wanglab/gogpt-training-data huggingface dataset:
Protein: P2X purinoceptor 3 (P2X3) (ATP receptor) (Purinergic receptor) (Q3UR32)
Organism: Mus musculus (Mouse)
Function: Receptor for ATP that acts as a ligand-gated cation channel (By similarity). Plays a role in sensory perception. Required for normal perception of pain. Required for normal taste perception.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P56373}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}. Note=Localizes to neuronal cell body of sensory neurons. {ECO:0000250|UniProtKB:P49654}.
Interaction partners:
- P2X purinoceptor 2
- P2X purinoceptor 6
- P2X purinoceptor 1
- P2X purinoceptor 7
- P2X purinoceptor
- Glutamate receptor ionotropic, NMDA 1
- Neuronal acetylcholine receptor subunit alpha-7
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2D
- Glutamate receptor ionotropic, NMDA 2C
Sequence:
MNCISDFFTYETTKSVVVKSWTIGIINRAVQLLIISYFVGWVFLHEKAYQVRDTAIESSVVTKVKGFGRYANRVMDVSDYVTPPQGTSVFVIITKMIVTENQMQGFCPENEEKYRCVSDSQCGPERFPGGGILTGRCVNYSSVRRTCEIQGWCPTEVDTVEMPIMMEAENFTIFIKNSIRFPLFNFEKGNLLPNLTDKDIKKCRFHPEKAPFCPILRVGDVVKFAGQDFAKLARTGGVLGIKIGWVCDLDKAWDQCIPKYSFTRLDGVSEKSSVSPGYNFRFAKYYKMENGSEYRTLLKAFGIRFDVLVYGNAGKFNIIPTIISSVAAFTSVGVGTVLCDIILLNFLKGADHYKARKFEEVTETTLKGTASTNPVFTSDQATVEKQSTDSGAYSIGH
Protein: RNA polymerase I-specific transcription initiation factor rrn10 (Q10360)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. UAF seems to stimulate basal transcription to a fully activated level.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- RNA polymerase I-specific transcription initiation factor rrn5
- Upstream activation factor subunit spp27
- Homologous-pairing protein 2
- RNA polymerase I-specific transcription initiation factor RRN9 homolog
- RNA polymerase I-specific transcription initiation factor rrn11
- RNA polymerase I-specific transcription initiation factor rrn7
- RNA polymerase I-specific transcription initiation factor rrn3
- Uncharacterized protein C3B8.11
- TATA-box-binding protein
Sequence:
MSNPPTRPTLYNLVNADGELSYRARDLVQDFSVPIPHELPDPDLVHSIQDFATEYMLATGKKSFECLDESALLGLGYLVTEWMDAMVTDCLEEFEER
Protein: Cytochrome c-type biogenesis protein CcmE (Cytochrome c maturation protein E) (Heme chaperone CcmE) (P69490)
Organism: Escherichia coli (strain K12)
Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01959}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_01959}; Periplasmic side {ECO:0000255|HAMAP-Rule:MF_01959}. Note=Stabilized by CcmD in the membrane.
Interaction partners:
- Heme exporter protein D
- Heme exporter protein C
- Heme exporter protein B
- Cytochrome c-type biogenesis protein CcmF
- Thiol:disulfide interchange protein DsbE
- Cytochrome c biogenesis ATP-binding export protein CcmA
- Cytochrome c-type biogenesis protein CcmH
- Cytochrome c-type protein NapC
- Formate-dependent nitrite reductase complex subunit NrfF
- Probable cytochrome c-type biogenesis protein NrfE
Sequence:
MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKHDENYTPPEVEKAMEANHRRPASVYKDPAS
Protein: Lame duck, isoform C (A0A0B4KGM2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELLFPGCNKAFSRLENLKIHQRSHTGERPYGCQYKGCLKAFSNSSDRAKHQRTHYDTKPYACQLPGCTKRYTDPSSLRKHVKNHALRNANGQLRRKSAGGASVPPSGPKKAAKTRRHSESALVQRGVGAGVGVAVPSAPGDQRQHRSNSCSEALLLQQHQQQQQQQQQQQKQHQPENERTTDRSNCGTGVAANNNSMNFNELSNCIVIIEHNQSGGPAGPATLATATATTTATATYGNGNMAPAPETEVLSVCSGGGSSNSNSNNNRYNANINQLSELEQLLTTAKPTGTPAASANGISLANNNGRANGDSKCHLSEFVSFEYVTKYLTDVYEPQCKSPQPPANFHLQPEFDNSFDMLDFPQFI
Protein: Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) (Q5SUR0)
Organism: Mus musculus (Mouse)
Function: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Amidophosphoribosyltransferase
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
Sequence:
MAPVLHFYVRPSGHEGAASGRVFRRLQEKLPTLQSVETELCYNVHWAAETLPWAEEMKKLMWLFGCPLVRDDVAQEPWLVPGSNDLLLEVGPRLNFSTPASTNIVSVCQAAGLRAVDRVETTRRYRLSFTDHPTAEMEAISLAALHDRMTEQHYPDPIQSFSPQSIPAPLKGSIDILAEGRPALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEVFDLAQSNSEHSRHWFFKGQLHVDGKKLAHSLFESIMSTQASSNPNNVLKFCDNSSAIQGKKVKFLRPEDSTRPSCFQQQQGLRHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPDYNLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEAKHVGKKPPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPGGNPICSLHDQGAGGNGNVLKELSDPEGAIIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDRECLVGKTGQGDAPLTPPTPVDLDLDWVLGKMPQKEFFLQRKPPVLQPLALPPELSVRQALNRVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHQECIGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAALADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVQAPGSLVISAYAVCPDITATVTPDLKHPGGKGHLLYVPLSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFHITQGLLKECRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPAPGIHALPVLFAEEPGLVLEVQEADVAGVRQRYESAGLRCLELGHTGEAGPQAMARISVNKAVVVEEPVGELRALWEETSFQLDLLQAEPRCVIEEKQGLKERTGPSYYLPPTFPVASVPCKPGGPVPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAIRLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCNGCQLLALLGWVGSDPSEEQAEPGQDSQPTQPGLLLRHNLSGRFESRWATVRVEPGPALMLRGMEGSVLPVWSAHGEGYMAFSSPELQAKIEAKGLVPLHWADDDGNPTEQYPLNPNGSPGGIAGICSQDGRHLALMPHPERAVRLWQWAWRPSPFDVLPTSPWLQLFINARNWTQEDSC
Protein: Zinc finger BED-type containing 5 (D3Z5B1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRAAPRRAPAAQPPAAAAPSAVGSPAAAPRQPGLMAQMATTAAGVAVGSAVGHTLGHAITGGFSGGGSAEPAKPDITYQEPQGAQLQNQQSFGPCSLEIKQFLECAQNQSDVKLCEGFNEVLRQCRIANVDHPRPVDHGERNVKRRKYNEGFLQYGFTSTITVGIERPQCVICGVVLSAESMK
Protein: DNA repair and recombination protein RAD54-like (EC 3.6.4.12) (RAD54 homolog) (hHR54) (hRAD54) (Q92698)
Organism: Homo sapiens (Human)
Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks. Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:8805304}.
Interaction partners:
- DNA repair protein RAD51 homolog 1
- DNA repair and recombination protein RAD54B
- DNA repair protein RAD52 homolog
- Protein VAC14 homolog
- HCG2039718, isoform CRA_g
- DNA repair protein RAD51 homolog 4
- Cell division control protein 45 homolog
- DNA repair protein RAD51 homolog 3
- DNA repair protein RAD51 homolog 2
- Exonuclease 1
Sequence:
MRRSLAPSQLAKRKPEGRSCDDEDWQPGLVTPRKRKSSSETQIQECFLSPFRKPLSQLTNQPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILSKVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGKWLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCLIRRTSDILSKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPAEELLEGKMSVSSLSSITSLKKLCNHPALIYDKCVEEEDGFVGALDLFPPGYSSKALEPQLSGKMLVLDYILAVTRSRSSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDEEQDVERHFSLGELKELFILDEASLSDTHDRLHCRRCVNSRQIRPPPDGSDCTSDLAGWNHCTDKWGLRDEVLQAAWDAASTAITFVFHQRSHEEQRGLR
Protein: Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1) (P38652)
Organism: Rattus norvegicus (Rat)
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Subcellular location: Cytoplasm.
Interaction partners:
- Glucose-6-phosphate isomerase
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, brain form
- Glycogen phosphorylase, muscle form
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen debranching enzyme
- Hexokinase-3
- Hexokinase-2
- Transaldolase
- Phosphoglucomutase 2-like 1
Sequence:
MVKIVTVKTQAYPDQKPGTSGLRKRVKVFQGNANYAENFIQSIVSTVEPALRQEATLVVGGDGRFYMTEAIQLIVRIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRNIFDFNALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIASYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQRVEDILKDHWQKFGRNFFTRYDYEEVEAEGANKMMKDLEALMLDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISKNQGLRLIFADGSRIIFRLSGTGSAGATIRLYIDSYEKDAAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT
Protein: Uncharacterized protein (Q57WT5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRGSNRAQLSALFSIVSAATHPGVRAGRIPCVTQVTAPNDATAPSATALRPEKSHLTWQEALCEMEGLHEMSVPVRSAVALHEFLTSEAKKLGCDAAQRGELRRRAGVFCAKDNARPPRWSSGVFAGDDSRVNGRKLKDVLVEEMEGCRAWATECIQKMGSAAGIDQTRCALKPVGGAGEPFEEICGAVACFAGEESGVVESFALASVLLNHLRPMRRCLVELARDAWEEALNVCEQFLNSDDAISSALGAELFRCVASVAPSNSRVKLLSLYVHQRRNQLLSNLKDLPNLFRFCSLRCFDEEELLNWRRKLREQMQAMLDIIREMDALDVERAQEFKRACSLGRRAAVNMVPAGGYSQEHHGSHSNRFSFSSPASLSRNMEKRGCGVECEEGKKSVQVREISAKGAEYVKGNVEGLDNTSRSGNRFTSSEMAVVSSCWQRTALETWRKQRGSAIRMLCSQDGKEAKEGGQGKQFRVELGHHEACRADVAEGPHRTPLSRLRATISGGCKDYSDLLTALCSWVRENRRDLNETCYMTFVLEIVVFIFVCELRPSVGVAALSQLTSLLVQFRKEQVVNNSVNLFTEPLTVGLAAAALRTSMEAARRGTVRGGIAIDPEDVGNSPFLKDVAALLFEVRLPHMLRQTVSILRDGYFTSPLETIGAPPPLGFSNEFYQHTGVIAVLVRMAACRNMRPTVSPDFPTVPIQPVAFLIELTEVVGESAILMLREIPLRRKKPIPGVLNEALWGLFVPFAAWLLHNGESLAGELPVDGVRRLLKLCEAVVADLAARWNYSVVPTRRRWISMEKPVVSLFTQEYVADEVTRRKVVSFASLLEGILSAALRFFPNIFSEARGFSRVCSAVAIILHDVDTHTAHQIMEFLLRLSPPPEQMDCSAHHAVVRCLSAMRHGCTLWMQAVHHYTQTLRTIIRDEEDASVTASKRSRVSADVSTSLVLRCVGSSNAPRAVRCMLTLRIAALASAAGISLNAQSLVSCMHNFVMRRSQPNGIFNGVPWCDVLGWHSNLMTRARRASWAMRDVQFLHAACLQALLAQGEWPEALLLLPRVEIPFASDYCREGSKTGTRGFKSCVMSLLALCASDRTRSCRDTAATLIEMVRRRTSEREMCPTWDGTVTKLCQIACVEPPIYRGRDEKSRTPLFRDCAPSFPQPAPDAEGELLIRLGSTALSYNHPRYSHEALVKRLEARVARLRSEVAVTLAITCTGTEEPQRGHEGEKHCRPSLIRVCERTSVGLHRSRVVWSQNTLMREETDPSHARVHDEAARSLLDTRLASVMVPLRRLERIRAEKHHRHDGGKKW
Protein: Histone H2B type 3-B (H2B-clustered histone 26) (H2B.U histone 1) (Q8CGP0)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
Sequence:
MPDPSKSAPAPKKGSKKAVTKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Protein sickie (Q9VIQ9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the immune deficiency pathway, which mediates responses to Gram-negative bacterial infection. Favors Rel activation and nuclear translocation.
Interaction partners:
Sequence:
MLARCVSYQGSCDNINGILTRDYAEIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVGGLENITTNDICAGRLKAVLALFFALSRFKQQAKQTKSIGVGCGGGVGGSSSTLTGSGSVLGIGIGGLRTPGSSLNQDKNQQEQQQQQQQQQTPQQLAQSLENGNEMVNRQIAPAYAKVNGGTAIPLPATVMVQRRCPPDKVRPLPPTPNHTPSIPGLGKSGSDFNTSRPNSPPTSNHTIQSLKSGNNNSLRPPSIKSGIPSPSSPQTAPQKHSMLDKLKLFNKEKQQNAVNAASVASKTQIQSKRTSSSSGFSSARSERSDSSLSLNDGHGSQLKPPSISVSSQKPQPKTKQSKLLAAQQKKEQANKATKLDKKEKSPARSLNKEESGNESRSSTMGRTGKSSLVRAVGGVEKNTPKTSSKSSLHSKSDSKSSLKAPQLLQSPSSGGLPKPIAAIKGTSKLPSLGGGAGHLPAAESQQNQQLLKRETSDISSNISQPPPAEPPISTHAHIHQNQTPPPPYYANSQPTSHISSHGFLSEPSTPQHSSGIYGSSRLPPPKSALSAPRKLEYNAGPHILSSPTHHQRQGLPRPLVNSAPNTPTASPNKFHTIPSKIVGTIYESKEEQLLPAPPPASGGSSILPMRPLLRGYNSHVTLPTRGARGGHHPHQSYLDFCESDIGQGYCSDGDALRVGSSPGGSRFHDIDNGYLSEGSSGLNGPSSSAGGISPGKHFLSMMRARTQLPTTIEERIRNSRGSLDSIGTAANGSSAASQASSSGGSTTTHAQNNNNNNNNNSGGGAKMDGSPHHRPGSRNGRDNWSKMPEPLNGQKVEKSDKSSPSRRSMGGGGSGSSSKQGSPSSSSRTKGVPPSFGYVKRANGSIASTAEQQNIAMMMAAGGAGANGLPCGRTAHVSAVPRTASGRKVAGGTQTLPNDMNKLPPNTQHRSFSLTGPTATQLSQSIRERLATGSHSLPKPGSDLHVFQHRISNRGGTRHDGSLSDTQTYAEVKPEYSSYAMWLKHSNTAGSRLSDGESVEQLQIGSPALTRHGHKMIHNRSGGPGQMAGQMSGNESPYVQSPRMNRSNSIRSTKSEKMYPSMMSRAGEVEIEPYYCLPVGTNGVLTAQMAAAMAAQSQAAQGNPGVGVNVGGVAWSQPTSPTPLTRGPFNTAAGASVLSPTHGTTSAAGLVGPGGGAGGGAMVGHRLTYPKKNDEVHGSAASLLSGGSSLYGNAEERQAHEIRRLKRELQDARDQVLSLSSQLSTNAHVVTAFEQSLSNMTNRLHQLTATAERKDGELTDMRQTIELLRKQSIQAGLTTAHMQSMGVQTQGQGQVQGQALGQALGQPGSDQKPPNSGSQRAINANNGSMPLGMQRQHSTDSMCSLNSISSGCSAAQDKNKANKKKGWLRSSFTKAFSRNAKISKTSRHVGHHHHHNHSQQELASGKLPLHNGHGEPLGLASLATQPAPPLPNSKQSSPAKTVTLIDNAKPIDAIDQEDQHVVEDLKKQLREKDLVLTDIRLEALSSASQLESLKEMMNKMRAEMMSLKHNNERLQKLVTTRSLAGSEASLGQAISPNGSVAGSSEVSRRYSLADSNSRPPMELPARLSEELELEEDCLPPAPAPEQPPPPAPNGVSVAPLSPSTHVDLTPPPPALEAAPMASPVHMASATEELADVCDGKKIAIACYLGQPEAFAKYCEELQELDGFYANGHEADSQSQSERKSNYTSASCNEFVIACTYISGKTTWQNLDYVVRKTFKDYVARIDPGTNLGLNTDSITSYHLGEAKRGPEMGFPELLPCGYIVGSVRTLYICLQGVGSLAFDSLIPRSIVHRYISLLTEHRRLILCGPSGTGKSYLARRLAEFLVARSARGNPSEAIATFNVDHKSSKDLRQYLGHIAEQAAIANGVSELPSVIILDNLHHASALGDVFSCLLSAGPANKLPCIIGTMSQATCNTTNLQLHHNFRWVLTANHMEPVKGFLGRFLRRRLFQLELQTQHPQPELAAVLAWLPSVWQHINRFLEVHSSSDVTIGPRLFLACPMDLKDSQVWFTDIWNYHLSPYLVEAVREGVQLYGRRGGAWNDPSAFIRNSYPWPYGPDSVPPLRQINAEDVGLEGVALTNGDQQDPLLNMLMRLQEAANYSEAQDQESDCASLDSNVTPESSAGAE
Protein: Secretin PulD (General secretion pathway protein D) (Pullulanase secretion envelope PulD) (Type II secretion system protein D) (T2SS protein D) (P15644)
Organism: Klebsiella pneumoniae
Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of pullulanase. This subunit forms the outer membrane channel (By similarity).
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:2677007}. Note=Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane. {ECO:0000250|UniProtKB:P45779}.
Interaction partners:
Sequence:
MIIANVIRSFSLTLLIFAALLFRPAAAEEFSASFKGTDIQEFINTVSKNLNKTVIIDPSVRGTITVRSYDMLNEEQYYQFFLSVLDVYGFAVINMNNGVLKVVRSKDAKTAAVPVASDAAPGIGDEVVTRVVPLTNVAARDLAPLLRQLNDNAGVGSVVHYEPSNVLLMTGRAAVIKRLLTIVERVDNAGDRSVVTVPLSWASAADVVKLVTELNKDTSKSALPGSMVANVVADERTNAVLVSGEPNSRQRIIAMIKQLDRQQATQGNTKVIYLKYAKASDLVEVLTGISSTMQSEKQAAKPVAALDKNIIIKAHGQTNALIVTAAPDVMNDLERVIAQLDIRRPQVLVEAIIAEVQDADGLNLGIQWANKNAGMTQFTNSGLPISTAIAGANQYNKDGTVSSSLASALSSFNGIAAGFYQGNWAMLLTALSSSTKNDILATPSIVTLDNMEATFNVGQEVPVLTGSQTTSGDNIFNTVERKTVGIKLKVKPQINEGDSVLLEIEQEVSSVADAASSTSSDLGATFNTRTVNNAVLVGSGETVVVGGLLDKSVSDTADKVPLLGDIPVIGALFRSTSKKVSKRNLMLFIRPTVIRDRDEYRQASSGQYTAFNDAQSKQRGKENNDAMLNQDLLEIYPRQDTAAFRQVSAAIDAFNLGGNL
Protein: Ephrin-A5 (AL-1) (EPH-related receptor tyrosine kinase ligand 7) (LERK-7) (O08543)
Organism: Mus musculus (Mouse)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Membrane, caveola {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Compartmentalized in discrete caveolae-like membrane microdomains. {ECO:0000250}.
Interaction partners:
- Ephrin type-A receptor 2
- Ephrin type-A receptor 3
- Ephrin type-A receptor 4
- Ephrin type-B receptor 2
- Ephrin type-A receptor 5
- Ephrin type-A receptor 1
- Ephrin type-A receptor 7
- Ephrin type-A receptor 8
- BDNF/NT-3 growth factors receptor
- Regulatory-associated protein of mTOR
Sequence:
MLHVEMLTLLFLVLWMCVFSQDPGSKVVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL
Protein: Cu-binding protein (A0A1D8PTX2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|PIRNR:PIRNR037736}.
Interaction partners:
- Cox11p
- Cytochrome c oxidase subunit 2
- Copper metallochaperone
- Cox15p
- SURF1-like protein
- Cytochrome c
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase subunit 1
- Copper metallochaperone
- Cytochrome c oxidase subunit 3
Sequence:
MLSRLALRSTIRSGTILQSSRLFSVSTGRSQEQQPQKSTNNEPAAKPKKRPLSRVAIGGSSDHNKKGFGMSVEFATWKAVLLLLTVGGLGAYYFQKEKERLHKRREMEANKSIGTPLIGGPFTLQDTKGNKFTEQNLVDPNNKRFSILYFGFTHCPDVCPEELDKLGDMLDKLAKDGIPIQPVFITCDPARDTPEVLDAYLKDFHPGIIGLTGTFEQVKNTCKKFRVYFSTPPDVKPGQDYLVDHSIFFYLIDPEGNFVDVIGRESEALESATKIAKYSDAFIPEKERVQKKEGIFGFLYK
Protein: 5-hydroxytryptamine receptor 2A (5-HT-2) (5-HT-2A) (5-hydroxytryptamine receptor) (Serotonin receptor 2A) (O46635)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15862800}; Multi-pass membrane protein {ECO:0000269|PubMed:15862800}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35363}. Cell projection, axon {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P14842}. Membrane, caveola {ECO:0000250|UniProtKB:P14842}. Presynapse {ECO:0000250|UniProtKB:P14842}.
Interaction partners:
- 5-hydroxytryptamine receptor 2C
- Uncharacterized protein.
- Guanine nucleotide-binding protein G
- Voltage-dependent L-type calcium channel subunit alpha
- 5-hydroxytryptamine receptor 2B.
- Voltage-dependent L-type calcium channel subunit alpha
- Voltage-dependent L-type calcium channel subunit alpha
- Voltage-dependent L-type calcium channel subunit alpha
- G protein subunit alpha 14.
Sequence:
MDVLFEDNAPLSPTTSSLMPSNGDPRLYGNDLNAGDANTSDAFNWTVDAENRTNLSCEGCLSPPCFSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDPGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDIIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKKDAKSTDNDYSMVALGKQHSEDAPTDNINTVNEKVSCV
Protein: PLATZ transcription factor family protein (F4I7U9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- B3 domain-containing protein REM-like 3
- B3 domain-containing protein REM22
- B3 domain-containing protein At5g60140
- Transmembrane protein
- B3 domain-containing protein At2g36080
- NAC domain-containing protein 41
- At4g28530
Sequence:
MVREGEEEEEMMMMMATKPAWLEGLMAETFFSSCGIHETRRKSEKNVFCLLCCLSVCPHCLPSHRSHPLLQVRRYVYHDVVRLSDLEKLIDCSYVQPYTINGAKVIFLNQRQQSRAKVSSNVCFTCDRILQEPFHFCSLSCKVDYLSYQGDDLSSILYRIDESDFTFEGLRMDGHDQLGEISTMEDGEDILVISDESEQGNNSHKKEKKKSKKKKPESNYLPGMVLSSLGNRRKGAPHRAPFS