wanglab/gogpt-training-data huggingface dataset:
Protein: Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX [Includes: Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS); Phosphatidylglycerol lysyltransferase (EC 2.3.2.3) (Lysylphosphatidylglycerol synthetase) (LPG synthetase)] (P9WFU7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Isoleucine--tRNA ligase
- Lysine--tRNA ligase 1
- Glutamate--tRNA ligase
- GMP synthase
- Leucine--tRNA ligase
- tRNA
- Proline--tRNA ligase
- Methionine--tRNA ligase
- Serine--tRNA ligase
- Peptide chain release factor 2
Sequence:
MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSLGYFATRRDKSVVFASSGRACITYRVEVGVCLASGDPVGDHRAWPQAVDAWLRLCQTYGWAPGVMGASSQGAQTYREAGLTALELGDEAILRPADFKLSGPEMRGVRQAVTRARRAGLTVRIRRHRDIAEDEMAQTITRADSWRDTETERGFSMALGRLGDPADSDCLLVEAIDPHNQVLAMLSLVPWGTTGVSLDLMRRSPQSPNGTIELMVSELALHAESLGITRISLNFAVFRAAFEQGAQLGAGPVARLWRGLLVFFSRWWQLETLYRSNMKYQPEWVPRYACYEDARVIPRVGVASVIAEGFLVLPFSRRNRVHTGHHPAVPERLAATGLLHHDGSAPDVSGLRQVGLTNGDGVERRLPEQVRVRFDKLEKLRSSGIDAFPVGRPPSHTVAQALAADHQASVSVSGRIMRIRNYGGVLFAQLRDWSGEMQVLLDNSRLDQGCAADFNAATDLGDLVEMTGHMGASKTGTPSLIVSGWRLIGKCLRPLPNKWKGLLDPEARVRTRYLDLAVNAESRALITARSSVLRAVRETLFAKGFVEVETPILQQLHGGATARPFVTHINTYSMDLFLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHADYLEWIDGCRELIQNAAQAANGAPIAMRPRTDKGSDGTRHHLEPVDISGIWPVRTVHDAISEALGERIDADTGLTTLRKLCDAAGVPYRTQWDAGAVVLELYEHLVECRTEQPTFYIDFPTSVSPLTRPHRSKRGVAERWDLVAWGIELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGIDRVVMLITGRSIRETLPFPLAKPH
Protein: Ferritin (A0A0B4KHF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ferritin
- Ferritin
- Protein Malvolio
- Transferrin
Sequence:
MKFFVALALFACLGSLALAKDDEYCQNTVITACSTSAFSALTGFFTGKTNSICNARFAGIDHIEPEIQSYINANLAKSYDYLLLATHFNSYQKNRPGFQKLYQGLSDRSFEDSIALIKQVTRRGGIVDFNTRHESSGSVSTKRGTLEVDELHSLALALDTEKQLATGATHVHSRATHATDAERDPELAHYFEENFLGKQAESVRKLSGYANDLAKLMKVPDPSLSVYLFDEYLQKQ
Protein: Tetraspanin-12 (Q22495)
Organism: Caenorhabditis elegans
Function: Together with tsp-14, regulates cell fate specification in the postembryonic mesodermal M lineage, body size and male development, probably by positively modulating BMP-like Sma/Mab signaling. May regulate BMP-like Sma/Mab signaling by mediating protease sup-17 trafficking to the cell surface. Together with tsp-14, probably acts by modulating the activation of glp-1, a Notch-like receptor, to regulate germline maturation. Probably acts by modulating the activation of lin-12, a Notch-like receptor, to regulate cell fate specification such as the anchor cell/ventral uterine precursor cell decision.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28068334}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28068334}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Early endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Late endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Recycling endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Note=Often in close juxtaposition to the retromer but not part of it, suggesting separate microdomains of the same endosome. {ECO:0000303|PubMed:31988138}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 10 homolog
- Tetraspanin
- Tetraspanin
- Tetraspanin
Sequence:
MANRRQPVQHRAQQRVYRQSQIRYAPGAGGESEISCCVKYSVFSFNVIFFLLGFGLLLFGVWAQIEKNTFVNMLSKASKLYLDPTWPLLIVGFLTFIIGFSGCVGSLRENTSFLTFYSTLLGLLLIAEFSAGVFAYACRDQLDNYIRNLLNDVVVGYRDDPDLQLLIDSMQETWMCCGINGADDWDRNTYFSIEAREVASPEAGGVPFSCCINSSKLEFKNYFCGHGVRLKPESHMAAHLAAQRVMAHTASIYTEGCLPKLQLWLNNNMLLVAVSMVIIAIIQVLGICFAQNLKSDILAQRAKWYYTH
Protein: ETS variant transcription factor 4 (cDNA FLJ55351, highly similar to ETS translocation variant 4) (B7Z5F4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MERRMKAGYLDQQVPYTFSSKSPGNGSLREALIGPLGKLMDPGSLPPLDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENLAFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSSVFQQPLDICHSFTSQGGGREPLPAPYQHQLSEPCPPYPQQSFKQEYHDPLYEQAGQPAVDQGGVNGHRYPGAGVVIKQEQTDFAYDSDVTGCASMYLHTEGFSGPSPGDGAMGYGYEKPLRPFPDDVCVVPEKFEGDIKQEGVGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELAGPAQPFGPKGGYSY
Protein: F-box and associated interaction domains-containing protein (B3H7F2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVRDIVDDPLDEDDIALVKTYGLVPYSAPIKKVEKEIKELTEKINDLCGIKESDTGLAPLSKQMMQEGQPLQVGYVSCFRYIPIDLLMDIFSRVPAKSIARFRCVSKLWESILCRPDFKELFMTMSSIRPPLLLFTFQDDDGNLFFFSSPHPQIPCNENTSLVPTRYHVQHTTDSFSEIGSPLCGFICRRGKRNLDTMVICNPVTGESVSLPKVELKSINTETRPYLGYDPVRKQLKVLCIKSDDIPNTCDEHQVLTLENGNHLWRTIQCKPHYPKSDGICIDGILYYTAGFDMRARVSMVVCFDVRSEKFSFINIHVFMLMNDSCTLINYKGKLGALQFTCLSPKRLRFWVLVNAEKNIWTKCIYALPPLWNNLVQHTELAIVGMTDGGEVVLSQYCLIYAFYIYYFNLESKSLTRVQIQDVEMFKRTRVYTSLGYVENFKLMTDYDRGFNTFSPQGRLF
Protein: Protein phosphatase 1F (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) (Partner of PIX 2) (Q9WVR7)
Organism: Rattus norvegicus (Rat)
Function: Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type 1
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
Sequence:
MASGAPQNSSQMACDGEIPGFLDTLLQDFPAPLSLESPLPWKVPGTVLGQEEVEAELTELAMGFLGSRNAPPAVAAAVTHEAISQLLQTDLSEFKRLPEQEEEEEEEEERVLTTLLDAKGLSRSFFNCLWEVCSQWQKRVPLTAQAPQRKWLVSIHAIRNTRRKMEDRHVSLPAFNHLFGLSDSVHRAYFAVFDGHGGVDAARYASVHVHTNASHQPELLTDPAAALKEAFRHTDQMFLQKAKRERLQSGTTGVCALITGAALHVAWLGDSQVILVQQGQVVKLMEPHKPERQDEKSRIEALGGFVSLMDCWRVNGTLAVSRAIGDVFQKPYVSGEADAASRELTGLEDYLLLACDGFFDVVPHHEIPGLVHGHLLRQKGSGMHVAEELVAVARDRGSHDNITVMVVFLRDPLELLEGGGQGAGGAQADVGSQDLSTGLSELEINTSQRS
Protein: Small GTP-binding protein sar1 (Q8I1S0)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- Protein transport protein SEC31
- Protein transport protein SEC23
- Guanine nucleotide-exchange factor SEC12
- Protein transport protein Sec24A
- Protein transport protein SEC13
- Protein transport protein Sec24B, putative
- Merozoite surface protein 4
Sequence:
MFIINWFRDILAHLGLSQKSARILFLGLDNAGKTTLLHMLKDDRVAQHVPTLHPHSEELVVGKIRFKTFDLGGHETARRIWRDYFAAVDAVVFMIDTTDRSRFDEAREELRHLLETEELSNVPFVVLGNKIDKPDAASEDELRQHLNLFSNITVHNNMKGGSGVRPVELFMCSVIRRMGYAAAFKWISQFLT
Protein: Probable E3 ubiquitin-protein ligase RHY1A (EC 2.3.2.27) (RING-H2 finger Y1a) (RING-H2 zinc finger protein RHY1a) (RING-type E3 ubiquitin transferase RHY1A) (Q852U6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Interaction partners:
- Probable protein phosphatase 2C 33
- AT4G01090 protein
- E3 ubiquitin-protein ligase UPL4
- SBP family protein
- Putative E3 ubiquitin-protein ligase XBAT31
- Small ribosomal subunit protein eS4z
- ERAD-associated E3 ubiquitin-protein ligase HRD1A
- Proliferating cell nuclear antigen 2
- Probable beta-D-xylosidase 7
- Protein POLYCHOME
Sequence:
MTSASELFSTRRSRPGRSDPALESDTSSYRHHSHHHHRRHGVHHHNQRHDSDGCDPLRRPTPRLRRFFHHPIQERSRPIRDVQGTSQYLNTDSTDTETQSSSFVNLNGSERLPGAVLLARDRLFERLRGVSLSSNSRSNRVSLDDQRESSFHSIDGDPIFQLAGLQVTYECNKKPQGLTQDAINCLHRQTFSSAEVKSEMRDCSICLESFTKGDMLISLPCTHSFHSSCLNPWLRACGDCPCCRRAIAKE
Protein: F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5) (Q9QXW2)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate-specific adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the polyubiquitination and subsequent degradation of TSC2. May also act as a negative regulator of MAP3K7/TAK1 signaling in the interleukin-1B (IL1B) signaling pathway. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication (By similarity). The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes required to allow mitotic progression.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q969U6}.
Interaction partners:
- DNA damage-binding protein 1
- S-phase kinase-associated protein 1
- Cullin-4A
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Cullin-4B
- Protein transport protein Sec23B
- DDB1- and CUL4-associated factor 1
- Denticleless protein homolog
- Tuberin
Sequence:
MDEGGLPLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWKEQFYRYYQVARDVPRHPAATSWYEEFRRLYDMVPCVEVQTLKEHTDQVLHLSFSHSGYQFASCSKDCTVKIWNNDLTISLLHSADMRPYNWSYTQFSQFNQDDSLLLASGVFLGPHNSSSGEIAVISLDSFALLSRVRNKPYDVFGCWLTETSLISGNLHRIGDITSCSVLWLNNAFQDVESENVNVVKRLFKIQNLNASTIRTVMVADCSRFDSPDLLLDASDQAGLPCRVFDLGGDTEEEATDPGLHTSGSDHVKKGLRRVFDSVLDGHGQLSDCALETKVAELLAQGHTKPPECNDADTRNKYLIFTTGCLTYSPHQIGIKQILPHQMTTAGPVLGEGRGSDAFFDALDHVIDVHGHIIGMGLSPDNRYLYVNSRAWPPGSVVADPMQPPPIAEEIDLLVFDLKTMREVKRALRAHRAYTPNDECFFIFLDVSRDFVASGAEDRHGYIWDRHYNICLAKLRHEDVVNSVAFSPQEQELLLTASDDATIKAWRSPRIVRVLQAPRPRPRPRPRPFFSWFASHRR
Protein: Gamma-aminobutyric acid receptor subunit beta-2 (GABA(A) receptor subunit beta-2) (GABAAR subunit beta-2) (P47870)
Organism: Homo sapiens (Human)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor and the alpha2/beta2/gamma2 receptor exhibit synaptogenic activity. Functions also as histamine receptor and mediates cellular responses to histamine (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P63138}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cell membrane {ECO:0000269|PubMed:19763268, ECO:0000269|PubMed:8264558}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P63138}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-3
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid receptor subunit beta-1
- Huntingtin-associated protein 1
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Succinate-semialdehyde dehydrogenase, mitochondrial
- Gamma-aminobutyric acid receptor subunit gamma-1
Sequence:
MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAASANNEKMRLDVNKIFYKDIKQNGTQYRSLWDPTGNLSPTRRTTNYDFSLYTMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN
Protein: Selectin P (p-selectin) (E5DV48)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Si:dkey-261h17.1
- von Willebrand factor
- CD44 antigen
- Vascular cell adhesion molecule 1b
- Sorting nexin-17
- CD44 antigen
- Glucose-6-phosphate isomerase
- Integrin, alpha 2b
- Golgi glycoprotein 1a.
- P-selectin glycoprotein ligand 1 precursor
Sequence:
MVLLVHITLFSGSLVFMTGMYNVNAWTYHYNIDSKLDWTAARQWCQTHFTDMVAIQNQAEIAYLNEILPFHRAYYWIGIRKIDGHWTWVGTKKRLTVEAANWATNEPNNQGTGEDCVEIYIKRNKDTAKWNDERCSKKKATVCYLASCTEISCSEHARCVETIGNYTCQCDAGFMGPRFVQCQPVENPQQGLVKCDGAFGEFNFNSSCQFQCATGFNLVGAERIHCLTTGHWNDTLPVCQAVKCQAIIDAPRGWTMICTHPLSMNSFNSSCEFECKEGFELNGSKTTWCDHTGHWTDKAPTCTVVTCNPLLAPANSSLACADPLGKSSFRSSCNVTCDEGYKLRGRAALTCQREGNWSAPLPVCEVVKCDSLKPIANGSYQCHDSVDEFSYGSTCWFKCDSGFVHNGTNSTHCTKQGNWSHISPICHAVQCPPLSDTPKYGSVSCVHPLSTNSYNSSCEFKCEEGLVLRGTDSTHCDHTGHWTNTAPICTAVACDPLVTPVNSNLTCANPLGKFSFRTSCEVICEVGYKLRGDTTLNCLSNGNWSAPTPACKVIRCEALESVHHGSVHCHDLLEEFSYGSECWLECEAGFTLNGTNSTYCTSQGKWKQELSVCQAQQCSSLTDPSHGSLTCTHPHGQFSFGTVCEVSCQAGFKLHGTPKMECLEMGKWTDTPPFCLAQECPLLSAPENGWMNCSHPHSLFSYESQCLLGCETGFELTGEPDIQCSASGNWSQEMPSCAVVHCEPLWLTHLSDLGPPPSMNCSHPHGNFSFGSQCMFWCANSHELNGTSQLVCTSNGYWTHSPPICVVKEMSVSASMLIYAAVGAVSSAGLLLLGGLIFLLTRQITKKAHYSLNKSSLEGDLNLAFELN
Protein: Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129) (Protein LIPID X A) (AtLpxA) (Q9SU91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257}.
Interaction partners:
- Probable lipid-A-disaccharide synthase, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 5, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 2, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3, mitochondrial
- Probable tetraacyldisaccharide 4'-kinase, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
Sequence:
MISLLKAREKLLSPLVSSTIRRLSSSLSYSREDSRDSEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDELPGYTFIGCNNIIGHHAVVGVKCQDLKYKHGDECFLCIGNNNEIREFCSIHRSSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFMSTETVSLSFEERLTELEQDQELYSVPAVSAMLQSIRDSFTESRRGICKFRQWLDSTT
Protein: C2 domain-containing protein (H2KYE1)
Organism: Caenorhabditis elegans
Interaction partners:
- SMP-LTD domain-containing protein
- Thioredoxin domain-containing protein
- Uncharacterized protein F15G9.5
- PH domain-containing protein
- cAMP-dependent protein kinase, catalytic subunit-like
Sequence:
MLSGERFESLLKSPKHHAKQFQEKVLNAYNYAIQLYTDAIESETFATYGQLILPLAVLVSVVLTILLCSVIWKILYYTSFLQVLGWLFGEMLWVILSWGLVAVLCYFALNHLGSTGEAAHTSSTFGSSVSGNGVANGGTHTSSGEWSNEIVSWLYSNFHKVPAPMDAWIKSLNEAAKKVTSPTKCEVLFEGFGDHSDVLQPPKISNVRVEHGPRDHLTVRSNVHLPCVKLRLVSSQRTPERMIVSNYDVSIVDLRGEVECRMACIANQLYLMGCFSGRPEMDIELRNTDPNAQYQVSIPMVEESIRRCLLSAVTNINLSEEMPEERNTFADTFSRTIYNPPTHSPSGTMRNSYNNYDTNLHVDAYGTQSSHRSNSPSGDVPEMFKKLNESHLISPSYNTNSIPNKMRIKVIKASRLGREVSQPFVNVEMDEPAQKYSTTKGINANPFWEETFDFDLTPATEEILFEIYEGNDKLHMNDDEGFLGLAIVNFEEIRRSGETVHSLKLQGRPYRKDAISGEITVQFDFFYDPNLLTSGKLTDTVKVTNPNGSEFRETLTTHRRPIYDPHDNFDGHEPIVPSKTTTVTVKTVSQTLKEKPTIQSVHGSLENAVDPATQKILDRQFKNHNDPKTRELEAKLQSVAQSMSASSTLDRPSKNGNNGQYYRDQTAPPEFHEELDVRQSRDKSKKAPTEKRDRSFFGELKDRLSGRRGRSQKRSKSVDVENNQLLEEAVSLPPSRDPSRTRYAVSSNDKYRETHSVGGRSGESTKSLYQHSTLILELDQDKQAKYFLIPPAMLNEPAASRLMRKGKKLHIYNDHTFVAVKVKGCSGATCNVCQQRIRSSFSKQAYQCRDCKMVCHKTCHYKTDAFCTQSNVSKLQIAKDVDWAHFLSHYQLEEFISSEGL
Protein: EseG (Q4G4D4)
Organism: Edwardsiella tarda
Interaction partners:
Sequence:
MPWMPRLRCAMARPTATQAIHCCASGHRICWIRLINPKEPMMINGVFTDAPLPPTAAPGPCPAPSRREIGTQCDLLGIEAPRSRAPGASAPLDQLRAQAQEAEQKAKACGVDMAKRSFVAKVLTLVAASAVLITAALITGLTAGAGVPLLALASIGFTIAVGDVACAAYDWNHKKNGGEGLAMGSDAIGNAIHWLGKVSGASDERARQVAAYGSLLARSAITVSTVAVSGFLPVAAPLALQTTIPALTLGRTMIEISASAIKTNETHHGIVQRGHEINAGRAWGRVEIAQSEPTVDRDADERRIAAQLATLEKTRAFLIQTLRQNGVESAPPARRYSFA
Protein: Guanylate cyclase 2G (EC 4.6.1.2) (Guanylyl cyclase receptor G) (mGC-G) (Q6TL19)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000305|PubMed:14713286}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Bis
- Inosine triphosphate pyrophosphatase
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
- Natriuretic peptides A
- cGMP-specific 3',5'-cyclic phosphodiesterase
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
- cGMP-dependent 3',5'-cyclic phosphodiesterase
- High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
Sequence:
MASRTRSESPLEPRLYAGAGSRADHPSLVLMLSVVMLVTCLEAAKLTVGFHAPWNISHPFSVQRLGAGLQTVVDKLNSEPVGLGNVSWEFTYTNSTCSAKESLAVFIDQVQKEHISALFGPACPEAAEVIGLLASEWNIPLFDFVGQMAALKDHFWCDTCVTLVPPKQEISAVLRESLRYLGWEHIGVFGGSSADSSWEQVDEMWGAVEDGLQFHFNITASMRYNSSSSDLLQEGLRNMSYVARVIILICSSEDARRILQAAVDLGLDTGEFVFILLQQLEDSFWKEVLTKDKVIRFPKVYESVFLIAPSAYGGGIGDDGFRKQVSQELRRPPFQSSITSEDQVSPYSAYLHDALLLYAQTVEEMRKAEKDFRDGRQLISTLRAGQVTLQGITGPVLLDSQGKRHVDYSVYALQESGNRSLFLPFLHYDSFQKVIRPWRNDSNTSWPHGSLPEYKPGCGFHNDLCKTKPPTVAGMTVTVTAVIPTVTFLVLASAAAITGLMLWRLRGKVQSHPGDTWWQIRYDSITLLPQHKLSHRGTPVSRRNVSDTSTVKASADCGSLVKRHQDEELFFAPVGLYQGNQVALCYIGDEAEAWVKKPTVRREVCLMCELKHENIVPFFGVCTEPPNICIVTQYCKKGSLQDVMRNSDHEIDWIFKLSFAYDIVNGLLFLHGSPLRSHGNLKPSNCLVDSHMQLKLSGFGLWEFKHGSTWRSYNQEATDHSELYWTAPELLRLRESPCSGTPQGDVYSFAILLRDLIHQQAHGPFEDLEAAPEEIISRIKDPRAPVPLRPSLLEDKGDGRIVALVRECWDESPELRPIFPSIKKTLREASPRGHVSILDSMMGKLETYANHLEEVVEERTRELVAEKRKVEKLLSTMLPSFVGEQLIAGKSVEPEHFESVTIFFSDIVGFTKLCSLSSPLQVVKLLNDLYSLFDHTIQSHDVYKVETIGDAYMVASGLPIRNGAQHADEIATMALHLLSVTTHFQIGHMPEERLKLRIGLHTGPVVAGVVGITMPRYCLFGDTVNMASRMESSSLPLRIHVSQSTAGALLAAGGYHLQKRGTISVKGKGEQTTFWLKGKDGFPVPLPEFTEEEAKVSEIL
Protein: Small ribosomal subunit protein uS13 (40S ribosomal protein S18) (Q8JGS9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity). Plays an essential role in early embryonic development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62269}.
Interaction partners:
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL30
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL27
- Mitochondrial ribosomal protein L27.
- Ribosomal protein L3
- Ribosomal protein L4
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL33
- Ribosomal protein L18
Sequence:
MSLVIPEKFQHILRVLNTNIDGRRKIAFAITAIKGVGRRYAHVVLRKADIDLNKRAGELTEDEVERVVTIMQNPRQYKIPDWFLNRQKDIKDGKYSQVLANGLDNKLREDLERLKKIRAHRGLRHFWGLRVRGQHTKTTGRRGRTVGVSKKK
Protein: Ubiquitin carboxyl-terminal hydrolase 36 (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Protein scrawny) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36) (Q9VRP5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolase that deubiquitinates polyubiquitinated target proteins including imd. Required for preventing the constitutive activation of the imd/NF-kappa-B (Imd) signaling cascade under unchalleneged conditions. Deubiquitinates imd linked 'Lys-63' chains which leads its proteasomal degradation and consequently down-regulation of the Imd signaling cascade. Removal of the activating 'Lys-63'-linked chains is likely to enable their replacement with 'Lys-48'-linked chains which act as 'tags' the for proteosomal degradation of imd. Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4me3). Controls selective autophagy activation by ubiquitinated proteins.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19039105}. Cytoplasm {ECO:0000269|PubMed:19837371}.
Interaction partners:
- FI07430p
- P53, isoform B
- CAAX prenyl protease 2
- Protein immune deficiency
Sequence:
MPVSMAVCETANVVNAALRESLGGNSSAGSSTDQAKSGEDTNGSLQNHIVANAKRILMAKIEYEEVPNYHESVLENLKSKYIVIKPGNPGAINGFSGKNNTGKLVGANGHDNNGARKQAEHPNNQSHHINHHNHQHPTSNPNELPKPKRVLYPRENIRIGWKQSERKWQVGTGMINVGNTCYLNSTLQALLHIPALANWLVSEQAHLADCNVAEPGSGCIICAMTKTLLATQSNQSAVRPFLIYSKLKQICKHMVVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKADSLEDAFEGHFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMIGNKLTKQISFKSRIDLSKYAARSQAAQAQPLTYRLVSMVTHLGASQHCGHYTAIGSTDTGSFYNFDDSYVRPIAMHSVCNTNAYIMFFELDLSQAASPAANRPNGVRLTNGHSTTPVPAATVSSPSPTRFIGPQLPAGGANGYTNGNAQKTAIQFKQQNQQSPQNGLQLGTGKFQDTAKPPLVGAHAKGEATSAPTANGNKSSSPSSNSSSNHKSINQQQYLPISSDDEDIEDEMKPRPTTAQLPSMPNMTENHTEPKAKSPVKIQVKTPVKTPLKSLVPYESASEEEEAPLPNPRKRPSGEDSSESDQESGQTNGHSKTNGSHTNGSASSSVHVNNSKQKTDAIDEIFKSLKKSADSDEDDDEEEPSIQLTNGWHPQKQSQSQSKAPPSPKTPPSPAVIKSKTGIWKVTRNDEVDAIEDDVDVVVVEGSPVKIPTPNKNHRNPFSSSKPSTDSPATPGAKRQKLLNGSALKSHQQPRVGNGYQSNATSNGSTINELLKQSYRGYGSPVLSWNGKPAELEKELLVDAREQRQRDIDDDEENEMDRGRQRKVKSGSAKGNNASNSTPGYNPFQEYEGQKRWNKNGGGGGFPRFYNQNYRQNFQQRNKFKFNRFGGPGSAKFQQQRALQRHLSAGGGFSRRQPSAQQQQQT