wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (Q580G3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tyrosyl/methionyl-tRNA synthetase, putative
- Lysine--tRNA ligase
- GST N-terminal domain-containing protein
- glutamine--tRNA ligase
- glutamate--tRNA ligase
- isoleucine--tRNA ligase
- arginine--tRNA ligase
- proline--tRNA ligase
- leucine--tRNA ligase
- Prokaryotic-type class I peptide chain release factors domain-containing protein
Sequence:
MSAVEELRAQIDALASQISAVKKEQGASSEACKSLVAKMTELRKQLPQEKKEKKAEKAPEISYYDTRLAMVKEMGPLGAAYPHKFHRDYTLPAFRECFKPMLQEKGQRLDKVVTIAGRIVVKRSSSSKLHFLALQGDGEVLQVISMASDYVNDGFADIHSKIKRGDIIGVRGVPSFSNTGEFSMSAYEITLLSTCFHMLPDEHYGLSSVEQRFRQRYLDLIVNRENAKTFILRSKIISYIRSFFDQKDFLEVETPMLNQIAGGAAARPFITHHNELNQTMYLRIAPELYLKKLVVGGLDRVYEIGKQFRNEGIDLTHNPEFTSVESYWAYADYNDWMETTEELLYGMVMHLYGSPIVKYSPRDSEGRQLPEVTFNFNRPFKRLHIVPKLEEILGLKFPADFYSSEANSFFLDICKKNQVECNPPFTTTRLLDALVSHYLEPQCHDPTFLCDHPRIMSPLAKWHRKDLRLSERFELFINKKEICNSYTELNSPLVQREEFERQLRDREKGDDEAMDIDEGYVQALEYALPPTGGWGLGIDRLVMYLTSQNNIKEVLLFPAMKPEGTSSATFPPGTMLNGQGVPLL
Protein: Hepatocyte nuclear factor 1-alpha (HNF-1-alpha) (HNF-1A) (Liver-specific transcription factor LF-B1) (LFB1) (Transcription factor 1) (TCF-1) (P20823)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver (By similarity). Binds to the inverted palindrome 5'-GTTAATNATTAAC-3'. Activates the transcription of CYP1A2, CYP2E1 and CYP3A11 (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:10966642, ECO:0000269|PubMed:38018242}.
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Hepatocyte nuclear factor 4-alpha
- Hepatocyte nuclear factor 1-beta
- Solute carrier family 2, facilitated glucose transporter member 2
- Pterin-4-alpha-carbinolamine dehydratase 2
- Hepatocyte nuclear factor 4-gamma
- Hepatocyte nuclear factor 3-gamma
- Hepatocyte nuclear factor 6
- Hexokinase-4
- Hepatocyte nuclear factor 3-beta
Sequence:
MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLLAGEGPLDKGESCGGGRGELAELPNGLGETRGSEDETDDDGEDFTPPILKELENLSPEEAAHQKAVVETLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYSGPPPGPGPGPALPAHSSPGLPPPALSPSKVHGVRYGQPATSETAEVPSSSGGPLVTVSTPLHQVSPTGLEPSHSLLSTEAKLVSAAGGPLPPVSTLTALHSLEQTSPGLNQQPQNLIMASLPGVMTIGPGEPASLGPTFTNTGASTLVIGLASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMPPVQSHVTQSPFMATMAQLQSPHALYSHKPEVAQYTHTGLLPQTMLITDTTNLSALASLTPTKQVFTSDTEASSESGLHTPASQATTLHVPSQDPASIQHLQPAHRLSASPTVSSSSLVLYQSSDSSNGQSHLLPSNHSVIETFISTQMASSSQ
Protein: Cysteine-rich repeat secretory protein 55 (Q9LV60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Receptor Serine/Threonine kinase-like protein
- Inactive serine/threonine-protein kinase BKN2
- non-specific serine/threonine protein kinase
- Transmembrane protein
- Protein MODIFYING WALL LIGNIN-2
- non-specific serine/threonine protein kinase
- Probable LRR receptor-like serine/threonine-protein kinase At1g07560
- ACD11 homolog protein
- Probable carboxylesterase 6
Sequence:
MKTLVVKCFLLLALVCSCRAADSIWQLCNTNSNISASSQVSKNIDSLLATLVSKTPSKGFKTTTSSSYNNKEKVYGLAQCRGDISNTDCSTCIQDAAKKIREVCQNQSDSRILYDFCFLRYSQENFIGKLDTGAGLIYFNVANVTEIDPKKFDNELGALFDKIRSEAVLPKNKGLGKGKTKLTPFVTLNGLVQCTRDLSELDCAQCFATAVGSFMTTCHNKKGCRVLYSSCYVRYEFYPFYFPLDPAKTGPSVGRISSVHLSP
Protein: Lethal giant larvae homologue 2 domain-containing protein (A0A0K3AR90)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDRAKKKFASAIDGLRSLHNRTEINVDEKIQSEHCRFTRVVRHGLPEDPRCFAYDPVQRLIAIGTGRGHIRIIGDAGVDYLLKHESGEPVLHMQFLVNEGGLITSCGTDSIHLWNYRQKTAEIVHTVQLSKESVSCIHLPVAGKWLFIGTDKGNVYFLCLNSFLLSPYVINWNKAIDLSCRVHPGPVRQLAVSPAENTKLLIVYDKGIVVQWNLGTREVDRYPLDPPIKSVNWHFDGRQILTGNVDGSISLYNHKKSTEAIQRTTPHGSGPCRPIQQVEWKHMSETESIIMFSGGMPTDDGLPMPALTILKGGKSATVLEMDWPIIQFIPLNQNIWNSIPQCPHSVAVLLKHDFMVLDLNQNGHPVIESPHAMNIHESPVTCMAYYSDCPLDLIGALTLVGTKQRNKEFSARSWPVTGGLGRECATGHQELVVTGHKDGSLKFWQETGEHLQILYKLKSSSHFERLEEMETSDKVSHAVKYIELCLESRQLLVAGISGQVTLFRFTKQEICGTIAVVNIPLLGNLSSNLPNNDFDKSPVPNGPGKEIRRQRKIVSRESTNSLDTSDSGDERIVPFKVRGAPVKRPPGFVPELACFVPWHSHAKVDQITTICLNSSYGIIAIGTSSGLALVDTTQCALIYSWTTNELYGSDPTPAIQLSMQLSDAASPLEIDEFENDDTLIYNTDTGNYTLRSTRNSLTPSSNGFLHPGEMPTRPKSAANSSNKSGGMMGLFRRNTAELAATIRERYQGNRSESATTDRPDVEHRGETPPPTPNEGNKVQKAGRSHSVKGSFIRRFAKSSSSKEKKEVKIEVDNQSNSGIERSRSFHSHISEEGDSQRESPSSGRQLNTSSPSTSSQSLERSMSTQPQESITSLSFIHSYSKKNDSKMSPCLWVGTSAGASLALNLILPEDRFTSTIVVAPSGTVVRLKGQVISQSFMDNTFCIISPASESYKEAAKEQSATSPDRSLLNRVNTKASLAPQYSSSIDSNDEISQILIVAAENEVKVVALPTFSQLYVQKFDEIPLVKATPTHIRGYPCLMCLSAAGQIIMLSLPSLRILQTSTIFPHSVEIDDPLCQKTAFSDHGLGVYMASQTEMEKYTMCSEIAEQTGESLGELFVPCEMPEQPKNNSFLKGVSSIFGGTPRNDPNDIDAILSENMGVKNSSGVNPMRSVARTIPGPSVQMDRAQAGGVSAGQAAAMALQNLNERTEKLNATVDATENLKNNAMSLSSRTGKLVEKYEKKKWYNF
Protein: Pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (P38075)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Putative pyridoxal kinase BUD17
- Putative pyridoxal kinase BUD16
- Probable pyridoxal 5'-phosphate synthase subunit SNZ2
- Probable pyridoxal 5'-phosphate synthase subunit SNZ3
- Pyridoxal 5'-phosphate synthase subunit SNO1
- Pyridoxal 5'-phosphate synthase subunit SNZ1
- Uncharacterized protein YGR017W
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
- Putative pyridoxal reductase
Sequence:
MTKQAEETQKPIIFAPETYQYDKFTLNEKQLTDDPIDLFTKWFNEAKEDPRETLPEAITFSSAELPSGRVSSRILLFKELDHRGFTIYSNWGTSRKAHDIATNPNAAIVFFWKDLQRQVRVEGITEHVNRETSERYFKTRPRGSKIGAWASRQSDVIKNREELDELTQKNTERFKDAEDIPCPDYWGGLRIVPLEIEFWQGRPSRLHDRFVYRRKTENDPWKVVRLAP
Protein: Zinc finger, MYND-type containing 8 (A0A8I6A294)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDISTRSKDPKEDPGSTERTAQKRKVPSPPHSSNGHSPQDSSTSPIKKKKKPGLLNSSSKDQSELRHGPFYYMKQPLTTDPVDVVPQDGRNDFYCWVCHREGQVLCCELCPRVYHAKCLRLTSEPEGDWFCPECEKITVAECIETQSKAMTMLTIEQLSYLLKFAIQKMKQPGTDAFQKPVPLEQHPDYAEYIFHPMDLCTLEKNAKKKMYGCTEAFLADAKWILHNCIIYNGGNHKLTQIAKVVIKICEHEMNEIEVCPECYLAACQKRDNWFCEPCSNPHPLVWAKLKGFPFWPAKALRDKDGQVDARFFGQHDRAWVPVNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRKKFGVFNYSPFRTPYTPNSQYQMLLDPSNPSAGTAKTDKQEKVKLNFDMTASPKIILSKPLLSGGAGRRISLSDMPRSPTSTNSSVHTGSDVEQDPEKKAPSSHFSASEESMDFLDKSTASPASTKTGQAGSLSGSPKPFSPQAPTPIMTKPDKTSTATTGSILNLNLDRSKAEMDLKELSESVQQQSAPVPLISPKRQIRSRFQLNLDKTIESCKAQLGINEISEDVYTAVEHSDSEDSEKSESSDSEYVSDEEQKPKNEPEDPEDKEGSRVDKEAPAIKRKPKPSNQVEVKEEVKSNSPVGEKVDPAPAKDKASPEPEKDFAEKAKPSPHPTKDKLKGKDETDSPTVHLGLDSDSESELVIDLGEDPSGREGRKNKKEPKVPSPKQDAIGKPPPPTPAGNQSPPETPVLTRSATQAPAAGVTVAATTSTMSTVTVTAPATAAVTGSPVKKQRPLLPKETVPAVQRVVWNASSKFQTSSQKWHMQKIQRQQQQQQQQQQQQQSQQQQPQSSQGTRYQTRQAVKAVQQKEVTQSPSTSTITLVTSTQPAALVSSSGSASTLASVINADLPIATASADVAADIAKYTSKMMDAIKGTMTEIYNDLSKNTTGSTIAEIRRLRIEIEKLQWLHQQELAEMKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKKKQWCANCKKEAIFYCCWNTSYCDYPCQQAHWPEHMKSCTQSATAPQQEADAEANQETGNKTSQGSSSNTQSAPSEPASTPKEKETSTEKSKDSNSTLDLSGSRETPSSILLGSNQGSVSKRYDKQPAYTPTTTDHQPHPNYPAQKYHSRSSKAGLWSSSEEKRGSSRSEHSAGTSTKNLMPKESRESRLDTFWD
Protein: Sec-independent protein translocase protein TatE (P0A843)
Organism: Escherichia coli (strain K12)
Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatE shares overlapping functions with TatA.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00903}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00903}.
Interaction partners:
- Sec-independent protein translocase protein TatB
- Sec-independent protein translocase protein TatC
- 3'-5' ssDNA/RNA exonuclease TatD
- GMP synthase
- Sec-independent protein translocase protein TatA
- Trimethylamine-N-oxide reductase 1
- Flagellar regulator flk
Sequence:
MGEISITKLLVVAALVVLLFGTKKLRTLGGDLGAAIKGFKKAMNDDDAAAKKGADVDLQAEKLSHKE
Protein: Grainyhead-like protein 2 homolog (Brother of mammalian grainyhead) (Transcription factor CP2-like 3) (Q6ISB3)
Organism: Homo sapiens (Human)
Function: Transcription factor playing an important role in primary neurulation and in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes (By similarity). During embryogenesis, plays unique and cooperative roles with GRHL3 in establishing distinct zones of primary neurulation. Essential for closure 3 (rostral end of the forebrain), functions cooperatively with GRHL3 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (By similarity). Regulates epithelial morphogenesis acting as a target gene-associated transcriptional activator of apical junctional complex components. Up-regulates of CLDN3 and CLDN4, as well as of RAB25, which increases the CLDN4 protein and its localization at tight junctions (By similarity). Comprises an essential component of the transcriptional machinery that establishes appropriate expression levels of CLDN4 and CDH1 in different types of epithelia. Exhibits functional redundancy with GRHL3 in epidermal morphogenetic events and epidermal wound repair (By similarity). In lung, forms a regulatory loop with NKX2-1 that coordinates lung epithelial cell morphogenesis and differentiation (By similarity). In keratinocytes, plays a role in telomerase activation during cellular proliferation, regulates TERT expression by binding to TERT promoter region and inhibiting DNA methylation at the 5'-CpG island, possibly by interfering with DNMT1 enzyme activity. In addition, impairs keratinocyte differentiation and epidermal function by inhibiting the expression of genes clustered at the epidermal differentiation complex (EDC) as well as GRHL1 and GRHL3 through epigenetic mechanisms.
Subcellular location: Nucleus {ECO:0000269|PubMed:20938050, ECO:0000269|PubMed:25152456, ECO:0000269|PubMed:29499165}. Membrane {ECO:0000269|PubMed:25152456}. Note=detected at cell-cell contact areas. {ECO:0000269|PubMed:25152456}.
Interaction partners:
- Epithelial splicing regulatory protein 1
- Transcription factor Ovo-like 2
Sequence:
MSQESDNNKRLVALVPMPSDPPFNTRRAYTSEDEAWKSYLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRDKRLLSVSKASDSQEDQEKRNCLGTSEAQSNLSGGENRVQVLKTVPVNLSLNQDHLENSKREQYSISFPESSAIIPVSGITVVKAEDFTPVFMAPPVHYPRGDGEEQRVVIFEQTQYDVPSLATHSAYLKDDQRSTPDSTYSESFKDAATEKFRSASVGAEEYMYDQTSSGTFQYTLEATKSLRQKQGEGPMTYLNKGQFYAITLSETGDNKCFRHPISKVRSVVMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDVNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQNRKKGKGQASQTQCNSSSDGKLAAIPLQKKSDITYFKTMPDLHSQPVLFIPDVHFANLQRTGQVYYNTDDEREGGSVLVKRMFRPMEEEFGPVPSKQMKEEGTKRVLLYVRKETDDVFDALMLKSPTVKGLMEAISEKYGLPVEKIAKLYKKSKKGILVNMDDNIIEHYSNEDTFILNMESMVEGFKVTLMEI
Protein: Serine/threonine-protein kinase 4 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 1) (MST-1) (STE20-like kinase MST1) [Cleaved into: Serine/threonine-protein kinase 4 37kDa subunit (MST1/N); Serine/threonine-protein kinase 4 18kDa subunit (MST1/C)] (Q9JI11)
Organism: Mus musculus (Mouse)
Function: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between nucleus and cytoplasm. {ECO:0000250}.
Interaction partners:
- Protein salvador homolog 1
- Ras association domain-containing protein 5
- Ras association domain-containing protein 1
- MOB kinase activator 1A
- Serine/threonine-protein kinase 3
- Forkhead box protein O1
- Forkhead box protein O3
- Forkhead box protein O6
- Forkhead box protein O4
- Caspase-3
Sequence:
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFMDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENSEEDEMDSGTMVRAAGDEMGTVRVASTMSGGANTMIEHGDTLPSQLGTMVINTEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKNVSGSLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEMEEIRQKYRSKRQPILDAIEAKKRRQQNF
Protein: Calpastatin (Calpain inhibitor) (E7EVY3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Protein: Protein kinase (Pto disease resistance protein) (Pto kinase) (Q40234)
Organism: Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium)
Interaction partners:
Sequence:
MGSKYSKATNSINDALSSSYLVPFESYRVPLVDLEEATNNFDHKFLIGHGVFGKVYKGVLRDGAKVALKRRTPESSQGIEEFETEIETLSFCRHPHLVSLIGFCDERNEMILIYKYMENGNLKRHLYGSDLPTMSMSWEQRLEICIGAARGLHYLHTRAIIHRDVKSINILLDENFVPKITDFGISKKGTELDQTHLSTVVKGTLGYIDPEYFIKGRLTEKSDVYSFGVVLFEVLCARSAIVQSLPREMVNLAEWAVESHNNGQLEQIVDPNLADKIRPESLRKFGDTAVKCLALSSEDRPSMGDVLWKLEYALRLQESVI
Protein: Protein IQ-DOMAIN 7 (AtIQD7) (Q2NND9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
Interaction partners:
- Protein IQ-DOMAIN 33
- At1g23060/T26J12_16
Sequence:
MGGSGNWIRSLISNRKPVNDQQEKLSDKSSKKKWKLWRISSESLASSSFKSRGSYAASSLGSELPSFSADEAFTTAMAALIRAPPRDFLMVKREWASTRIQAAFRAFLARQAFRALKAVVRIQAIFRGRQVRKQAAVTLRCMQALVRVQSRVRAHRRAPSDSLELKDPVKQTEKGWCGSPRSIKEVKTKLQMKQEGAIKRERAMVYALTHQSRTCPSPSGRAITHHGLRKSSPGWNWYDDVGTFSRKSSESSVLSEYETVTVRKNNLSSTRVLARPPLLLPPVSSGMSYDSLHDETSTSSTSQSPVAFSSSVLDGGGYYRKPSYMSLTQSTQAKQRQSGLSCNGDARRSAGSDQCTDLYPPGNVWAKSQRS
Protein: Probable WRKY transcription factor 15 (WRKY DNA-binding protein 15) (O22176)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAVELMTRNYISGVGADSFAVQEAAASGLKSIENFIGLMSRDSFNSDQPSSSSASASASAAADLESARNTTADAAVSKFKRVISLLDRTRTGHARFRRAPVHVISPVLLQEEPKTTPFQSPLPPPPQMIRKGSFSSSMKTIDFSSLSSVTTESDNQKKIHHHQRPSETAPFASQTQSLSTTVSSFSKSTKRKCNSENLLTGKCASASSSGRCHCSKKRKIKQRRIIRVPAISAKMSDVPPDDYSWRKYGQKPIKGSPHPRGYYKCSSVRGCPARKHVERAADDSSMLIVTYEGDHNHSLSAADLAGAAVADLILESS
Protein: Complement C3a.2 precursor (Complement component C3-1) (Q3MU74)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEVKLLFLSAVLLSSALLTLCDPLYVLMAPNLLRVGSSENVFVEAQDYSGEPLRVKISVKNFPAKNVEMMQKTVTLTGEKYQILTDIEIPDDKNFFSDDEKKQYVYLQAHFPSVTLEKVVMVSFQSGYLFVQTDKPIYTPGSNVQYRIFSMTPNLKPLSQPGITVDIMNPQGITVASDAIKAEKGVKSSIYNIPDVTSLGMWKVVTRYTNTPLKTFTAEFEVKEYVLPTFEVKLTPSSFFYYVGDNKQENDEEDSLTVDIEAKYLFGKKMDGNAFVVFGVMDGAAKTSIVNSLQKVPVVNGVGTAELTREMITKTFKNIKDLVGKSIYVSVNLLTESGSEMVEAEKRGIQIVTSPYTIHYKRTSQFFKPGMPLGVSVYVTNPDETPAKDVEVEVLVDGKGGVSGKTRDNGIAKVKVNTPGGASTLKITAKTKNTEYTSEQQAVKTMTAQAYKTKHDSKNYLHINIESAEFEIGDQMTVNLITGQSSGDRDQDYTYMILSKGQIVLAERFKRQGQTLVTLSLTITKEMVPSFRFVAYYHVGKDEVVSDSVWVDVKDTCMGKLNVEVKEKKNTYETGNDVNLHITGDPGARVGLVVVDKAVQVLNKNRLTQSKVWDVIEKHDTGCTGGGGKDSMGVFSDAGLIFESNTAGGTDTRTVPECPAPLKRKRRSESLQTITTTLAGQYTEKIRPCCYDGMRNNRIGYTCERRASYVIDGEECVKAFLHCCKEVKNHKEKETEEEELILARSDEDEEGDYKDYDDITSRTQFPESWLWEEFDLCDKCSKPSKDKVIYLKDSITTWQILAISLSPTHGICVAEPEEIVVFKSFFIDLKVPYSAVRGEQVEIKAIIHNYTPKHLKKVRVEFLETAGVCSAASKKGKYRTTVNVDKDSSVAVSFVIVPMTLESQHIEVKASISDYEDGVRKTLKVVSEGVLTKFRTEKLELNPGKKGEKPLVLRSGIPADQVPGTPVNSYITVTGEEISQSIEQAINGSFMGELIIQPHGCGEQNMVTMTLPFIATHYLDNTNQWEYVGIDRRKVAINHIKTGYEGQLKFRKQDGSYALWIETDSSTWLTAYVAKVFAMASKLIAIEENVICSALKWLVMHKQLPDGSFKEDKPVYHREIMGGIEGQNTDVSLTAFVLIAMQEGKEICGGAVGSLHESIRKSVAFLKNQLTKLTNPYAAALTSYALANADSLDKEILMKHSTKGNDGRFWNVPGWHYHSIEATAYAVLALVKAKDYDTAGEAVHWLAKQKSSHGGYDTTQVTIMVFQAVAEYRAQVQDLKNFDLNVELVVPGRRKTDRWTIQRSNVHLTRSGSVDMNKDFTVIAKGTGSAILSVLTLYYARPFEKKTDCTFFDLSVKLDKIPETKPGTNGTYNFILDFFYKNKTNDATMTILDIGLPTGFDIDEADLKQLSTGKERYIQKYEKNKVLSERGSLIIYLNKVSHKESETLVFRMHKTFNVGLLQPASVTIYEYYSPDARCKKYYHPEREDSALYRLCKGDLCVCAEENCSYQKKNQVNESDRLIKACEPHLDYIYKAKLVKMDLKQDSDIYHMKVEKTVKEGTDMDVGGKVKPFLARPSCRVSLGLVEGKSYLIMGNSVDLPTLGGSLQYIIGEQTWIEYWPTSDESKSAEHRDRYIGMTAVENMFTTGGCLT
Protein: Prion protein (Prion protein a (Kanno blood group) precursor) (Prion protein-related 2) (Prion-like protein 1) (Q7T2P9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MHSKFKLFSFLNCLLLLAVLLPVAQSRRGGGFGRGGGRGGGWGGSSSGRAGWGAAGGHHRAPPVHTGHMGHIGHTGHTGHTGSSGHGVGKVAGAAAAGALGGMLVGHGLSSMGRPGYGYGYGGYGGHGYGYGHGYGHGHGHGGHGGHSGDHNETDADYYLDGAASGHAYSCVTVFGLMMSFLIGHFLS
Protein: Alpha 4 type V collagen (Procollagen, type V, alpha 3, isoform CRA_b) (Q9JI04)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Collagen type V alpha 2 chain
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Lumican
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
Sequence:
MRSCRRLDQLQAGLCLLLASLQLVSWTLAAEPVDVLETLGVHRDKAGVTKGPGFCPQRIPQGDRAFRVGKSSLLSVPTWQLFPDGHFPENFSVLLTLRAQPANQSVLLSIYDENGVRQMGLALGPALGLLGDSFRSLPKQINLMDGRWHRVAVSISGDKVTLVVDCEPQPPMFGQGPRVISTAGLTVMGTQELGEESFEGDIQELLLIPDPQAALQACELYLPDCETPDSTTTGVTKEEPETPAPRRRKGKGKKKDRGRKGKGRKKNKTSRLSPTPGAPENQTSLHTPETEKPSPHLPPTPTPLAITTTVTMGGNATVLQGLDSSTETEQMTPEMDATEESEGGGPTMGPEFRAAEQSLQTEFQIFPGAGEKGAKGEPATIEQGQQFEGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGVRGLPGTVIMMPFHFASGSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQGPRGLQGPPGPPGREGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGPVGQPGPPGEDGIKGLQGPPGPTGQAGEPGPRGLIGPRGPPGPLGRPGVTGSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKGLPGLQGPPGFPGPKGPPGPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELGPLGSLGKEGPPGPMGFPGPQGAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTGKDGIPGPPGLQGPPGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGDVGSMGPHGAPGPRGPPGPSGSAGSPGLPGGVGQPGAVGEKGEPGNAGDAGPPGVPGIPGPKGEIGEKGDSGPSGAAGPPGKKGPPGEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPGSLGPRGDPGPAGPPGPPGSPAEVHGLRRRRSVLDTPEGGLEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGGETCLYPDKKFETVKLASWSREKPGGWYSTFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSIRFQGTNWEELSFNQTTAATIKVPHDGCRVRKGQAKTLFEFSSSVGFLPLWDVAAVDFGQTNQKFGFELGSVCFSS
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (B55) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha) (P63151)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Essential for serine/threonine-protein phosphatase 2A-mediated dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Leucine carboxyl methyltransferase 1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
Sequence:
MAGAGGGNDIQWCFSQVKGAVDDDVAEADIISTVEFNHSGELLATGDKGGRVVIFQQEQENKIQSHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAQFLLSTNDKTIKLWKISERDKRPEGYNLKEEDGRYRDPTTVTTLRVPVFRPMDLMVEASPRRIFANAHTYHINSISINSDYETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPNSCNTFVYSSSKGTIRLCDMRASALCDRHSKLFEEPEDPSNRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKIWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSVVMTGSYNNFFRMFDRNTKRDITLEASRENNKPRTVLKPRKVCASGKRKKDEISVDSLDFNKKILHTAWHPKENIIAVATTNNLYIFQDKVN