGRVAVYPFDDHNPPTIELIQRFCSDVDMWLKEDSSNVVAVHCKAGKGRTGTMICAYLVFSGIKKSADEALAWYDEKRTKDRKGVTIPSQRRYVQYFSKLVCSSVPYSKVSLNVCEIRFSESSCVQNLGMVECSISVLHDSATENAKPDRLKTLPIDFQKSFVLTIKPSIPVSGDVKFELTKKSPDKIICHFWLNTFFVRNYSPCESDGTVNKYIHTLSKSEIDDVHKDSEHKRFSEEFKISIVFEAENFSNDVQAEASEKERNENVLNFERSDYDSLSPNCYAEKKVLTAIVNDNTTKSQTIETLDHKDIVTKIQYDTSTNSKNTSTACKRKQPNSKTLLPSLNDSTKEEIKRNHIFNQPSIKKTDLIKWQNSEVHITRSINENKNINYNSYITCKQSSPKFNCGTEDGEEDWESGESTYL
Protein: Tudor and KH domain-containing protein homolog (Partner of PIWIs protein) (Q9VQ91)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the piwi-interacting RNA (piRNA) metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons which is essential for germline integrity. Likely to act by recruiting Piwi proteins such as AGO3 and piwi to the piRNA biogenesis machinery in the nuage. Required for the final steps of primary piRNA biogenesis by participating in the 3' end-trimming of piwi-bound intermediates into mature piRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21447556}. Nucleus {ECO:0000269|PubMed:21447556}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:21447556}. Note=Component of the perinuclear meiotic nuage (also known as germline granule or P granule), a germline-specific membraneless ribonucleoprotein biocondensate involved in post-transcriptional regulation of transposons and mRNAs (PubMed:21447556). Expressed in the cytoplasm of germline stem cells, cyst cells, nurse cells and oocytes, with strong accumulation in region IIb germline cysts in the germarium (PubMed:21447556). In post-germarium egg chambers accumulates in the perinuclear loci that appear to be the nuage (PubMed:21447556). {ECO:0000269|PubMed:21447556}.
Interaction partners:
- Protein piwi
- Protein aubergine
- Staphylococcal nuclease domain-containing protein 1
Sequence:
MLRNTPFGATPTYKLLLGFGLCSLGGAMLYAYFKTRNDEEEADSGGQRPASGIRGQTEEQKPQKEVCLKIVVDNEHVPLIMGRGGSNIKLIEEKTLAKIRLRDKDSGHKFCDISGVPDAVKAARALLIKEIERAPVVKVELQVPQRLASKINGRGGELLQEIRSSSLAKLNIDLNGRNGKAKITIIGNQKQVNIARKMLDDQIEEDEELVRSMEEVEQRREPRRSPTNSIASSMYSSQTSLSSHTQPRDKLMASKGEGKPMEVYVSAVASPTKFWVQLIGPQSKKLDSMVQEMTSYYSSAENRAKHVLTAPYVGQIVAAVFKFDEKWYRAEIVDIMPNQYNPKEQVIDLYFVDYGDSEYISPADICELRTDFLTLRFQAVECFLANVKSTIQTEPITWPKSSIAKFEELTEVAHWRKLIARVVTYKERPRATTAVSAAAKEGTPLPGVELFDPADNSELNIADLMITQGFALPLDDSYPVRSRSSTPSSNSDSTIEELCVSNPVTPLTPHSPMSMSIDVDSITQAENEHLAQQLQHLQHKLNGNDIKNINPAKLTATDLENGNNNNASTTNGASAH
Protein: Mitochondrial ribosomal protein S22 (G5E9W7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDEEVQSILTKMTGLNLQKTFKPAIQELKPPTYKLMTQAQLEEATRQAVEAAKVRLKMPPVLEERVPINDVLAEDKILEGTETTKYVFTDISYSIPHRERFIVVREPSGTLRKASWEERDRMIQVYFPKEGRKILTPIIFKEENLRTMYSQDRHVDVLNLCFAQFEPDSTEYIKVHHKTYEDIDKRGKYDLLRSTRYFGGMVWYFVNNKKIDGLLIDQIQRDLIDDATNLVQLYHVLHPDGQSAQGAKDQAAEGINLIKVFAKTEAQKGAYIELTLQTYQEALSRHSAAS
Protein: Sodium-potassium/proton antiporter ChaA (Na(+)/H(+) exchanger) (P31801)
Organism: Escherichia coli (strain K12)
Function: Sodium exporter that functions mainly at alkaline pH. Can also function as a potassium/proton and calcium/proton antiporter at alkaline pH. Does not play a major role in calcium export. The K(+)/H(+) antiporter activity may enable E.coli to adapt to K(+) salinity stress and to maintain K(+) homeostasis.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Na
- Na
- Putative cation transport regulator ChaB
- Probable L,D-transpeptidase YcfS
- Multidrug resistance protein MdtA
- Periplasmic chaperone Spy
Sequence:
MSNAQEAVKTRHKETSLIFPVLALVVLFLWGSSQTLPVVIAINLLALIGILSSAFSVVRHADVLAHRLGEPYGSLILSLSVVILEVSLISALMATGDAAPTLMRDTLYSIIMIVTGGLVGFSLLLGGRKFATQYMNLFGIKQYLIALFPLAIIVLVFPMALPAANFSTGQALLVALISAAMYGVFLLIQTKTHQSLFVYEHEDDSDDDDPHHGKPSAHSSLWHAIWLIIHLIAVIAVTKMNASSLETLLDSMNAPVAFTGFLVALLILSPEGLGALKAVLNNQVQRAMNLFFGSVLATISLTVPVVTLIAFMTGNELQFALGAPEMVVMVASLVLCHISFSTGRTNVLNGAAHLALFAAYLMTIFA