wanglab/gogpt-training-data huggingface dataset:
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI) (Q8C9W3)
Organism: Mus musculus (Mouse)
Function: Cleaves the propeptides of type I and II collagen prior to fibril assembly (By similarity). Does not act on type III collagen (By similarity). Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form with reduced collagen-binding activity (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Fibrillin-1
Sequence:
MDPPAGAARRLLCPALLLLLLPPPPLLLLPPPPASVRLVAATEPPGGPPGQGAERILAVPVRTDAQGRLVSHVVSLETAGAGVRARRAALDQTSGLPGGAAQDPGGRLFYNLTVFGRDLHLRLRPNARLVAPGATVEWQGETGDTRVEPLLGSCLYVGDVADLPKASSVALSNCDGLAGLIRMEEEEFFIEPLEKGQTDQEAEQGRVHVVYRRPPTPKPPPVSEPQALDTGVSQGNLDSLSRALGVLEERINSSRRRVRRHATDDDYNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSHAKSMSLIEIGNPSQSLENVCRWAYLQQKPDTDHDEYHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSYDCLRDDPFAHDWPALPQLPGLHYSMNEQCRFDFGLGYMMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTMCAPGKHCFKGHCIWLTPDILKRDGNWGAWTPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCNPQDCPNSLADFREEQCQQWDLYFEHGDVQHHWLPHEHRDAKERCHLYCESKETGEVVSMKRMVHDGTRCSYKDAFSLCVRGDCRKVGCDGVIGSRKQEDKCGVCGGDNTHCKVVKGTFTRSPRKQDYIKMFEIPAGARHLLIQEADTTSHHLSVKNLETGKFILNEENHLDPNSRSFIAMGVEWEYRNEDERETLQTIGPLHGTITVLVIPEGDTRISLTYKYMIHEDSLNVDDNNVLEDDAVRHEWALKKWSPCSKPCGGGSQFTKYGCRRRLDSKMVHRAFCSALAKPKAIRRACNPQECSQPVWVTGEWEPCTQSCGRTGMQVRSVRCIQPLHNNTTRSVHTKHCNDHRPESRRACNRELCPGRWRAGSWSQCSVTCGNGTQERPVLCRTADDNFGVCREERPETARICRLAPCPRNGSDPSKKSYVVQWLSRPDPDSPIQKISSKDQCQGDKSMFCRMEVLSRYCSIPSYNKLCCKSCNPPRNLSNTEDGGVEPPPGKHNDIDVFMPTLPGPTVATQVQPSPGPPLEAPLNVSSTNATEDHPETNAVDVPYKIHGVDEEVPSPNLIPRRPSLYVKTRNQRIQELINAVQRKEKPGKF
Protein: Clathrin light chain B (Lcb) (P08082)
Organism: Rattus norvegicus (Rat)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
Interaction partners:
- Clathrin heavy chain 1
- Clathrin light chain A
- AP-2 complex subunit beta
- AP-2 complex subunit mu
- AP-2 complex subunit alpha
- Epsin-2
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha-2
- Huntingtin-interacting protein 1
- Synergin gamma
Sequence:
MAEDFGFFSSSESGAPEAAEEDPAAAFLAQQESEIAGIENDSGFGAPAASQVASAQPGLASGGGSEDMGTTVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQKKRLQELDAASKVTEQEWREKAKKDLEEWNQRQSEQVEKNKINNRIADKAFYQQPDADTIGYVASEEAFVKESKEETPGTEWEKVAQLCDFNPKSSKQCKDVSRLRSVLMSLKQTPLSR
Protein: Phospholipid phosphatase-related protein type 4 (Brain-specific phosphatidic acid phosphatase-like protein 1) (Inactive 2-lysophosphatidate phosphatase PLPPR4) (Lipid phosphate phosphatase-related protein type 4) (Plasticity-related gene 1 protein) (PRG-1) (Q7TMB7)
Organism: Rattus norvegicus (Rat)
Function: Postsynaptic density membrane protein that indirectly regulates glutamatergic synaptic transmission through lysophosphatidic acid (LPA)-mediated signaling pathways. Binds lysophosphatidic acid (LPA) and mediates its internalization into cells. Could act as receptor or a transporter of this lipid at the post-synaptic membrane (By similarity). Modulates lysophosphatidic acid (LPA) activity in neuron axonal outgrowth during development by attenuating phospholipid-induced axon collapse.
Subcellular location: Postsynaptic density membrane {ECO:0000305|PubMed:12730698}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 15
Sequence:
MQRAGSSGARGECDISGTGRLRLEQAARLGGRAVHTSPTGGLGARQVAGMSAKERPKGKVIKDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAIPFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGAGLEPNINAGGCNFNSFLRRAVRFVGVHVVGLCSTALITDIIQLATGYQAPYFLTVCKPMYTSLEGSCKENSYIVEEICSGSDLTVINNGKKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQYKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSEDSMLQHRDALRSLTDLNQDPSRVLSAKNGSSGDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKESMVTFSNTLPRANTPSVEDPVRRNASIHASMDSARSKQLLTQWKSKNESRKMSLQVMDSEPEGQSPPRSIEMRSSSEPSRVGVNGDHHVPGNQYLKIQPGTVPGCNNSMPAGPRVSIQSRPGSSQLVHIPEETQENISTSPKSSSARAKWLKAAEKTVACNRGNNQPRIMQVIAMSKQQGVLQSSPKNAEGSTVTCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSSTEGEGSGSWKWKAPEKSSLRQTYELNDLNRDSESCESLKDSFGSGDRKRKHIDSNEHHHHGITTIRVTPVEGSEIGSETLSVSSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRPYKD
Protein: Phakinin (49 kDa cytoskeletal protein) (Beaded filament structural protein 2) (Lens fiber cell beaded filament protein CP 47) (CP47) (Lens fiber cell beaded filament protein CP 49) (CP49) (Lens intermediate filament-like light) (LIFL-L) (Q13515)
Organism: Homo sapiens (Human)
Function: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. Plays a role in maintenance of retinal lens optical clarity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q28177}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q28177}; Cytoplasmic side {ECO:0000250|UniProtKB:Q28177}. Cytoplasm {ECO:0000250|UniProtKB:D3ZER2}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q28177}. Note=Expressed primarily at the plasma membrane in peripheral lens fiber cells, however also localizes to the cytoplasm in mature lens fiber cells. {ECO:0000250|UniProtKB:Q28177}.
Interaction partners:
- Filensin
- Cytochrome b
- Beta-crystallin B1
- Gap junction alpha-8 protein
- Gap junction alpha-3 protein
- Gamma-crystallin D
- Gamma-crystallin S
- Beta-crystallin B2
- Pituitary homeobox 3
- Heat shock factor protein 4
Sequence:
MSERRVVVDLPTSASSSMPLQRRRASFRGPRSSSSLESPPASRTNAMSGLVRAPGVYVGTAPSGCIGGLGARVTRRALGISSVFLQGLRSSGLATVPAPGLERDHGAVEDLGGCLVEYMAKVHALEQVSQELETQLRMHLESKATRSGNWGALRASWASSCQQVGEAVLENARLMLQTETIQAGADDFKERYENEQPFRKAAEEEINSLYKVIDEANLTKMDLESQIESLKEELGSLSRNYEEDVKLLHKQLAGCELEQMDAPIGTGLDDILETIRIQWERDVEKNRVEAGALLQAKQQAEVAHMSQTQEEKLAAALRVELHNTSCQVQSLQAETESLRALKRGLENTLHDAKHWHDMELQNLGAVVGRLEAELREIRAEAEQQQQERAHLLARKCQLQKDVASYHALLDREESG
Protein: Methyltransferase (Q5AMT3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein IMP4
- Ribosome biosynthesis protein
- Nucleolar GTP-binding protein 2
- U three protein 7
- U3 small nucleolar RNA-associated protein 11
- Rei1p
- rRNA-processing protein
- Bud22p
- Ribosomal RNA-processing protein 8
- Mitochondrial 37S ribosomal protein RSM22
Sequence:
MAKRKATESEPLPTKKPTKSVSETTISICIPSTVISSKNAYNLQQITNIIYQIAKACTIYKVAEIIVFDVPQSNNDKEDDKSTVVVGSKVKFVEDEPEKTLANPSKKSNVNGDKVSPSLLVASLLQFFITPPYLVKTMFSSHLNSKFKNILPKFTYAFKLPKITTLPFMQNNQVYKDFKEGMIIPRETPLMKKKNKKTKSDHKITVSKYVNIGEKEALKLNIKREIPIYSRVTVDLKNKTVVSPLQAYGVVGHKAAFGYHVRMASEFNKIFTQSPISDGYSSTIYVNCDDYFGNNNKISELDNLSTFKEATGNVLMVLGNYKDLQAGFKADTSNVFENIDSVAHLFDSKLNIPDGCRIEDAILISLAKVIE
Protein: MAP3K epsilon protein kinase 1 (AtM3KE1) (EC 2.7.11.1) (Mitogen-activated protein kinase kinase kinase 7) (Q9LJD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells. Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion, cell elongation, and embryo development.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane {ECO:0000269|PubMed:16965555}. Note=Accumulates in the nucleolus during interphase (PubMed:15292395). Localized to the plasma membrane in developing pollen grains (PubMed:16965555). {ECO:0000269|PubMed:15292395, ECO:0000269|PubMed:16965555}.
Interaction partners:
Sequence:
MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYKGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSSKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVAVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDNPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIKYMKEATASSEKDDEGSQDAAESLSGENVGISKTDSKSKLPLVGVSSFRSEKDQSTPSDLGEEGTDNSEDDIMSDQVPTLSIHEKSSDAKGTPQDVSDFHGKSERGETPENLVTETSEARKNTSAIKHVGKELSIPVDQTSHSFGRKGEERGIRKAVKTPSSVSGNELARFSDPPGDASLHDLFHPLDKVSEGKPNEASTSMPTSNVNQGDSPVADGGKNDLATKLRATIAQKQMEGETGHSNDGGDLFRLMMGVLKDDVIDIDGLVFDEKVPAENLFPLQAVEFSRLVSSLRPDESEDAIVSSCQKLVAMFRQRPEQKVVFVTQHGFLPLMDLLDIPKSRVICAVLQLINEIIKDNTDFQENACLVGLIPVVMSFAGPERDRSREIRKEAAYFLQQLCQSSPLTLQMFIACRGIPVLVGFLEADYAKYREMVHLAIDGMWQVFKLKRSTPRNDFCRIAAKNGILLRLINTLYSLNEATRLASISGGLDGQAPRVRSGQLDPNNPIFGQNETSSLSMIDQPDVLKTRHGGGEEPSHASTSNSQRSDVHQPDALHPDGDKPRVSSVAPDASTSGTEDVRQQHRISLSANRTSTDKLQKLAEGASNGFPVTQTEQVRPLLSLLDKEPPSRHYSGQLDYVKHITGIERHESRLPLLHGSNEKKNNGDLDFLMAEFAEVSGRGKENGSLDTTTRYPSKTMTKKVLAIEGVASTSGIASQTASGVLSGSGVLNARPGSATSSGLLAHMVSTLSADVAREYLEKVADLLLEFARADTTVKSYMCSQSLLSRLFQMFNRVEPPILLKILECTNHLSTDPNCLENLQRADAIKHLIPNLELKDGHLVYQIHHEVLSALFNLCKINKRRQEQAAENGIIPHLMLFIMSDSPLKQYALPLLCDMAHASRNSREQLRAHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDNDNRKVEQALLKQDAIQKLVDFFQSCPERHFVHILEPFLKIITKSYRINKTLAVNGLTPLLISRLDHQDAIARLNLLKLIKAVYEHHPRPKQLIVENDLPQKLQNLIEERRDGQRSGGQVLVKQMATSLLKALHINTIL
Protein: Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB1, chloroplastic (Q9LSE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the biogenesis and accumulation of native cytochrome b6 in the thylakoid membrane. Controls the conversion of apocytochrome b6 to holocytochrome b6. Required for covalent binding of the c-type heme to cytochrome b6.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:18593701}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB4
- Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB3, chloroplastic
- Cytochrome c biogenesis protein CCS1, chloroplastic
- Thioredoxin-like protein HCF164, chloroplastic
- Cytochrome c-type biogenesis ccda-like chloroplastic protein
- Photosystem II stability/assembly factor HCF136
- Cytochrome c biogenesis protein CcsA
- Pterin-4-alpha-carbinolamine dehydratase 2, mitochondrial
- AT3g17930/MEB5_15
Sequence:
MATKLISPPLSCPWVTSREVIIKGLPRRRREWMVTKRNRVSAVTAMIVEPLSVVSSSAIQIHQWWEQNPNSLLLMTEATGGYSLASYYTSLGLFVISVPGLWSLIKRSVKSKIVRKTFVVNDVKKEPKQVAGEILSFFTRKNFNITDRGETITFEGKMVPSRGQAALLTFCTCISLASVGLVLTITVPDFGNNWFFIILLSPLAGVYYWKKASRKEEIKVKMMVGSKGRLDEIVVQGDDVQVEEMRKELQLNEKGMVYVKGLFERSS
Protein: DNA damage-inducible protein D (P23840)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YebG
- DNA damage-inducible protein I
- DNA repair protein RecN
- LexA repressor
- Protein RecA
Sequence:
MNEHHQPFEEIKLINANGAEQWSARQLGKLLGYSEYRHFIPVLTRAKEACENSGHTIDDHFEEILDMVKIGSNAKRALKDIVLSRYACYLVVQNGDPAKPVIAAGQTYFAIQTRRQELADDEAFKQLREDEKRLFLRNELKEHNKQLVEAAQQAGVATATDFAIFQNHGYQGLYGGLDQKAIHQRKGLKKNQKILDHMGSTELAANLFRATQTEEKLKRDGVNSKQQANTTHFDVGRKVRQTIQELGGTMPEELPTPQVSIKQLENSVKITEKK
Protein: Uncharacterized protein PB2B2.11 (Q9HDU4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Galactose-1-phosphate uridylyltransferase
- Galactokinase
- Mannose-1-phosphate guanyltransferase
- Bifunctional protein gal10
- Probable 2-dehydropantoate 2-reductase
- UPF0643 protein PB2B2.08
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Probable mannose-1-phosphate guanyltransferase
Sequence:
MTGDYKEYKGYALITGGAGFIGSNFLDYAVDKYPDFHFTCIDKLSYVSNYTTVFLSKVLNQPNFRFLEMDLATNYKFLYQFMVEDSEINKITHIINFAAESSVDRSFIDPLYFTKNNILSTQNLLECVRILLGKKEELRNRLNFVHVSTDEVYGEQDENASVDEKSKLNPTSPYAASKAAVDLIIQSYRYSYKISVTVIRANNVYGPRQYEEKLIPMTLGKLKKFINQKSQKIMQDKITLHGDGLHKRKYLHIYDFINAIDLVWMKQGSEVYHSTLESKMSGQIFNIGSDDEIDNLSLVKFICDYFLYRKLSLKNLDYSKYITFVQDRNYNDSRYSLNYEKIKSLGWRPQIPLETGLRKLIDEYY
Protein: Pregnancy specific beta-1-glycoprotein 17 (Pregnancy specific glycoprotein 17) (Pregnancy-specific glycoprotein) (Q62056)
Organism: Mus musculus (Mouse)
Interaction partners:
- CD9 antigen
Sequence:
MEVSSELLSNGCTPWQRVLLTASLLSCCLLPTTARVTVEFLPPQVVEGENVLLRVDNLPENLLGFVWYKGVASMKLGIALYSLQYNVSVTGLKHSGRETLHRNGSLWIQNVTSEDTGYYTLRTVSQRGELVSDTSIFLQVYSSLFICERPTTLVPPTIELVPASVAEGGSVLFLVHNLPEYLISLTWYKGAVVFNKLEIARYRTAKNSSVLGPAHSGRETVFSNGSLLLQNVTWKDTGFYTLRTLNRYPRIELAHIYLQVDTSLSSCCHPLDSPQLSIDPLPPHAAEGGRVLLQVHNLPEDVQTFSWYKGVYSTILFQIAKYSIATKSIIMGYARSRRETVYTNGSLLLQDVTEKDSGVYTLITTDSNMGVETAHVQVNVHKLATQPVIKATDSTVRVQGSVIFTCFSDNTGVSIRWLFNNQRLQLTERMTLSPSKCQLWIRTVRKEDAGEYQCEAFNPVSSKTSLPVILAVMIE
Protein: Tigger transposable element-derived protein 3 (Q6B0B8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583}.
Interaction partners:
- CTP synthase 1
- CTP synthase 2
- RNA-binding Raly-like protein
Sequence:
MELSSKKKLHALSLAEKIQVLELLDESKMSQSEVARRFQVSQPQISRICKNKEKLLADWCSGTANRERKRKRESKYSGIDEALLCWYHIARAKAWDVTGPMLLHKAKELADIMGQDFVPSIGWLVRWKRRNNVGFGARHVLAPSFPPEPPPPGLTSQAQLPLSLKDFSPEDVFGCAELPLLYRAVPGSFGACDQVQVLLCANSRGTEKRRVLLGGLQAAPRCFFGIRSEALPASYHPDLGIPWLEWLAQFDRDMGQQGRQVALLLAARVVEELAGLPGLYHVKLLPLAASSTTPPLPSSVVRAFKAHYRHRLLGKLAAIQSERDGTSLAEAGAGITVLDALHVASAAWAKVPPQLIFSSFIQEGLAPGKTPPSSHKTSEMPPVPGGLSLEEFSRFVDLEGEEPRSGVCKEEIGTEDEKGDREGAFEPLPTKADALRALGTLRRWFECNSTSPELFEKFYDCEEEVERLCCL
Protein: Small ribosomal subunit protein bS18B (30S ribosomal protein S18 2) (P9WH47)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Interaction partners:
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS14A
- Large ribosomal subunit protein bL28B
- Large ribosomal subunit protein bL33A
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS7
Sequence:
MAAKSARKGPTKAKKNLLDSLGVESVDYKDTATLRVFISDRGKIRSRGVTGLTVQQQRQVAQAIKNAREMALLPYPGQDRQRRAALCP
Protein: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Q9QUR7)
Organism: Mus musculus (Mouse)
Function: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (By similarity). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (By similarity). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (By similarity). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:29686383}. Nucleus speckle {ECO:0000250|UniProtKB:Q13526}. Cytoplasm {ECO:0000250|UniProtKB:Q13526}. Note=Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73 by DAPK1 results in inhibition of its nuclear localization. {ECO:0000250|UniProtKB:Q13526}.
Interaction partners:
- Homeodomain-interacting protein kinase 2
- Interferon regulatory factor 3
- Cellular tumor antigen p53
- Peptidyl-prolyl cis-trans isomerase
- Neutrophil cytosol factor 1
- Neutrophil cytosol factor 4
- Neutrophil cytosol factor 2
- DNA-directed RNA polymerase II subunit RPB1
- Gephyrin
- Mothers against decapentaplegic homolog 3
Sequence:
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGGSTVGGSSKNGQGEPAKVRCSHLLVKHSQSRRPSSWRQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGPFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
Protein: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC 7.1.1.2) (Complex I-75kD) (E5KRK5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
Sequence:
MLRIPVRKALVGLSKSPKGCVRTTATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKVLFLLGADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDDIEGANYFQQANELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQAVEEPSIC
Protein: Methyl-CpG-binding domain-containing protein 11 (AtMBD11) (MBD11) (Methyl-CpG-binding protein MBD11) (Q9LW00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that binds DNA independently of its methylation status. Required during plant organogenesis and development.
Subcellular location: Nucleus {ECO:0000269|PubMed:12954765, ECO:0000269|PubMed:15010609}.
Interaction partners:
- Methyl-CpG-binding domain-containing protein 8
- Methyl-CpG-binding domain-containing protein 6
- Methyl-CpG-binding domain-containing protein 9
- Methyl-CpG-binding domain-containing protein 2
- Methyl-CpG-binding domain-containing protein 7
- Methyl-CpG-binding domain-containing protein 5
- Methyl-CpG-binding domain-containing protein 4
- Methyl-CpG-binding domain-containing protein 1
- Methyl-CpG-binding domain-containing protein 13
- Putative methyl-CpG-binding domain protein 12
Sequence:
MGGEEEVVSVELPAPSSWKKLFYPNKVGSVKKTEVVFVAPTGEEISNRKQLEQYLKSHPGNPAIAEFDWTTSGTPRRSARISEKTKATPSPDKEPPKKRGRTKSPVSKKDAEGEKSEGGGEENSHVKDTEMNPPEGIAENENVTDKNGSGETERVNDAKENIVAEETPNAAPVQEEGESMKEKALDSVDDKSKETDKEKDTGSIEKNSVDVEKKTVEASDEKKNSEAETRNHEENGLTTEAEGKEKTAEGEATG
Protein: Intrinsically Disordered Protein, class C (O16463)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHSAIGLLLVIASASQAQVLSLNCATPPCPEPMPVCATPPCPPQYAPLPPPPMPAPAPAYNPYPCANPPCIVVEPMPVAPPAPAPAYNPYPCATPPCPLPYIPEPVAPVPAPAPVYEPYACAAPPCPPPTPVYEPYACAAPPCPAPVAPQPVIQHVPVPVPVQVPVPIRVPVPVPVPTPVYQPTYCAVPPCPAPAATPVYAQPAPRPMPVYAPAPACAQPPCPAYNPYGYQGTPGYAPAYNPYSYVLRSPVAAAPGYAQGYAPAYAQGYAPAYAPSYAPAYAPSPFRRAMYLLGSNKGKKAAAAAAAATEEKKKTA
Protein: CRAL-TRIO domain-containing protein (Q57YC5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Haemolysin-III related
Sequence:
MVKTVSSLNSVDKLSHGTVSESSSRAQGQCPQRVLRELRDYLSITPHNEADGLTEAYLLRCLEATEHSIPKTVQLLRQRRVFEQTFPTIRLTPQVLTALRSGAISTIGRDLQGRLVLYIHPKCFKQDPLDEQETQRLFVIVMEYALGCCTANQAPQQVLTTESPRVVHTDRRTSASEVQKQQIVVLVNEEGSSWHSSNMALSRAKSLLALLTKYYPRLVVQILLYQPSCDVKLLVKHVLPSGPAASGALTAVEVVTPNHIQKYISPTTLPEELGGTSNFVSSSSSSAFADAVLRHWFLETSYLLTEDASSRPIWKLPPCTVAAAGWSNLLARASAAAVAKCGTTNYVAITDGNEGADYHVDPLSGEVNREQLHARVDNWVQESHVMYSRCRGQIRCSSAEAENDDGGGSILSDVHFLSCREAELSTSDVWLGVDGFNSAAEREALLRELQNERNRRFAMEKQLLNSRTSLGTTTQLDAQVTEKIEEALKTARVSLNMLVMNVVACAQESEACGNPPTLRQLLDLTLTTIEGGTSEVQKVSNMKSPKLVKKKKEDKSSCCTVM
Protein: Dual specificity mitogen-activated protein kinase kinase 4 (MAP kinase kinase 4) (MAPKK 4) (EC 2.7.12.2) (JNK-activating kinase 1) (MAPK/ERK kinase 4) (MEK 4) (SAPK/ERK kinase 1) (SEK1) (Stress-activated protein kinase kinase 1) (SAPK kinase 1) (SAPKK-1) (SAPKK1) (c-Jun N-terminal kinase kinase 1) (JNKK) (P45985)
Organism: Homo sapiens (Human)
Function: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to pro-inflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase kinase kinase 7
- Beta-arrestin-2
- Mitogen-activated protein kinase kinase kinase 5
- Mitogen-activated protein kinase kinase kinase 1
- Mitogen-activated protein kinase 14
- C-Jun-amino-terminal kinase-interacting protein 3
- Filamin-B
- Filamin-C
Sequence:
MAAPSPSGGGGSGGGSGSGTPGPVGSPAPGHPAVSSMQGKRKALKLNFANPPFKSTARFTLNPNPTGVQNPHIERLRTHSIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKILDQMPATPSSPMYVD
Protein: Biliverdin reductase B (A0A2R8YEP4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAADVDKTVAGQDAVIVLLGTRNDLSTEPPLCPRPSPTPRPPAPPPPPAPPLPPLPPPPPTSDSHSLSPLRSHDSDVRGRPEHCGSHEGSWCGQAFLLWDPTKVPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTDEYDGHSTYPSHQYQ