wanglab/gogpt-training-data huggingface dataset:
Protein: 5'-AMP-activated protein kinase catalytic subunit alpha-2 (EC 2.7.11.1) (EC 2.7.11.31) (Acetyl-CoA carboxylase kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (Q2LAI0)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- 5'-AMP-activated protein kinase beta-2 non-catalytic subunit transcript variant 2
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase subunit gamma-1
- Uncharacterized protein.
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- Serine/threonine-protein kinase STK11
- Regulatory associated protein of MTOR complex 1.
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- TSC complex subunit 2.
- Serine/threonine-protein kinase TOR
Sequence:
MAEKQQKHDGRVKIGHYVLGDTLGVGTFGKVKVGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVISTPTDFFMVMEYVSGGELFDYICKHGRVEEAEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLLMHMLQVDPLKRATIKDIREHEWFKEELPSYLFPEDPSYDATVIDDDAVREVCEKFECTESEVMNSLYSGDPQDQLAVAYHLVIDNRRIMNQASEFYLASSPPTGSFMDDTMHIPPGVKPHPERMPPLIADSPKARCPLDALNTTKPKPLTVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVVNSYHLRVRRKNPVTGNYVKMSLQLYQVDNRSYLLDFKSIDDEVMEQRSGSSTPQRSCSAAGLHRPRLSIDAAAAAECQSLMGSLSGSFVGSISSVPPRLGSHTMDFFEMCASLIMALAR
Protein: Protein NDNF (Neuron-derived neurotrophic factor) (Q8TB73)
Organism: Homo sapiens (Human)
Function: Secretory protein that plays a role in various cellular processes. Acts as a chemorepellent acting on gonadotropin-releasing hormone (GnRH) expressing neurons regulating their migration to the hypothalamus. Also promotes neuron migration, growth and survival as well as neurite outgrowth and is involved in the development of the olfactory system. May also act through the regulation of growth factors activity and downstream signaling. Also regulates extracellular matrix assembly and cell adhesiveness (By similarity). Promotes endothelial cell survival, vessel formation and plays an important role in the process of revascularization through NOS3-dependent mechanisms.
Subcellular location: Secreted {ECO:0000269|PubMed:20969804, ECO:0000269|PubMed:24706764, ECO:0000269|PubMed:31883645}.
Interaction partners:
Sequence:
MVLLHWCLLWLLFPLSSRTQKLPTRDEELFQMQIRDKAFFHDSSVIPDGAEISSYLFRDTPKRYFFVVEEDNTPLSVTVTPCDAPLEWKLSLQELPEDRSGEGSGDLEPLEQQKQQIINEEGTELFSYKGNDVEYFISSSSPSGLYQLDLLSTEKDTHFKVYATTTPESDQPYPELPYDPRVDVTSLGRTTVTLAWKPSPTASLLKQPIQYCVVINKEHNFKSLCAVEAKLSADDAFMMAPKPGLDFSPFDFAHFGFPSDNSGKERSFQAKPSPKLGRHVYSRPKVDIQKICIGNKNIFTVSDLKPDTQYYFDVFVVNINSNMSTAYVGTFARTKEEAKQKTVELKDGKITDVFVKRKGAKFLRFAPVSSHQKVTFFIHSCLDAVQIQVRRDGKLLLSQNVEGIQQFQLRGKPKAKYLVRLKGNKKGASMLKILATTRPTKQSFPSLPEDTRIKAFDKLRTCSSATVAWLGTQERNKFCIYKKEVDDNYNEDQKKREQNQCLGPDIRKKSEKVLCKYFHSQNLQKAVTTETIKGLQPGKSYLLDVYVIGHGGHSVKYQSKVVKTRKFC
Protein: PHO85 cyclin-8 (Q08966)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL10, negatively controls glycogen accumulation under favorable growth conditions. Involved in phosphorylation and negative regulation of glycogen synthase GSY2. Also has minor GLC8 kinase activity.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Cyclin-dependent protein kinase PHO85
- PHO85 cyclin-6
- PHO85 cyclin CLG1
- PHO85 cyclin-9
- PHO85 cyclin-5
- Cyclin-dependent kinase 1
- PHO85 cyclin PHO80
Sequence:
MANDQDPNKSLINDALTRSMSEFYDDDDDNDSDMCRANDEGEDVFDLPLKVGVSQSRNFSEVNDVLDPLSSLHGPSKKVRFEQQKQQQQHQQLHNDFNTDFNLKSPSSKKMGVEQLIQSANEINDYLANNIDKVNSFNSELLSGSGKLPGRVKSDTATQGTGRLDSMSNFALSDTELDNDDDNYLLDPLANASSTTPTVEHHGYSLLDKALSTSDKEKIYTNKVNSNSQIDTDNHSHESGNTTNNETDENESSEILDYTKFDSFPYPPSSAPNGEPPDLKVLSIECEQENEKELRRISLLLDHYESIPKIPELSDDEALSKFRENIELILQLSKKINDNANTLAISSEDPQKFVNFVMKNPPSLSFRDFIDRIQNKCMFGAVVYLGATYLLQLVFLTRDEMDGPIKLKAKLQEDQAHRIIISTIRIATKLLEDFVHSQNYICKVFGISKRLLTKLEISFMASVNFDGLMITCEKLEKTLHILDDTRQALGNT
Protein: Gasdermin-D (Gasdermin domain-containing protein 1) [Cleaved into: Gasdermin-D, N-terminal (GSDMD-NT) (hGSDMD-NTD); Gasdermin-D, C-terminal (GSDMD-CT) (hGSDMD-CTD); Gasdermin-D, p13 (Gasdermin-D, 13 kDa) (13 kDa GSDMD); Gasdermin-D, p40] (P57764)
Organism: Homo sapiens (Human)
Function: Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-D, N-terminal) binds to membranes and forms pores, triggering pyroptosis.
Subcellular location: [Gasdermin-D]: Cytoplasm, cytosol {ECO:0000269|PubMed:27281216}. Inflammasome {ECO:0000250|UniProtKB:Q9D8T2}. Note=In response to a canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 inflammasone with similar kinetics to that of uncleaved CASP1 precursor. {ECO:0000250|UniProtKB:Q9D8T2}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cell membrane {ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:32109412, ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:36227980, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38599239}; Multi-pass membrane protein {ECO:0000269|PubMed:33883744, ECO:0000305|PubMed:29898893}. Secreted {ECO:0000250|UniProtKB:Q9D8T2}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9D8T2}. Note=Released in the extracellular milieu following pyroptosis. {ECO:0000250|UniProtKB:Q9D8T2}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cytoplasm, cytosol {ECO:0000269|PubMed:36227980}. Note=(Microbial infection) Upon infection by M.tuberculosis, localization to cell membrane is prevented by M.tuberculosis phosphatase PtpB that catalyzes dephosphorylation of phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol 4-phosphate, thereby inhibiting the membrane targeting of Gasdermin-D, N-terminal and subsequent cytokine release and pyroptosis. {ECO:0000269|PubMed:36227980}.; SUBCELLULAR LOCATION: [Gasdermin-D, p13]: Nucleus {ECO:0000250|UniProtKB:Q9D8T2}.; SUBCELLULAR LOCATION: [Gasdermin-D, C-terminal]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9D8T2}.
Interaction partners:
- Caspase-1
- Caspase-4
- NACHT, LRR and PYD domains-containing protein 3
- Caspase-5
- Interferon-inducible protein AIM2
- NLR family CARD domain-containing protein 4
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 1
- Interleukin-1 beta
- Interleukin-18
Sequence:
MGSAFERVVRRVVQELDHGGEFIPVTSLQSSTGFQPYCLVVRKPSSSWFWKPRYKCVNLSIKDILEPDAAEPDVQRGRSFHFYDAMDGQIQGSVELAAPGQAKIAGGAAVSDSSSTSMNVYSLSVDPNTWQTLLHERHLRQPEHKVLQQLRSRGDNVYVVTEVLQTQKEVEVTRTHKREGSGRFSLPGATCLQGEGQGHLSQKKTVTIPSGSTLAFRVAQLVIDSDLDVLLFPDKKQRTFQPPATGHKRSTSEGAWPQLPSGLSMMRCLHNFLTDGVPAEGAFTEDFQGLRAEVETISKELELLDRELCQLLLEGLEGVLRDQLALRALEEALEQGQSLGPVEPLDGPAGAVLECLVLSSGMLVPELAIPVVYLLGALTMLSETQHKLLAEALESQTLLGPLELVGSLLEQSAPWQERSTMSLPPGLLGNSWGEGAPAWVLLDECGLELGEDTPHVCWEPQAQGRMCALYASLALLSGLSQEPH
Protein: AAA ATPase domain-containing protein (Q58A41)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MHIPVVGETPDDAVNQLAEKVENANVEDKEGEIKACVAEPHDGEVTKGNGEEEEPKIKEDLKVQLEPKVEKIETPKNTNILVLGSTGVGKSTFISSLVNYLKYESLEQAMNLASLDNVATIPNKVQIVDSNNVSHSFVVGKSKYLSQEHKDGESVTVKPKRYVIDMGNNKTMTILDTPGVADTRGCKQDDLNFEVILKELSEFEELHGILILLRSTDNRINTMYKYCINELLHHLHYSAKNNIFFCFTNTRSSMYRAGPALTLLQTHLESMVHHTDVKMETTGRVFNFENEAFNVLASKLNGANFSEEDIEVYSHSWKRSSSEATKLMNTILSTPPHRVKDTECINNTREMIRKMGTPIHFCLTSIQRFLYNIEQQNENIRKHKDDLEKLKPYVMAQLDKLVWEQLDEPAVFCNKLGCHKTSKMDTPKGAKEFVGRHCSASFKNKINKSSSLYWHHTFGILGGCKECGCSYKDHSVSDIVHVKEAIQVIDEGIKGKILSKEELTAVANRRVKENLELKEKYSQEFEVLSNAFAKFAIFVAHNSLVAVNHDYAEYLQLEIKNLKESPNVKDREKQLEKLNEILKSHQIELDTFEAARSKEKEGLSPHDINLLGEEVLSLEISGRIIKDIQSHNEKQKYASSKKVKNVKITLNKQVESAIKWLLN
Protein: Ubiquitin-conjugating enzyme E2 R2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme R2) (Ubiquitin carrier protein R2) (Ubiquitin-conjugating enzyme E2-CDC34B) (Ubiquitin-protein ligase R2) (Q712K3)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin.
Interaction partners:
- Polyubiquitin-C
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-conjugating enzyme E2 R1
- Ubiquitin D
- Ubiquitin-like modifier-activating enzyme 7
Sequence:
MAQQQMTSSQKALMLELKSLQEEPVEGFRITLVDESDLYNWEVAIFGPPNTLYEGGYFKAHIKFPIDYPYSPPTFRFLTKMWHPNIYENGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMFRKWRDSKGKDKEYAEIIRKQVSATKAEAEKDGVKVPTTLAEYCIKTKVPSNDNSSDLLYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES
Protein: Peptidyl-prolyl cis-trans isomerase CYP40 (PPIase CYP40) (EC 5.2.1.8) (Cyclophilin of 40 kDa) (AtCYP40) (Cyclophilin-40) (Protein SQUINT) (Rotamase CYP40) (Q9C566)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in promoting the expression of the juvenile phase of vegetative development, and, to a lower extent, in regulating the positioning of floral buds, floral morphogenesis and the expression of HSPs. Collaboratively with RBL and ULT1, influences floral meristem (FM) determinacy in an AGAMOUS and SUPERMAN-dependent manner, thus contributing to the floral developmental homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18441215}.
Interaction partners:
- Co-chaperone protein p23-1
- Heat shock protein 90-1
- Co-chaperone protein p23-2
- Heat shock protein 90-6, mitochondrial
- Heat shock protein 90-5, chloroplastic
- Heat shock protein 90-2
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- At2g29210/F16P2.41
- Heat shock protein 90-4
- Aha1 domain-containing protein
Sequence:
MGRSKCFMDISIGGELEGRIVIELYDDVVPKTAENFRLLCTGEKGLGPNTGVPLHYKGNRFHRVIKGFMIQGGDISANDGTGGESIYGLKFDDENFELKHERKGMLSMANSGPNTNGSQFFITTTRTSHLDGKHVVFGRVTKGMGVVRSIEHVSIEEQSCPSQDVVIHDCGEIPEGADDGICDFFKDGDVYPDWPIDLNESPAELSWWMETVDFVKAHGNEHFKKQDYKMALRKYRKALRYLDICWEKEGIDEETSTALRKTKSQIFTNSAACKLKFGDAKGALLDTEFAMRDEDNNVKALFRQGQAYMALNNVDAAAESLEKALQFEPNDAGIKKEYAAVMKKIAFRDNEEKKQYRKMFV
Protein: Transmembrane emp24 domain-containing protein p24beta2 (p24 family protein beta1) (p24beta1) (p24 family protein beta2) (p24beta2) (Q9S7M9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side (By similarity). Interacts with p24delta5 at endoplasmic reticulum export sites for endoplasmic reticulum exit and coupled transport to the Golgi apparatus.
Subcellular location: Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein. Note=Cycles between the endoplasmic reticulum and Golgi via COPI and COPII dependent pathways.
Interaction partners:
- Transmembrane emp24 domain-containing protein p24delta7
- Transmembrane emp24 domain-containing protein p24delta11
- Transmembrane emp24 domain-containing protein p24delta3
- Transmembrane emp24 domain-containing protein p24delta9
- Transmembrane emp24 domain-containing protein p24delta10
- Transmembrane emp24 domain-containing protein p24delta5
- Transmembrane emp24 domain-containing protein p24delta4
- Transmembrane emp24 domain-containing protein p24delta6
- ER lumen protein-retaining receptor A
- Emp24/gp25L/p24 family/GOLD family protein
Sequence:
MSLKGTIVLLGLLWSFQATLGIRFVIDREECFSHKAEYEGDTLHVSFVVIKSDSQWHFNEDGVDLVIHGPTGEQIHDFREQISAKHDFVVQKKGVYRFCFTNKSPYHETIDFDVQLGHFAYYDQHAKDEHFTPLMEQISKLEEALYNIQFEQHWLEAQTDRQAIVNENMSKRAVHKALFESFALIGASFLQVYLLRRLFERKLGMSRV
Protein: Protein CONTINUOUS VASCULAR RING 1 (F4IUE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of vascular patterning in the stem, probably by negatively regulating the differentiation of vascular tissue.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Berberine bridge enzyme-like 16
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
Sequence:
MGDEKPVIVMANRERDRELLIPVADSGDKDDGSSSKPSSSSSASSSSHQSSHETLSLFIRGWASKKFMTGCVILLPIAITFYITWWFIHFVDGFFSPIYAQLGINVFGFGFLTSIAFIFLVGVFMSSWLGASVLNLGEWFIKRMPFVRHIYNASKQISTAISPDQNTQAFKEVAIIRHPRVGEYAFGFITSTVVLQNYPTEEELCCVYVPTNHLYIGDILLVNSNDVIRPNLSVREGIEIVVSGGMSMPQILSTVDKPLASIDRATSL
Protein: Multisubstrate pseudouridine synthase 7 (EC 5.4.99.-) (EC 5.4.99.27) (RNA pseudouridylate synthase 7) (RNA-uridine isomerase 7) (tRNA pseudouridine(13) synthase) (Q08647)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing. Also catalyzes pseudouridylation at position 56 in U2 snRNA. Catalyzes also pseudouridylation at position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr). Pseudouridine residues in tRNAs may stabilize the local RNA conformation, favor interactions with protein partners and play an important role in the stabilization of the codon-anticodon interaction with mRNA. Also catalyzes pseudouridylation of mRNAs in response to heat shock: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25219674}. Cytoplasm {ECO:0000269|PubMed:25219674}. Note=Predominantly nuclear in 30 degrees Celsius and primarily cytoplasmic in heat shock. {ECO:0000269|PubMed:25219674}.
Interaction partners:
- tRNA pseudouridine synthase 1
- tRNA pseudouridine
- tRNA pseudouridine
- 21S rRNA pseudouridine
- tRNA pseudouridine
- Bifunctional protein RIB2
- tRNA pseudouridine synthase 4
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
Sequence:
MSDSSEATVKRPLDAHVGPSENAAKKLKIEQRTQADGIHEADVGITLFLSPELPGFRGQIKQRYTDFLVNEIDQEGKVIHLTDKGFKMPKKPQRSKEEVNAEKESEAARRQEFNVDPELRNQLVEIFGEEDVLKIESVYRTANKMETAKNFEDKSVRTKIHQLLREAFKNELESVTTDTNTFKIARSNRNSRTNKQEKINQTRDANGVENWGYGPSKDFIHFTLHKENKDTMEAVNVITKLLRVPSRVIRYAGTKDRRAVTCQRVSISKIGLDRLNALNRTLKGMIIGNYNFSDASLNLGDLKGNEFVVVIRDVTTGNSEVSLEEIVSNGCKSLSENGFINYFGMQRFGTFSISTHTIGRELLLSNWKKAAELILSDQDNVLPKSKEARKIWAETKDAALALKQMPRQCLAENALLYSLSNQRKEEDGTYSENAYYTAIMKIPRNLRTMYVHAYQSYVWNSIASKRIELHGLKLVVGDLVIDTSEKSPLISGIDDEDFDEDVREAQFIRAKAVTQEDIDSVKYTMEDVVLPSPGFDVLYPSNEELKQLYVDILKADNMDPFNMRRKVRDFSLAGSYRTVIQKPKSLEYRIIHYDDPSQQLVNTDLDILNNTRAKESGQKYMKAKLDRYMPDKGGEKTAVVLKFQLGTSAYATMALRELMKLETSRRGDMCDVKENI
Protein: Transcription factor MYB76 (Myb-related protein 76) (AtMYB76) (Protein HIGH ALIPHATIC GLUCOSINOLATE 2) (Q9SPG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in determining the spatial distribution of aliphatic glucosinolates (AGLSs) within the leaf, mostly short chained. Together with MYB28/HAG1 and MYB29/HAG3, promotes aliphatic glucosinolate biosynthesis and represses indolic glucosinolate biosynthesis, but could not activate AGSL biosynthesis on its own.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Dihomomethionine N-hydroxylase
- Cytochrome P450 83A1
- Hexahomomethionine N-hydroxylase
- Methylthioalkylmalate synthase 3, chloroplastic
- Transcription factor MYC4
- Transcription factor MYC3
- Methylthioalkylmalate synthase 1, chloroplastic
- Methionine aminotransferase BCAT4
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Transcription factor MYC2
Sequence:
MSKRPYCIGEGLKKGAWTTEEDKKLISYIHDHGEGGWRDIPEKAGLKRCGKSCRLRWTNYLKPDIKRGEFSYEEEQIIIMLHASRGNKWSVIARHLPKRTDNEVKNYWNTHLKKRLIDDGIDPVTHKPLASSNPNPVEPMKFDFQKKSNQDEHSSQSSSTTPASLPLSSNLNSVKSKISSGETQIESGHVSCKKRFGRSSSTSRLLNKVAARASSIGNILSTSIEGTLRSPASSSGLPDSFSQSYEYMIDNKEDLGTSIDLNIPEYDFPQFLEQLINDDDENENIVGPEQDLLMSDFPSTFVDEDDILGDITSWSTYLLDHPNFMYESDQDSDEKNFL
Protein: Helt bHLH transcription factor (A0A087WSW0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDKLKERKVSRLSPNGTCALVVEASDSPTRHLGGPMAGKCPHGTLSVEESRVRTPVSHKVIEKRRRDRINRCLNELGKTVPMALAKQGEPQEALAQIRSRVRSLVLSSATVPDQQALGRCEGPFLLLQSSGKLEKAEILEMTVQYLRALHSADFPRGREKAELLAEFANYFHYGYHECMKNLVHYLTTVERMETKDTKYARILAFLQSKARLGAEPAFPPLGSLPEPDFSYQLHPAGPEFAGHSPGEAAVFPQGSGAGPFPWPPGAARSPALPYLPSAPVPLASPAQQHSPFLTPVQGLDRHYLNLIGHAHPNALNLHTPQHPPVL
Protein: LD33732p (Q95TP3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRSRSRERKDTRSSRPLEASIDSRQRKPRERSAATPPRKEPERHRERSKDRQRSKEKHRSRDRLRSRERQRSRERQRSRERQRSKERQRSKERQRSIERQRSKERQRSKERQRSRSKDALRCKEKPQCNEKERSRERRRSKSKDRQRSKEKHRPKDEQQSVDKRRDRSTDRSKENQRSNERQRSKERQRSKERERSKDRQRSRERRRSKEGQLSKDRQGLKERQRSNERKRSKERQPSKEKQRSRERQRSREPLQSKDRQRSKERQRSRERPAKEARPTRSPRERSSKSRDDRRHRSPTNASRKQKDDTKLSRNARFKSPAHSPEAPPKKSVPTPAFNPFKAAEDTVNDILGTKSVMVALEQTKRQRAASSSSSDSDSSGSSSTSSRTPSPKPTPRKQKKRSKTPELKEVKKEISPRKESRVSVKREQSNSPQKSKSKSKVDESSPKRTSRRSRSISSELRYSPAERHPERYHDIVQDKKRPSKLTQELLII
Protein: FI18025p1 (Sox102F, isoform B) (Q59DN5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Forkhead domain 102C
- Sox100B
- FI06413p
Sequence:
MKPPGEDQTNEKEHSDLGMIKQLQLIRNRILSQAHYDSMTDIDASAQQQQQLQNVQRLQHESCLQELHNHLSSQYGAVRFTAANPQHQNQQAVSVSSGNLMPFLPAFLQPPMPNAQQLLQLIPGHENAQSVPTHHHSHPQSEAFSTHKMALAPMWSTAAVAAAHIQAALAAAAVAAANNNKNSSHFSNNTNIVGLATRGNELLNTDSDPQMEIGETRRGGNGGSCRSRPESPTYENPPYEILSYSHNTPPESPHGRTADCSKNFSPSPTDNLSIASVSEAQDSEMDAPLNLSKPKGSPSSSPNSSSQRDHCENLTPVVSSPPLSWHQGQPHYAEIELPLLKSHGRVWNSAVACSGGSRATRVSRDSVNSCGTNSERSAALDPESLNSGQLGPVPASPSSQPLRQGNGHGHGGNHGHVHSKPHIKRPMNAFMVWAKDERRKILKACPDMHNSNISKILGARWKAMSNADKQPYYEEQSRLSKLHMEQHPDYRYRPRPKRTCIVDGKKMRISEYKVLMRNRRAEMRQLWCRTGGVSGGSGSLCADACPKGSGGSNSQVAVAAAAAVYHLQDMASSAASTAHGHDCGHTPPQQFFYPPESLSPSGFSSDEVELASQRELDD
Protein: Replication protein A subunit (A0A8I5ZL77)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MVGHLSEGAIAAIMQQGDTSIKPVLQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNALVEGGQLASNCVCQVHRFIVNTLKDGRRVVILMDLEVVKSAGEVGVKIGNPVPYNEGHAQQQAVSAPASAATPPASKPQPQNGSLGVGSTVAKAYGASKPFGKPAGTGLLQPTSGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSIELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFSAVKNDYEMTFNNETSVLPCEDGHHLPTVQFDFTGIGDLESKSKDSLVDIIGICKSYEDATKITVKSNNREVAKRNICLMDMSGKVVTATLWGEDADKFDGSRQPVMAIKGARVSDFGGRSLSVLSSSTVLVNPDIPEAYKLRGWFDSEGQALDGVSISDLRSGGTGGSNTNWKTLYEAKSENLGQGDKADYFSTVATVVFLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDREFPNFKYRMILSNEQAFEEVFQNANFRSFTFRIRVKLETYNDESRIKATVIDVKPVDYRDYSKRLIMNIRKNI
Protein: Spa40 (Q6XVW1)
Organism: Shigella flexneri
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MANKTEKPTPKKLKDAAKKGQSFKFKDLTTVVIILVGTFTIISFFSLSDVMLLYRYVIINDFEINEGKYFFAVVIVFFKIIGFPLFFCVLSAVLPTLVQTKFVLATKAIKIDFSVLNPVKGLKKIFSIKTIKEFFKSILLLIILALTTYFFWINDRKIIFSQVFSSVDGLYLIWGGLFKDIILFFLAFSIFVIILDFVIEFILYMKDMMMDKQEIKREYIEQEGHFETKSRRRELHIEILSEQTKSDIRNSKLVVMNPTHIAIGIYFNPEIAPAPFISLIETNQCALAVRKYANEVGIPTVRDVKLARKLYKTHTKYSFVDFEHLDEVLRLIVWLEQVENTH
Protein: Nuclear receptor subfamily 1 group D member 1 (Rev-erbA-alpha) (V-erbA-related protein 1) (F1RAU6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Period circadian protein homolog 2
- Aryl hydrocarbon receptor nuclear translocator-like 1a
- Cryptochrome 3
- Period circadian clock 3.
- Nuclear receptor corepressor 2
- Period circadian clock 1a.
- Nuclear receptor corepressor 1.
- BHLH-PAS transcription factor
- Period homolog 1b
- Cryptochrome-1
Sequence:
MTLLGLNMTTAVDTNNTGGVISYIGSCGGSPNRTSPVSMYSENSNSSMQSLTQPCFGSSFPPSPNGSHDSSRMYTSSSSSSSSGSGEDGNSSCSGGSPRGRDDGGSARNSPNKSVATLTKLNGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKKCLKNETCTIMRINRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLAEMQNAMNNMVNNQLQNEFQLASITSNTPCPSSSSPSNTSSSSSSPCPGLTVGPQPQPPAVPVAQSPSSPAPTSPTVQLAQSPPPLTSTPPPCTSPGVDKTIAAITRAHRETFIYAHDKLGSPLLPHNSELDNRSNNRCMAGYHLNGHNTIYHHDNNVAHHCNNFEVQQDNSLHFQASQTPEKHQQHNNNSQRPPNSNFYSIHHGQEMNSASQGQNCPWKKHKEILLACPMNMHPYSDPNKTPQEIWEDFSLSFTPAVREVVEFAKHIPGFSTLSQNDQVTLLKAGTFEVLMVRFSSLFNVKEKTVTFISGATYSLEALKSMGMGDLLGTMFDFSEKLNSLELSAEELGLFTAVVLVSADRSGIENVNSVEMLQESLIRALRTLVSKSAPTDASRFTKLLLKLPDLRTLNNMHSEKLLSFRIDA
Protein: rRNA-processing protein utp23 (U three protein 23) (O74862)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in rRNA-processing and ribosome biogenesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- KRR1 small subunit processome component homolog
- U3 small nucleolar RNA-associated protein 5
- Probable U3 small nucleolar RNA-associated protein 7
- Uncharacterized protein C57A7.06
- U3 small nucleolar RNA-associated protein 15
- Probable U3 small nucleolar RNA-associated protein 11
- Uncharacterized protein C3B8.09
- Uncharacterized protein C18B11.06
- U3 small nucleolar ribonucleoprotein protein imp4
- U3 small nucleolar ribonucleoprotein protein imp3
Sequence:
MRQKRAKNYRKLMHTYQLLFGFREPYQVLVDADFLKDLSQQKIDIQAALARTVQGAIKPMITQCCIRQLYSKSDELKQEIRIAKSFERRRCGHIDEALSPSECIQSVVNINGRNKHRYVVATQDPELRQALRSVPGVPLIYMKRSVVILEPASRATLLEKHNKESVQMGMSKEEKLLLSGKKRSANELAIDDQDTKESTDLAGTEDSAPKANKKRKGPKGPNPLSIKKRSSKNHTTDEPTLPVNIIGDVGERKKHRRKRK
Protein: Adenylate kinase 8 (AK 8) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 8) (A0A4X1T4U3)
Organism: Sus scrofa (Pig)
Function: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96MA6}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96MA6}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q96MA6}.
Interaction partners:
Sequence:
MDATTAPHRIPPEMPQYGEANHIFEMMQNMLEQLLIHQPTDPIPFMIDHLQLDNDYVPKILVLGPPASGKTTVAMWLCKHLRSNLLSVENLIARQFSSLAAGARQHYQKFKTLPSGLLVRLVQARLREEDCVTRGWILDGIPETREQALLLQTLGIAPRHVIVLSAPDTVLIERNLGKRVDPLTGEVYHTTFDWPPQPEIQNRLLVPAGISEGETARKLLEFHRNIVRIAPSYPKILRVIPADQPCVDVFCQALTYVQTIHRSNAPFTPRVLLLGPMGSGKSLQAALLAQKYGLVNVCCGQLLKEAVADKSKYGKVILSFFEKEIAVPDSIIMKVLGRRLDQQDCVERGWVLHGFPRDLDQAHMLNSLGYKPNRVFFLNVPFDSILERLTLRRTDPVTGERYHLMYKPPPTVEIQARLLQNPKDTEEQVKLKMDLFCRTSAELEQFYQPVLPLNGDQDPYTVFEHLESGIINPLPNKVP