wanglab/gogpt-training-data huggingface dataset:
Protein: DASH complex subunit spc19 (Outer kinetochore protein spc19) (Q50HP3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. May be necessary for growth under high osmotic stress.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q03954}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q03954}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q03954}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore. Kinetochore association occurs only during mitosis (By similarity). In the cytoskeleton, localizes to cortical microtubules (Probable). {ECO:0000250|UniProtKB:Q03954, ECO:0000305|PubMed:20624975}.
Interaction partners:
- DASH complex subunit dad4
- DASH complex subunit dad3
- DASH complex subunit dad2
- DASH complex subunit dam1
- DASH complex subunit ask1
- DASH complex subunit duo1
- DASH complex subunit dad1
- Kinetochore protein ndc80
- DASH complex subunit DAD5
- DASH complex subunit spc34
Sequence:
MSYLDGLQQCVDSLQISIGTLSSSIDTLESGIHDFPRIKHILKVQRHFNLISEDELSARQAKFEEIVKPILSKAFQRLEDSISSLQRQEDSLKTKYELQEARLDMLKNRPATSAFSVTTESSEQLKAIIAKRQKLVYTLERYTLQLQQKRGH
Protein: LexA repressor (EC 3.4.21.88) (Q9PH24)
Organism: Xylella fastidiosa (strain 9a5c)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- Recombination-associated protein RdgC
- DNA repair protein RecN
Sequence:
MSLSDIQQAILSLITNHINADGVSPSQTEIARAFGFKGVRAVQHHLDVLEQQGMIRRVPRQARGIRLKHLTEVDETALALQSEDVLRLPVLGRVAAGQPIGADIGEGRVVLLDRVFFSPAPDYLLRVQGDSMRDEGIFDGDLIGVHRTQDAHSGQIVVARIDDEITVKLLKISKDRIRLLPRNPDFAPIEVRSDQDFAIEGLYCGLLRPNR
Protein: Protein RALF-like 33 (Q8L9P8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant activation of some intracellular mitogen-activated protein kinases (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Secreted transmembrane peptide 5
- Succinate dehydrogenase assembly factor 4
- tRNA N
- Transcription factor bHLH99
- AT1G25275 protein
- At3g13845
- Transmembrane protein
- Small polypeptide DEVIL 10
- AT4g05070 protein
- Transmembrane protein
Sequence:
MRGLSTKPVAIIIAILTVHFLFAAVTSQSSGDFVPIESKCNGTIAECSLSTAEEEFEMDSEINRRILATTKYISYGALRRNTVPCSRRGASYYNCRRGAQANPYSRGCSAITRCRR
Protein: Calsequestrin-1 (Calmitine) (Calsequestrin, skeletal muscle isoform) (P31415)
Organism: Homo sapiens (Human)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:27185316, ECO:0000269|PubMed:28895244}. Sarcoplasmic reticulum {ECO:0000269|PubMed:27196359}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07221}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P07221}. Mitochondrion matrix {ECO:0000250|UniProtKB:O09165}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells. Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells (PubMed:28895244). In a minority of cells, homogeneously detected in the ER lumen (PubMed:28895244). Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium (PubMed:27185316). {ECO:0000250|UniProtKB:P07221, ECO:0000269|PubMed:27185316, ECO:0000269|PubMed:28895244}.
Interaction partners:
- Aspartyl/asparaginyl beta-hydroxylase
- Triadin
- Ryanodine receptor 1
- Ryanodine receptor 2
- Ryanodine receptor 3
- Calsequestrin-2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Myosin light chain 1/3, skeletal muscle isoform
- Sarcalumenin
- Junctional sarcoplasmic reticulum protein 1
Sequence:
MSATDRMGPRAVPGLRLALLLLLVLGTPKSGVQGQEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEVDSMYVFKGDEVIEYDGEFSADTIVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKSKDSEHYKAFEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGFEFLETLKAVAQDNTENPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDDDDD
Protein: Mitochondria-eating protein (Spermatid-expressing gene 1 protein) (Spetex-1) (Spermatogenesis-associated protein 18) (Q6AYL6)
Organism: Rattus norvegicus (Rat)
Function: Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). May have a role in spermatogenesis, especially in cell differentiation from late elongate spermatids to mature spermatozoa.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8TC71}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TC71}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q8TC71}. Note=Localizes to the cytosol under normal conditions. Relocalizes to mitochondrion outer membrane following cellular stress. May form molecular condensates in the mitochondrial matrix. Colocalizes with BNIP3 and BNIP3L at the mitochondrion outer membrane. {ECO:0000250|UniProtKB:Q8TC71}.
Interaction partners:
- Sperm microtubule inner protein 10
Sequence:
MAENLKKLAQSESFLSLQDKVCFWANDYQTNSCDQNLNCCIELIEQVAKVQAQLFAILTATAQEGGHNEGVETIKSRLLPLLQTSFSSLGVGKIIQTEIRPIQDFQLRSKNRQSSLDQEQQQSDGDSFIESQPTQVQDDLTESGKNLEGTKNGSAISLLAAEEEINQLKKQLKSLQAQEDARHKTSENRRAEISRTDRRPSGKRNSERPQDVVSNYEKHLKNLKDEIAVLSAEKSGLQASHRQTRSRSPSPGPRGPRGPRGRRRSRSHSRSHSRSHSRSHSHSNSHSNSRSNSPCTTVAKIRSPSPNRSKMSSVARKAALLSRFSDAYSQARLDAQCLLRRCIDRAETVQRIIYIATVEAFHIAKMAFRHFKIRVRKMLTPSHVGSNDFETAVSDYIVCHLDLYDSQSSVNDVIRAMNVNPKISFPPEVDFCLLTDFIQEICCIAFAMQSLEPPLDIAFGADGEVFNEAKYRRSYDSDFTAPLVFYHVWPALMENDCVIMKGEAVTKRGAFWTTVRPVMRCRSRSLSPICPRSRFGISTVSRSRSPSPIRCTFARY
Protein: TAF4 (Q5UEC5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSIISLEVPIQPYAGQLLIINDLILPDSGSQDASKAKVSIKKNQRASFFDRSSIYKKIMKHLSQGNQADDINISEQEWLLDSFLAALETYMKHVVKKTIELCEHRTSYHLHNDERCVMKNDMRVTMMFLNDLEIADYGSSDDETGFYRKRRAENIDEERKVARLESVNDTALLAISGRKRPGEQLAPESAPSGSKVAKLTGAPIQRACAPRFKHMNIRDVLQFMEEDRRYARSNMLFEAFLKYKS
Protein: Naphthalene 1,2-dioxygenase system, large oxygenase component (EC 1.14.12.12) (ISP NAP) (Naphthalene 1,2-dioxygenase ISP alpha) (Naphthalene 1,2-dioxygenase subunit alpha) (ND subunit alpha) (NDO subunit alpha) (P0A110)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene.
Interaction partners:
Sequence:
MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR
Protein: IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 (B7FAS2)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MYNSLDRRGSLTIGTWEIRDILHPPRQRRKTYDTLEEMFNARYRNIKEKKAAKMTYRAMIYNCLERPTGWKCFLYHFSVFLIVLICLILSVLSTVEEHSHFAAELLYILEIVLVVFFSVEFIVRLWSAGCRSKYIGVYGRLKFVRKPITLIDLVVVICSLFVICFGTEGQVFAASAMRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDHIGVDGRQAFTSYADALWWGVITMTTIGYGDVVPQTWLGRIVASCFSIFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAATLIQCLWRCHAAEKKVSATWNAHIDPLAHETKETHHWNGKKHASSMDSNNLTRKRQLFKKQSSLVNTFRRKGSPSTDVEMGELQQERLLRHERNSDTDDEKRIYRVGADIEIDYETEEPTTPTRPQGHISHVCELTDAHRNAIRAIRRVKYFVARRRFQQARKPYDVRDVIEQYSQGHLNMMVRIKELQRRLDQTLGKPGQYDGKGSRKGHPVTIGSRLSRLELQMSSLDRKVESSNRTLNALYRLMADRNSLTISPSPPALISRPVSPAACLSPRDQLSPTSISSQRSGSPGWQ
Protein: GTP-binding protein (Interferon gamma inducible protein 47) (Interferon-gamma-inducible GTPase Ifggc1 protein) (Q61635)
Organism: Mus musculus (Mouse)
Interaction partners:
- Predicted gene 5431
- Immunity-related GTPase family M protein 2
- Immunity-related GTPase family M protein 3
- Guanylate-binding protein 3
- Guanylate-binding protein 2
- Interferon-inducible GTPase 1
- Protein mono-ADP-ribosyltransferase PARP14
- Immunity-related GTPase family M protein 1
- Guanylate-binding protein 7
- Receptor-transporting protein 4
Sequence:
MDQFISAFLKGASENSFQQLAKEFLPQYSALISKAGGMLSPETLTGIHKALQEGNLSDVMIQIQKAISAAENAILEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPYQHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANYDFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQKAKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPNISDASIELKKHFLREKIWLEALKSAAVSFIPFMTFFKGFDLPEQEQCLKDYRSYFGLDDQSIKEIAEKLGAPLADIKGELKCLDFWSLVKDNSIIAQATSAAEAFCAVKGGPESSAFQALKVYYRRTQFLNIVVDDAKHLLRKIETVNVA
Protein: Histone H2A type 2-A (H2A-clustered histone 18) (H2A-clustered histone 19) (Histone H2A.2) (Histone H2A/o) (Q6FI13)
Organism: Homo sapiens (Human)
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:
- Histone H3.1t
- Histone H3.3
- Histone H4-like protein type G
- Histone H3.2
- Histone H3.1
- Histone H4
- TP53-binding protein 1
- Histone H2B type 2-E
- Histone H3-7
- Histone H3.3C
Sequence:
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
Protein: Histone deacetylase 7 (HD7) (EC 3.5.1.98) (Histone deacetylase 7A) (HD7a) (Protein deacetylase HDAC7) (EC 3.5.1.-) (Q8WUI4)
Organism: Homo sapiens (Human)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3. Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding. In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response.
Subcellular location: Nucleus {ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:16980613}. Cytoplasm {ECO:0000269|PubMed:16980613}. Note=In the nucleus, it associates with distinct subnuclear dot-like structures (PubMed:11262386). Shuttles between the nucleus and the cytoplasm (PubMed:16980613). In muscle cells, it shuttles into the cytoplasm during myocyte differentiation (By similarity). The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (PubMed:16980613). {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:16980613}.
Interaction partners:
- Histone acetyltransferase KAT5
- Hepatocyte nuclear factor 3-alpha
- Myocyte-specific enhancer factor 2A
- Nuclear receptor corepressor 1
- Forkhead box protein P3
- Histone acetyltransferase p300
- Nuclear receptor corepressor 2
- Hypoxia-inducible factor 1-alpha
- Histone deacetylase 1
- Histone deacetylase 2
Sequence:
MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSVAPFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGGTLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEPLPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVVDDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSRHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL
Protein: Autophagy protein 13 (Meiotically up-regulated gene 78 protein) (O36019)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen, thus ensuring that they can adapt and subsequently propagate. Finally, atg13 is also required for glycogen storage during stationary phase and has a role in meiosis and sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Preautophagosomal structure {ECO:0000269|PubMed:23950735}.
Interaction partners:
- Autophagy-related protein 101
- Autophagy-related protein 17
- Serine/threonine-protein kinase atg1
- Taz1-interacting factor 1
- Autophagy-related protein 9
- Putative lipase atg15
- Vacuolar protein 8
- Serine/threonine-protein kinase tor2
- Serine/threonine-protein kinase tor1
- Target of rapamycin complex 1 subunit mip1
Sequence:
MPRLNTQLPRMYSAPPGHSKAVSTELNKDLSSVGGRSAKLGQVIHHCFYKTGLIILESRLNVFGTSRPRESSKNNKWFNLEIVETELYAEQFKIWKNIELSPSRKIPPMVLHTYLDISDLSKNQTLSVSDGTHSHAINFNNMSTMKIVLERWIVNLDGEALSTPLELAVLYKKLVVLFRSLYTYTHLMPLWKLKSKIHKLRAHGTSLKVGCALSTDDVLSNDFLPISAPISSSLGSSIATFSFSPVGTPAGDFRISVQYRKNCHFEVHDSDALLSNQLLSADKHQLAASNNSQDFEDGKQYDQPPPSFATRLAKQSDPNSLLQSEIQHLASIESITAQAAPLVTIHPFKSPSLSASPGSNFDNMSISPKVAVNRYIHRGPSATSLNKFSMISDAASKSRAKLPPLTSGSLKLNTLDISNTPNLRRFSSSFGPRERKESFSSRNRLPLVNHPIRSIFKHNVSENPITDHSEHAVYDSEFASKDDLSGFIQLLDSHAHHLNASEGSKSSGSFPGKVQTLTSGISPVAHPHNSLGSSNEIFDIDTYNHSIDNSGSRFTEAVKHNLGNSSHSIMRHHTLGTLRSRPSFSEKSTFPAPLTSISQASTFQGDNRSPSTVIPHTQTEVPSANDTSKQLASLHDMRKSQSPICARSATSAGLPRFEYHTSLSKSLEHSSTPASLQATKTPSPSFVLEPGIPQEYKKHFDNLSEERRQCLTPSTPTYEYYNEHNPNYDDDLLFTMTDMTLEPHDVSAIRLGSPKSDD
Protein: Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)] (P61809)
Organism: Mus musculus (Mouse)
Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution.
Subcellular location: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}.; SUBCELLULAR LOCATION: [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
Interaction partners:
- Cyclin-dependent kinase 5
- Microtubule-associated protein
- Calpain-1 catalytic subunit
- Calpain-2 catalytic subunit
- Cellular tumor antigen p53
- Transcription factor Jun
- Lamin-B1
- Prelamin-A/C
- Peroxiredoxin-2
- Golgin subfamily A member 2
Sequence:
MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
Protein: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) (A0A1D8PRQ1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Adenylosuccinate lyase
- Phosphoribosylaminoimidazole carboxylase
- Bifunctional aminoimidazole ribotide synthase/glycinamide ribotide synthase
- Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- Tyrosine--tRNA ligase
- Adenylosuccinate synthetase
- C-1-tetrahydrofolate synthase, cytoplasmic
Sequence:
MTSTNLEGTFPLIARGKVRDIYQVDDNTLLFVATDRISAYDVIMANGIPNKGKILTKLSEFWFAFLPIENHLIKGDIFEKYPQLEKYRDQLEGRSLLVRKLKLIPLEVIVRGYITGSGWKEYTKSKTVHGIPIGDVVESQQITPIFTPSTKAEQGEHDENITKEQADKIVGKELCDRIEKIAIDLYTKARDYAATKGIIIADTKFEFGLDGDKIVLVDEVLTPDSSRFWSAAKYKLGQSQESYDKQFLRDWLTANGVAGKDGVAMPEDIAVQTKQKYVEAYENLTGEKWQD
Protein: UPF0352 protein YejL (P0AD24)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Inner membrane protein YejM
- Nucleoid-associated protein YejK
- RNA chaperone ProQ
- Negative modulator of initiation of replication
- Lipopolysaccharide assembly protein A
- DNA mismatch repair protein MutH
- Lipopolysaccharide export system protein LptC
- Fatty acid metabolism regulator protein
- Met repressor
- Regulator of ribonuclease activity B
Sequence:
MPQISRYSDEQVEQLLAELLNVLEKHKAPTDLSLMVLGNMVTNLINTSIAPAQRQAIANSFARALQSSINEDKAH
Protein: Glycinin G1 (Glycinin 11S G1) (Glycinin A1aB1b) (allergen Gly m 6) [Cleaved into: Glycinin A1a subunit (Glycinin acidic 1a subunit); Glycinin Bx subunit (Glycinin basic x subunit) (Glycinin B1b subunit) (Glycinin basic 1b subunit)] (P04776)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Glycinin is the major seed storage protein of soybean. Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:29348620}. Protein storage vacuole {ECO:0000269|PubMed:29348620}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles. {ECO:0000269|PubMed:29348620}.
Interaction partners:
- Beta-conglycinin alpha' subunit
- Uncharacterized protein
- Beta-conglycinin beta subunit 1
- Beta-conglycinin alpha subunit 1
- 2S seed storage albumin protein
- Bowman-Birk type proteinase inhibitor
- Kunitz trypsin inhibitor
- Kunitz-type trypsin inhibitor KTI1
- Uncharacterized protein
- Beta-conglycinin alpha subunit 2
Sequence:
MAKLVFSLCFLLFSGCCFAFSSREQPQQNECQIQKLNALKPDNRIESEGGLIETWNPNNKPFQCAGVALSRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSGFTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRPRGSQSKSRRNGIDETICTMRLRHNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLRLSAEFGSLRKNAMFVPHYNLNANSIIYALNGRALIQVVNCNGERVFDGELQEGRVLIVPQNFVVAARSQSDNFEYVSFKTNDTPMIGTLAGANSLLNALPEEVIQHTFNLKSQQARQIKNNNPFKFLVPPQESQKRAVA