wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin, type I cytoskeletal 17 (Cytokeratin-17) (CK-17) (Keratin-17) (K17) (Type I keratin Ka17) (Q6IFU8)
Organism: Rattus norvegicus (Rat)
Function: Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state. Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway. Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial 'stem cells'. Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors. May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QWL7}.
Interaction partners:
Sequence:
MTTTIRQFTSSSSIKGSSGLGGGSSRTSCRLSGSLGAGSCRLGSASGLGSALGGNSYSSCYSFGTGSGYGGNFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPARDYSAYYQTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKPKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR
Protein: Proton-gated ion channel (GLIC) (Ligand-gated ion channel) (LGIC) (Q7NDN8)
Organism: Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Function: Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glr0003 protein
- Chaperone protein
- Chaperone protein
- Proline iminopeptidase
- Chaperone protein DnaJ
- Gll4130 protein
- Large-conductance mechanosensitive channel
- Oxidase
- Chaperone protein ClpB
- Heat shock protein
Sequence:
MFPTGWRPKLSESIAASRMLWQPMAAVAVVQIGLLWFSPPVWGQDMVSPPPPIADEPLTVNTGIYLIECYSLDDKAETFKVNAFLSLSWKDRRLAFDPVRSGVRVKTYEPEAIWIPEIRFVNVENARDADVVDISVSPDGTVQYLERFSARVLSPLDFRRYPFDSQTLHIYLIVRSVDTRNIVLAVDLEKVGKNDDVFLTGWDIESFTAVVKPANFALEDRLESKLDYQLRISRQYFSYIPNIILPMLFILFISWTAFWSTSYEANVTLVVSTLIAHIAFNILVETNLPKTPYMTYTGAIIFMIYLFYFVAVIEVTVQHYLKVESQPARAASITRASRIAFPVVFLLANIILAFLFFGF
Protein: L-Ala-D/L-amino acid epimerase (EC 5.1.1.-) (A4AQI7)
Organism: Maribacter sp. (strain HTCC2170 / KCCM 42371)
Function: Broad specificity dipeptide epimerase. Catalyzes the epimerization of L-Ala-L-Ala, L-Ala-L-Glu, L-Ala-L-Ser, L-Ala-L-Thr and L-Ala-L-Met (in vitro).
Interaction partners:
- 8-amino-7-oxononanoate synthase
Sequence:
MQISLKKYTLELKHTFSISRESHDFQDTLIAGLTLNGKTGYGEATSNPYYKITAESMIKEIEGIKNEIESFEFTTPESFHSFLEEKELSNFAICALDLAAHDLYGKLLGKPLYEIWGTNNDQYPTTNYTIGIAELDTMVAKMKEKPWPIYKIKLGTDNDVAIIRELRKHTTATFRIDANCAWSAEETIANAPQLKELGVEFLEQPLQADDWAGMEKVMHQCVLPVIADESCIVESDVEKCGLHFNGINIKLTKCGGLTPALRMIKKAKLMGLKVMVGCMTESSVGISAIAQLLPQLDYVDMDGAILLKRDIANGVRIGEDGSVVFPTLGGSGVTLNQ
Protein: cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE) (O54735)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
Interaction partners:
- Adenine phosphoribosyltransferase
- Guanylate kinase
- GMP synthase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Atrial natriuretic peptide receptor 2
- Guanylate cyclase soluble subunit beta-1
- Atrial natriuretic peptide receptor 1
- Guanylyl cyclase C
- cGMP-dependent 3',5'-cyclic phosphodiesterase
Sequence:
MLPFGDKTRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLPQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTSPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLVSRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCPDSFSRVFQMEWEEVGKSSEPLTREHDANKINYMYAQYVKNTMEPLNIPDVTKDNRFPWTNENMGHINTHCIRSLLCTPIKNGKKNKVIGVCQLVNKMEEKTGKIKAFNQNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQALAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLETLALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSTMEHHHFDQCLMVLNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNEFSFEDPLQKELFLAMLMTACDLSAITKPWPIQQRIAELVAAEFFDQGDRERKELNMEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCLPLLDGCRKNRQKWQALADQQEKTLLNGESGQAKRD
Protein: B3 domain-containing protein LFL1 (LEC2 and FUSCA3-like protein 1) (OsLFL1) (A4LBC0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription repressor involved in flowering time regulation. Represses the flowering activator EHD1 by binding specifically to the DNA sequence 5'-CATGCATG-3 of its promoter.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326, ECO:0000269|PubMed:17913295}.
Interaction partners:
Sequence:
MRGEERWQEQPALASHPSRATLRPRGWPRLGLAPTGVGSSCPPAPASELARHLARRAPVSASPPVLPPIKDQGARPPTLAASAAAASSPPPPPPPPIPPLPPSTSTSAARPTDMAGVTSKRRSSSASTSSSSGDGAAVSDRPRGVTRKRRSGGRCPRPAASLRPAAPRPSSHHTAGLRVILQKELRYSDVSQLGRIVLPKKEAEAYLPILTSKDGKKSLCMHDLQNAQLWTFKYRYWPNNKSRMYVLENTGDYVRTHDLQLGDSIVIYKDDENNRFVIGAKKAGDQQAATVPQVDEHISTLFPIFPIAQVDDYLSPMAPQVDISAFVPHADENHEIFDGILNSLPEIPVANVRYSDFFDPFDDGMDMANTLNANANQSASLHVTDDKSGHSLIPNPKSGPHM
Protein: GCN5-related N-acetyltransferase 3, chloroplastic (EC 2.3.1.48) (Q940H2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:32633465}.
Interaction partners:
Sequence:
MGLVGCVGKSSLVSMELRWARRRKSDNAASALPRSIPIYISTLKKDINLEELRNLYSLCNHSCNRLSEKDSNVEKIVDMKKLRRAISRSDVIVSVFCKPQHVDVDDAVLYSEEESLSSSLYTSEFGRQNKDDSFLGDLFQNAVPLTPSNGQLVGFGRAYSDYGLTASIHDLMVLPSLQRMGIGKLIVNRIVRLLTSRDIYDIAALCFEDERPFFKACGFGDDRMGSTTMMFTKSLEA
Protein: AT23738p (Q8IHA0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EQYTTLPRNYNIPVKMEDISHEERVLILDTFRILDKDNEGAITSKEMAVVIRALGRQPNDAEVQSMINEVDSEGNGSIVAPEFCNVILRKMRDTNHEDELREAFRIFDKDNNGYITTTELKNVFTALGVKLSDDELEEMIREYDLDQDNHLNYEEFVNMMTMR
Protein: Profilin-1 (Profilin I) (P26199)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Protein VASP homolog
- Cofilin-1A
- HP domain-containing protein
- Severin
- Exportin-6
- Actin domain-containing protein
- Adenylyl cyclase-associated protein
Sequence:
MSWQQYVDEQLTGAGLSQGAILGANDGGVWAKSSGINITKPEGDGIAALFKNPAEVFAKGALIGGVKYMGIKGDPQSIYGKKGATGCVLVRTGQAIIVGIYDDKVQPGSAALIVEKLGDYLRDNGY
Protein: ABC transporter, transmembrane ATP-binding protein, putative (Q5LVX1)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Glycosyltransferase, group 1
- Glycosyl transferase, group 1 family protein
- Mechanosensitive ion channel family protein
- Adenylate/guanylate cyclase
- Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein
- Glycosyl transferase family 28 C-terminal domain-containing protein
- Glycosyl transferase family 28 C-terminal domain-containing protein
- Polysaccharide deacetylase
- S-adenosyl-L-methionine methyltransferase
- S-adenosyl-L-methionine methyltransferase
Sequence:
MSGRDSLGEGRRLRVWRPSCLRPILGVGAIERTLFRFIWKYSRRDQLILLMVTATLFPLLYLTLELPKRIINDAIGAASSTIEVWGFTFDQVTYLGILCAAFLISVLAHGLMKMRINTMKGVMSERMLRRFRYLLITRVLRFPQPYFERVSQGELVSMITAESEPMGGLMGDAISQPVLQAGQMITILSFLFLQSLWFGLAAVALIPLQAWLIPRMQRQINLLNKKRIQEVRVLAAQIGENAAGAATLRSNAGWPWRMSMISYQLGRLFTIRFDIYQKKFFMKFVNNFIGQLTPFLFYSIGGYLVLQGSVSLGALVAALAAYKDLSSPWKELLTYYNQTQDMSLRWEVILDRFAPPGMIDEDKFTGFPDERPRLIGDIVLDKVSVRDADGNLVLDDLDLTLPGGKVIGIAASSEEDRRALSELLTREVLPASGQVRIGEIALSDLHQMVVASRIGHATSRPVLFQGTFGDNVTMPVRVRPQGDSGEPGFHAETLRAGNSADPYHSDWLEPGLAGFDDARALRDWWLKLVEGLGSGAALYRRGAEQVFAEADHPDLAARLVALRPVIQEAAERAGLAGQAHFFDPDHYNPALPVAENLLFASPRAPFTPEVLAGQTDFLEQIRQIGLDEPLVRLTQDVIDMLRQIFGLDGTDHPLFRKMNLDVRTYETALELVEKTRDAGARALEDDQLASLLAVPFRISADQIGPAFSDQIKARILELRKSHSSELMRSLDDVFAPLDPGAFAPGLNVLENALFGKVSEVGGARSDELRKLITDLLDEHGLRPQVIQLIYDLPVTLGGQNVPAIFAEPLAFTRATIKRPDILLLDRALASYDMQTQIAVYRNLRALLPETTLIYLNDAFENPDVFDLYVEVQQGRIVTEEVPRQQEEEDSVASADLSRKVRTLEQTPLFSGLDRRQLRLLAFGARWYSAKAGEVVFLKDDEPTDGAYMMIEGEAGLYLPREGQEDQLIVTVGPGRLVGELGLIRKEPRALSMVAATDITCLRIGEEEFLAVVENDAATAFKLLQVVAGYVSN
Protein: NKG2-A/NKG2-B type II integral membrane protein (CD159 antigen-like family member A) (NK cell receptor A) (NKG2-A/B-activating NK receptor) (CD antigen CD159a) (P26715)
Organism: Homo sapiens (Human)
Function: Immune inhibitory receptor involved in self-nonself discrimination. In complex with KLRD1 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Upon HLA-E-peptide binding, transmits intracellular signals through two immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHP-1 and INPPL1/SHP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules. Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions. Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity. On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens. In HLA-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12165520, ECO:0000269|PubMed:20952657}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Natural killer cells antigen CD94
- HLA class I histocompatibility antigen, alpha chain E
- HLA class I histocompatibility antigen, alpha chain G
- Killer cell immunoglobulin-like receptor 2DL3
- Tyrosine-protein phosphatase non-receptor type 6
- Beta-2-microglobulin
- Killer cell immunoglobulin-like receptor 2DL1
- HLA class I histocompatibility antigen, C alpha chain
- Killer cell immunoglobulin-like receptor 3DL1
- HLA class I histocompatibility antigen, A alpha chain
Sequence:
MDNQGVIYSDLNLPPNPKRQQRKPKGNKNSILATEQEITYAELNLQKASQDFQGNDKTYHCKDLPSAPEKLIVGILGIICLILMASVVTIVVIPSTLIQRHNNSSLNTRTQKARHCGHCPEEWITYSNSCYYIGKERRTWEESLLACTSKNSSLLSIDNEEEMKFLSIISPSSWIGVFRNSSHHPWVTMNGLAFKHEIKDSDNAELNCAVLQVNRLKSAQCGSSIIYHCKHKL
Protein: Sodium/proline symporter (Proline permease) (Q79VH1)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU366012}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU366012}.
Interaction partners:
- L-glutamate gamma-semialdehyde dehydrogenase
- Ectoine/proline transporter ProP
- Uncharacterized protein Cgl1270/cg1434
- Glutamate transport ATP-binding protein GluA
- PAS/PAC domain
- Adenine phosphoribosyltransferase
- Transcriptional regulator WhiB
- Lactose phosphotransferase system repressor
- Lysine exporter LysE
- Na+/alanine symporter
Sequence:
MSDNTWFIIAIVIYMLVMVLIGYWSYRKTEKYDDYMLAGRGLNPFVAAMSAGASDMSGWLLMGLPGALFVTGMSELWIAVGLTIGAWANWMWVAPRLRSYSEISANSITLPSFFENRLRDKSRALRIIAALIIIVFFTFYISSGMVAGGVYWESTFGGDYLLGMAIVAGVTVLYTFIGGFLAVSYTDAVQGTIMFFSLIIVPVMAYFALANPMDIWSFANSNDYGPHTDGIGNPTYFSMISGISAAAIIGNLGWGLGYFGQPHIVVRFMALRTPAEAKQGRRIGISWMIICLIGATFTAIISTVFFAQNPDANITDTRAYESIFLDLARMLFHPLIAGLILTAVLAAIMSTMSSQLLVTASSLIEDLLKVVKKDSLSERTLIMLSRATVIILAIIAAAMAINPSDSILGLVGFAWAGFGSAFGPIILASLYWKRLNAAGAISGMITGAIVSIAWGMSPLSDTLYEIIPGFALATIVMVVVSLLTKEPSEEILNEFETAKDLAAAVESNEDVDFADAAQKLSKES
Protein: DNA-directed RNA polymerase subunit Rpo8 (EC 2.7.7.6) (DNA-directed RNA polymerase, subunit G) (RNA polymerase subunit 8) (B8YB59)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00866, ECO:0000269|PubMed:22848102}.
Interaction partners:
Sequence:
MESKAQEIILSCEINSIERGSLKNLSIIHMSCNDFNISFDIIDSINIFSQKEKVKAFISKNRLSYTNDDFCGHGYIVTELKDSSSNNGNRYITIISLFGLLVKIISNKESFLKIHQLNVMDHIYFCVKKNT
Protein: Microtubule-associated protein 9 (M9P175)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDGEPVSTTLAYTKSPKTSRRTTFQDELKKAVSARASRHSYSDDFENDDDEDCKVKSDDDDDDILNTLIKTQKQKKERFKAGKTKGKINDFKLSDDEEENVKPKKVSFMKTKRTSSPLHFEQSNSAGSADGQCSSVYSSQSRNPSQSPSNTYTPEKNQQSDSPFSSLSDKYLPESTLLKNDEQSKSAVRLRNQTESSMVRKSLSESPLPLNSENSQWDSSIPFTSEGSQWDSPVPLPSEKHEDNQKIEKDDEVPVPQPRERTVKSKSSARCLLQDVSPRPKPRQKTSNLCDTGQLEEETKPETPDCSRAATSSMSITFSNRSSSEKSQASTNKCTSVQGPDGDQAMTERSLLSSEQLSENLATAGSAATEESKERNYSTSFEEKPESSQGDLEQASTTPNQMSRKTTDRPSSSQSTSSRKSKCSYKAESKYLGTLKILDQRTQKAQQVPEAADSLRAAVYQEWLKKKEETLEITRRAKKQEQKMKEEKMQEEKLSKTADAKASYDAWKEKKRDVIRKKLSEKQKLINQQQVEMDKKQEKKVTAKQVFEKWKEEHDSILKDKIREKKQAERKLKLQKVTEKEERKKDCSSAFTKWSDQKKDVIEEKVREERREQKIKEVEEQYEKEEKDKMALEMYDKWLRRKEFQQEKEKKEKRIQAILQEEPPPPWSPPNKTIPFGK
Protein: Lipoarabinomannan carrier protein LprG (27 kDa lipoprotein) (Antigen P27) (Lipoprotein LprG) (Triacylated glycolipid carrier LprG) (Triacylglyceride transfer protein LprG) (P9WK45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably helps membrane protein Rv1410c (P55) transport triacylglycerides (TAG) across the inner cell membrane into the periplasm; TAG probably regulates lipid metabolism and growth regulation. Binds TAG and transfers it between lipid bilayers, probably to the outer membrane in vivo. Binds di- and triacylated phosphatidyl-myo-inositol mannosides (PIMs), and glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM), facilitating their recognition by TLR2. Binds LM > PIM6 > ManLAM > PI-LAM > PIM2 (mannose-capped LAM and phospho-myo-inositol-capped LAM, E.coli expressed without acyl-groups); deacylated LM and LAM also bind to this protein via their mannose moieties, showing LprG has at least 2 different ways to bind glycolipids. Binds triacylglycerides (TAG) in the same cavity, is able to transfer TAG between lipid bilayers. Overexpression of LprG and Rv1410c leads to increased levels of TAG in the culture medium. Required for Rv1410c-mediated export of drugs. Required, probably with Rv1410c, for normal surface localization of LAM.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:21762531, ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000305}. Secreted, cell wall {ECO:0000269|PubMed:21762531}. Secreted {ECO:0000269|PubMed:21762531}. Cell surface {ECO:0000269|PubMed:25041568}. Note=Present in extracytoplasmic vesicles (PubMed:21364279). Immunoelectron microscopy indicates this protein is close to the cell surface (PubMed:25041568). {ECO:0000269|PubMed:21364279, ECO:0000269|PubMed:25041568}.
Interaction partners:
- Triacylglyceride transporter Rv1410c
- Lipoprotein LpqH
- Riboflavin synthase
- Phosphate-binding protein PstS 1
- Lipoprotein LpqN
Sequence:
MRTPRRHCRRIAVLAAVSIAATVVAGCSSGSKPSGGPLPDAKPLVEEATAQTKALKSAHMVLTVNGKIPGLSLKTLSGDLTTNPTAATGNVKLTLGGSDIDADFVVFDGILYATLTPNQWSDFGPAADIYDPAQVLNPDTGLANVLANFADAKAEGRDTINGQNTIRISGKVSAQAVNQIAPPFNATQPVPATVWIQETGDHQLAQAQLDRGSGNSVQMTLSKWGEKVQVTKPPVS
Protein: NADH-ubiquinone oxidoreductase chain 4 (EC 7.1.1.2) (Q2F980)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion membrane {ECO:0000256|RuleBase:RU003297}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003297}.
Interaction partners:
Sequence:
MLEHFCECYFDLSGPILCPVLGSITLLFIPNSSIRLIRLIGLCVSLITFLYPLVPRIQFDPSTAKSQFVESLRWLPYENIHLYMGIDGLSLFFVILTTFLIPICISVGWSGMRSFGKEYITAFLIREFLMIAVSCMLDPLLFYVLSESVPIPMFIIIGVWGSRQRKIKAAYQFFLYTLLGSVFMLLAILLILLQTGTTDLQILLTTEFSERRQILLWIAFFASFAVKVPMVPVHIWLPEAHVEAPTAGSVILAGILLKLGTYGFLRFSIPMFPEATLCFTPFIYTLSAIAIIYTSLTTLRQIDLKKIIAYSSVAHMNLVTIGMFSPNIQGIGGSILLMLSHGLVSSALFLCVGVLYDRHKTRLVRYYGGLVSTMPNFSTIFFFFTLANMSLPGTSSFIGEFLILVGAFQRNSLVATLAALGMILGAAYSLWLYNRVVSGNLKPDFLYKFSDLNGREVSIFLPFLVGVVRMGVHPKVFPDCMHTSVSNLVQHGKFH
Protein: interactor of constitutive active ROPs 2, chloroplastic-like (p70 protein) (Q8VXD2)
Organism: Nicotiana tabacum (Common tobacco)
Interaction partners:
Sequence:
MQTPKARTVSVEVPQRTSPATPKTTRKLKTPGSDADSVSSPNPATRTPKDRSPKVVGRRSPRSPVIEKKRPSKVSDLEAQLAQLQEELKKAKDQLNSSESLKKRAQQDADEAKKQLAVMSEKLEDSKKQLLELSDSEEARLLELRKISQDRDRAWESELEAIQKQHELDSAALASALNEIQKLKIQLDRVADSEATQAHHAESAHAEIQSLRVELMETLTLVEKLRNQLNDSKESEACSLEEVSKAQMQLEMSKMTEDTLRSEGLKAMDACRTLSLELEKSKDRVASLEELVSKLQSSESSVAAEGNGVTVEADELKAEVSELRAALEASERKYQEEYIQSTLQIRSAYELVERTKSESTQREAEWEAKLNETKSEVQELKEKLMNKEAELQNISDENKGLSLHVEQMQSADKEFELSAQLKQSESISGDLRGNLLDKENELQSLMEENELLKSEIGKRESESTKMSDEALALVEAAKTAESEALIKLGDLTEEADRSSRKVARVTEELDAAQTANSEMETELRRLKVQCDQWRKAAEAAASMLSAGNNGKYVERTGSLDYHTIGGKLGSPLLDDLEDDSPKKKNNNMLKRIGVLLKKGQK
Protein: E3 ubiquitin-protein ligase PPP1R11 (EC 2.3.2.27) (Protein phosphatase 1 regulatory subunit 11) (Q6MFY6)
Organism: Rattus norvegicus (Rat)
Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of protein phosphatase 1.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 7
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Proline-rich protein 3
- Tripartite motif-containing protein 26
- Guanine nucleotide-binding protein-like 1
- Protein phosphatase 1, regulatory
- NSFL1 cofactor p47
Sequence:
MAEAGAGGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWSSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEDEEEGCGHTHCVRGHRKGRRPTTPGPTPTTPPQPPDPSQPPPGPMQH
Protein: AimR transcriptional regulator (Arbitrium communication peptide receptor) (P0DOE3)
Organism: Bacillus phage phi3T (Bacteriophage phi-3T)
Function: Transcriptional regulator which is part of the latency-replication switch system that decides at the onset of infection whether to replicate and lyse the host or to lysogenize (latency) and keep the host viable. Activates the transcription of the aimX locus. Transcriptional activation of aimX seems to lead to the productive viral replication (lytic cycle), aimX possibly acting as a regulatory non-coding RNA.
Interaction partners:
Sequence:
MIKNECEKDNQLAARLAKLAGYEKVNGFYKFVNTPEKEMENLGGLLKIVKNLFPDSEEQLLSEYFLELDPNKKCARQSVEYSDINQWDTLTDKIIINLCNSKNSTSQEWGKVYSLHRKLNKNEISLNDAIRESGKCKIKSAEMLFFSNAMLMYAYLNIGEFGLMKSTSKLLEFDDLPEGFIKESFKSRVSMLEANISLNENSLLEARQHSNRAIENSNVNRICFFAYLTIGNTLIFEDYDEAKKAYIKGQKYAKNPVHQEMLDGALCFLSNIWKKENQWVNYNSDNIKYLQLRAFYYINQGNIEEATEILDELSSRDQDENELGFYYYYKGLISQDKTDYYKSIRYFKKSDDKYFIQLPLLQLERMGADLELLNLISI
Protein: 10 kDa anti-sigma factor (10 kDa RNA polymerase-associated protein) (Audrey Stevens' inhibitor) (P32267)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Transcriptional inhibitor. Inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. This allows Gp55 to successfully compete for the core enzyme. Plays an important role during the prereplicative period of phage T4 development.
Interaction partners:
Sequence:
MNKNIDTVREIITVASILIKFSREDIVENRANFIAFLNEIGVTHEGRKLNQNSFRKIVSELTQEDKKTLIDEFNEGFEGVYRYLEMYTNK
Protein: Hepatocyte nuclear factor 3-alpha (HNF-3-alpha) (HNF-3A) (Forkhead box protein A1) (P23512)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3'. Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Involved in glucose homeostasis; activates the GCG promoter. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas, lungs and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles. Modulates the transcriptional activity of nuclear hormone receptors. Is required for maximal gene activation mediated by AR in the prostate. Negatively regulates AR transactivation via competition with coactivators such as NCOA2. Is involved in ESR1-mediated transcription. Involved in regulation of apoptosis. Involved in cell cycle regulation. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes.
Subcellular location: Nucleus.
Interaction partners:
- GATA-binding protein 3.
- Estrogen receptor
- Androgen receptor
- Transducin-like enhancer protein 3
- Nuclear receptor interacting protein 1
- Progesterone receptor
- Histone deacetylase 7
- CCAAT/enhancer-binding protein alpha
- Nuclear receptor coactivator 3
- Histone H3.1
Sequence:
MLGTVKMEGHESNDWNSYYADTQEAYSSVPVSNMNSGLGSMNSMNTYMTMNTMTTSGNMTPASFNMSYANPGLGAGLSPGAVAGMPGGSAGAMNSMTAAGVTAMGAALSPGGMGSMGAQPAASMNGLGPYAAAMNPCMSPMAYAPSNLGRSRAGGGGDAKTFKRSYPHAKPPYSYISLITMAIQQAPSKMLTLSEIYQWIMDLFPYYRQNQQRWQNSIRHSLSFNACFVKVARSPDKPGKGSYWTLHPDSGNMFENGCYLRRQKRFKCEKQPGAGGGSGGGGSKGVPENRKDPSGPVNPSAESPIHRGVHGKASQLEGAPAPGPAASPQTLDHSGATATGGGSELKSPASSSAPPISSGPGGWICTPLSPTWLAPHESQLHLKGAPHYSFNHPFSINNLMSSSEQQHKLDFKAYEQALQYSPYGATLPASLPLGGASVATRSPIEPSALEPAYYQGVYSRPVLNTS
Protein: Stress-associated endoplasmic reticulum protein (Q6DGW5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU364120}; Single-pass membrane protein {ECO:0000256|RuleBase:RU364120}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU364120}; Single-pass membrane protein {ECO:0000256|RuleBase:RU364120}.
Interaction partners:
- Taxilin beta b.
- Trinucleotide repeat-containing adaptor 6B.
Sequence:
MVAKQRIRMANEKHSKNITQRGNVKSSRNVSEDKVSVGPWLLALFVFVVCGSAIFQIIQSIRMGM