wanglab/gogpt-training-data huggingface dataset:
Protein: Ephrin type-B receptor 2 (EC 2.7.10.1) (EPH-like kinase 5) (EK5) (cEK5) [Cleaved into: EphB2/CTF1; EphB2/CTF2] (P28693)
Organism: Gallus gallus (Chicken)
Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
Interaction partners:
- Ephrin-A5
- Ephrin-B1
- Ephrin-B2
- Ephrin-A2
- Ephrin RBD domain-containing protein
- Ephrin type-A receptor 4
- Uncharacterized protein.
Sequence:
MGPLWFCCLPLALLPLLAAVEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHVEMKFSVRDCSSIPNVPGSCKETFNLYYYESDFDSATKTFPNWMENPWMKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSKNGFYLAFQDYGGCMSLIAVRVFYRKCPRVIQNGAVFQETLSGAESTSLVAARGTCISNAEEVDVPIKLYCNGDGEWLVPIGRCMCRPGYESVENGTVCRGCPSGTFKASQGDEGCVHCPINSRTTSEGATNCVCRNGYYRADADPVDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQFAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKNLSELNSTAVKSPTNTVTVQNLKAGTIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSVQEKLPLIIGSSAAGLVFLIAVVVIIIVCNRRRGFERADSEYTDKLQHYTSGHSTYRGPPPGLGVRLFVMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSSPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPNALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGVNLPLLDRTIPDYTSFNTVDEWLDAIKMSQYKESFASAGFTTFDIVSQMTVEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEV
Protein: Altered inheritance of mitochondria protein 4 (Synthetic with old yellow enzyme protein 1) (P38305)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10684247}.
Interaction partners:
- Pre-mRNA-splicing factor URN1
- Altered inheritance of mitochondria protein 3
Sequence:
MDQKKDPSNNLTERRVSKVQRPNKKKVRNQVESLSRNLERNKEGQLLQTVSKGHLEADSGHSLGREKENGELGIRSIFYDKDWNPRGTAPSHYRNIPYNPATFKRRTEVQARLGNLENIKIPK
Protein: DEK proto-oncogene (A0A494C028)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQVHSMSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS
Protein: Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na(+)/H(+) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1) (O14745)
Organism: Homo sapiens (Human)
Function: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa.
Subcellular location: Cytoplasm {ECO:0000250}. Apical cell membrane {ECO:0000250}. Endomembrane system; Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus. Note=Translocates from the cytoplasm to the apical cell membrane in a PODXL-dependent manner. Colocalizes with CFTR at the midpiece of sperm tail (By similarity). Colocalizes with actin in microvilli-rich apical regions of the syncytiotrophoblast. Found in microvilli, ruffling membrane and filopodia of HeLa cells. Present in lipid rafts of T-cells. {ECO:0000250}.
Interaction partners:
- Cystic fibrosis transmembrane conductance regulator
- Moesin
- Ezrin
- Radixin
- Beta-2 adrenergic receptor
- Sodium/hydrogen exchanger 3
- Sodium-dependent phosphate transport protein 2A
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MSADAAAGAPLPRLCCLEKGPNGYGFHLHGEKGKLGQYIRLVEPGSPAEKAGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDEQLQKLGVQVREELLRAQEAPGQAEPPAAAEVQGAGNENEPREADKSHPEQRELRPRLCTMKKGPSGYGFNLHSDKSKPGQFIRSVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIRAGGDETKLLVVDRETDEFFKKCRVIPSQEHLNGPLPVPFTNGEIQKENSREALAEAALESPRPALVRSASSDTSEELNSQDSPPKQDSTAPSSTSSSDPILDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL
Protein: Transcription factor bHLH36 (Basic helix-loop-helix protein 36) (AtbHLH36) (bHLH 36) (Transcription factor EN 6) (bHLH transcription factor bHLH036) (Q9FLI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Glucose-methanol-choline
- Protein GRIP
- Peroxidase 20
- Transcription factor bHLH137
- Zinc finger CCCH domain-containing protein 63
- Putative transcription factor bHLH041
- Transcription factor bHLH153
- Transcription factor bHLH123
- At1g12570
Sequence:
MEKMMHRETERQRRQEMASLYASLRSLLPLHFIKGKRSTSDQVNEAVNYIKYLQRKIKELSVRRDDLMVLSRGSLLGSSNGDFKEDVEMISGKNHVVVRQCLVGVEIMLSSRCCGGQPRFSSVLQVLSEYGLCLLNSISSIVDDRLVYTIQAEVNDMALMIDLAELEKRLIRMK
Protein: Complexin-2 (Complexin II) (CPX II) (Synaphin-1) (Q6PUV4)
Organism: Homo sapiens (Human)
Function: Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Also involved in mast cell exocytosis (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P84087}. Presynapse {ECO:0000250|UniProtKB:P84087}. Nucleus {ECO:0000250|UniProtKB:P84087}. Perikaryon {ECO:0000250|UniProtKB:P84087}. Note=Translocated from the perikaryon to the presynaptic terminals during maturation of neuronal cells. In mast cells, cytosol and nucleus. Becomes enriched near plasma membrane following stimulation. {ECO:0000250|UniProtKB:P84087}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Complexin-4
- Syntaxin-1A
- Complexin-1
- Synaptosomal-associated protein 25
- Complexin-3
- Neurogenic differentiation factor 2
- Synaptotagmin-1
- Syntaxin-3
- Synaptosomal-associated protein 23
Sequence:
MDFVMKQALGGATKDMGKMLGGEEEKDPDAQKKEEERQEALRQQEEERKAKHARMEAEREKVRQQIRDKYGLKKKEEKEAEEKAALEQPCEGSLTRPKKAIPAGCGDEEEEEEESILDTVLKYLPGPLQDMFKK
Protein: Dopamine receptor D4a (A0A0R4IR92)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVEADMPANLTISTHTTNYNFPALIFGILLIIIIICGNVLVCLSVYTEKALKTTTNYFIVSLAVADLLLAVLVLPLFVYAEFQDGVWSLNMTVCDGLMTMDVMLCTASIFNLCAISIDRFIAVSIPLNYNRKHVDQRQIVLLSATWILALAVASPVMFGINNVPNRDHSECKLEDNNYVIYSSVCSFFVPCPIMLLLYCGMFRGLRNWEEARKAKLRSNMEACRKLQEAAASLQPLSGLPPPLPPVIEKDITLEELDQDHYPDPDSPDPVSMLAYPGGGYNQDQNQNRQRKRAKINGRERKAMRVLPVVVGAFLFCWTPFFVVHTMRALCEDCEIPGSVTSIVTWLGYVNSAINPIIYTVFNTEFRKFFRKFLPTLPGCC
Protein: Aminodeoxychorismate synthase, chloroplastic (ADC synthase) (EC 2.6.1.85) (P-aminobenzoic acid synthase) (PABA synthase) (Para-aminobenzoate synthase) (Q6TAS3)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Bifunctional enzyme that catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. In the first step, a glutamine amidotransferase generates ammonia that is channelled between the binding sites of glutamine and chorismate and used along with chorismate in the second step, catalyzed by aminodeoxychorismate synthase, to produce ADC. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis. Does not possess ADC lyase activity.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14745019}.
Interaction partners:
- anthranilate synthase
- indole-3-glycerol-phosphate synthase
- aminodeoxychorismate lyase
- Pterin-binding domain-containing protein
- anthranilate phosphoribosyltransferase
- anthranilate phosphoribosyltransferase
- Chorismate synthase 2, chloroplastic
- Chorismate synthase 1, chloroplastic
- Anthranilate phosphoribosyltransferase
- GTP cyclohydrolase 1
Sequence:
MNSAMSSSSSFMVASSCCQNLQTRKYFLLAPEPFEKIGMIDALQKYNRKERKVFISSHLVPGHLDASGTRKKFLHEPVPKLEFVRTLLIDNYDSYTYNIFQELSIINGMPPVVIRNDEWTWKEVYHYLYEERTFDNIVISPGPGSPTCPSDIGICLRLLLECIDIPILGVCLGHQALGYVHGAEVVHAPEPFHGRLSDIEHNGCQLFHEIPSGRSSGFKVVRYHSLVIDPKSLPKELIPIAWTSTAETLPFQGVKRSNSFLNASKENKDIFNGMSELSDDSKDVKGGKVLMGIMHSSRPHYGLQFHPESVATCYGRQLFKNFRKITEDYWLLLMSTSFNERRAHYAACMQVPNLDPLSRSVAKRGHLVNKLIERRTAEVDGTLNLSHPGHSVKFLKMTWKKLDCSASQVGGADNIFCELFGDQEAKNSFWLDSSSIEKERARFSFMGGKGGSLWKQLSFRLSNRSDRMCKGGGHLSVEDANGHVISKFLEDGFFDYLDKELLSFCFDEKDYEGLPFDFYGGYIGYIGYDLKAECGVASNRHRSKTPDACLFFTDNVIVIDHQYDDIYTLSLHDGSTSTTSRLEDLEQRLLNLRAFTPRRLQSQASRGFSVVELKSGFSAEKSREQYIKDVENCQEFIKEGESYELCLTTQMRMKLGGIDSLELYRNLRIRNPAPYAAWLNFSRENLSICCSSPERFLRLDRNAILEAKPIKGTIARGSTPKEDEFLKLQLECSEKDQAENLMIVDLLRNDLGRVCETGSVHVPHLMEIESYATVHTMVSTIRGKKRSDASAIDCVRAAFPGGSMTGAPKLRSMELLDHLENCSRGIYSGCIGFFSYNQAFDLNIVIRTVVIHEGEASVGAGGAITALSDPNDEYEEMLLKTRAPIKAVLEHQSSIFSSDAQK
Protein: C2H2-type domain-containing protein (Q8BXC7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLERNLMNVINVVKPFLLITFFIYIKERILERNPMSVINVVKPLHITVIFKCMEEFIQERNLINVINVVKPLHVTEISEYIKENILERNPMNLTIIVKPFHNTVVFKYIKEHILERNPMNYNQCGKAFAHHSHLQRHERNHTERKPCECI
Protein: Glycogen synthase kinase-3 beta (EC 2.7.11.26) (A0A3B3ITW1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQDANTGDRGQTNNAASASASNST
Protein: Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l) (P68431)
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 H2B type 2-E
- DNA
- Histone chaperone ASF1A
- Histone H2A type 2-A
- Chromobox protein homolog 3
- Histone H4-like protein type G
- Histone H2A type 2-C
- DNA
- Chromobox protein homolog 1
- Histone H4
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (E2K) (Q7ZVL3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MLCHSRCLSRSLGRSITALRQGNSVLARRATSGIAASQCVSFQDSPRCETRSSVYQIRYFKTTAAHRNEVITVKTPAFAESVTEGDVRWEKAVGDSVAEDEVVCEIETDKTSVQVPSPAAGVIEELLVPDGGKVEGGTPLFKLKKGAGAVKTAAAVGAPPPAAKTPAPAAPAPAAAPAGGPIPSSMPPVPAVPAQPIQAKPVSAIKPTAAAPAAAAADTGAKAPRSEHRVKMNRMRLRIAQRLKEAQNTCAMLTTFNEVDMSNITEMRTHYKDAFLKKHGIKLGFMSAFVKAAAYALTDQPAVNAVIDDTTKEIVYRDYVDISVAVATPKGLVVPVIRGVEGMNFADIEKTINELGEKARKNELAVEDMDGGTFTISNGGVFGSMFGTPIINPPQSAILGMHGIFDRPVAIAGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKSVVEDPRVLLLDM
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q59LK7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Hym1p
- Sog2p
- CBK1 kinase activator protein MOB2
- Cas4p
Sequence:
MQMNATSLYKRTEVIGRGKFGVVYKAQNKQTKQIVAIKVLNLDTEEDEVIDVQQEIQFLSELKNVPNITHYYGCILNDTKLWIIMDYCAGGSLRTLLKAGVLEERYVAVIVRELLMTLSAVHKLGVIHRDLKAANVLISKEGNVQLCDFGVAAKITANSTKRTTMAGTPYWMAPEVIRTGDTYNSKADIWSLGITIYEIATGNPPYCDKDASWAMQLISKSTPPRLEGREFSQALKECIALCLDENPEERPSADDLMKCKLVKIYKNHPTSILKEVISRYLLWRDRNSSRDSVFINLENEQEDSVDEIVNKNLDGGYHNQQQQHQQQQQQNDHQDHDGHNNQIQVKWDFDSLSSREYIMENDIDLDKVNQQYNNNFDTQQGNTYSTLPTLKAPTTKNNTLAATNQNSMTASKNNSKSTTEVPKSLQMLFEDNSEEQEDLAPPKSNVNIMERMESPTIEIPDMDSLSQLPSASATNTTNHPQLNKPPALYHSQSASGNLESRFSSLNTSPKDNGGSTGGNNGINRPRKKTISNTGGTANAQFQQTSSAVPHTPPYTTPASVRTPSPKPPSSVNLLNATSMSKTGSPSKMKALQSSSNPLLQPINMKSENMNAGITGGTGSHPPMQAPPQLITQQSLPVLPTSSSTSASVSTSTTTTTTATSTTSGGMAGNMKSQRNKPGFIQMPTPSNTLINNMSSLTNDHQDGGNNGGGGGDNNNVNQFGINPAQAASMPVSMTPVTEKDHSQLFPNINNDESLEKTNNGSGNSRSHQNSLSSQKKSLASSSSHNLSSLGFSNGNNSAPTTAAASTAPPPPPTMFANRGSSNSVSQSQANFSLNGGGATNNGNPTFSVFPTIPNINGDIFSDTVSKQKLVNELDVMITLFNQGLEVLEEIL
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) (Q8STB9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MRFQWFLSASASLSLFLLLDFVVWIHGERDFNVNDSQVPVIEPKDVPAYKQDPYVTELMSCQNTPSEIVLSLLLKKHDWSELTATKRAHVQAKLAKFFAIPKEFISLDSVSKRELRSMHKLAMRKGGKGNKNIETLNRRLGRASFMIGCGPSYFVMGEPIAKQIAHQMKDGTIGALTEENFGLWFIWRKELKSRSNRKRRQSEGSGADEDDYDYGDDDEEVAEPSTEVPPVTTHAHRHHHGAPNTVLNELELSTQLPIDDFEGTATATQPTGTATATAIASTAAAAAATAAAATATATTANASATTAGESEFHIESTTHRTISSKEGGEPDAISSGNNSLANNELSTPATPTSSVATTTASTPESSSISSNFVSTDYMEPQPEENSPPIIKTRLQKLAVTSGKAFTFHVLPETFYDAEDQGNLRLALTDKDGHELKANSWLQFNADKRELYGLPLDDTVSRWQYRLSATDSGNASVTETVEISVQQHRAVRTINHEISVFVRINEKPGHNIDWQLKLINAVARTLDDSTNSAVVVREIRQTPHDPHSATFVYFNETLPTSECPEKELKDIIARLDANRLSDLVQPQLGIKSITGQLIGSCQKDLTQVKPTQHMTKNVPPMPRNQVDRVNASLGQLLVYKVPADTFYDANDNQLTLTLKTRDHLELSPRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVAEDSGGLSAHDALVVVVSPAPKRDFGFFFKAYLSIKHERFNADLQRKFVERVAKLNGDPTTGQIQIRSITTHHDSDGTIVNFYNTTLYRKHNSCREKEVAMTRSVYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSRPEEPTHKSSFGEDYMITFVWPIVIIVAMLVAASIIACCLHWCRQRSGKMELGDEEERKSFRAKGIPVIFQDEYEEKPEIGNKSPVILKDEKPPLLPPSYNTSNMNGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP
Protein: Polypyrimidine tract-binding protein 3 (Regulator of differentiation 1) (Rod1) (Q8BHD7)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes Fas exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U) (By similarity).
Interaction partners:
- Ribonucleoprotein PTB-binding 1
Sequence:
MNSSTSAGVYANGNDNKKFKGDRPPCSPSRVLHLRKIPCDVTEAEVISLGLPFGKVTNLLMLKGKSQAFLEMASEEAAVTMINYYTPVTPHLRSQPVYIQYSNHRELKTDNLPNQARAQAALQAVSAVQSGNLSLPGATANEGTLLPGQSPVLRIIIENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVNAQYAKMALDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDFTRLDLPTGDGQPSLEPPMAAAFGAPGIMSSPYAGAAGFAPAIAFPQAAGLSVPAVPGALGPLTLTSSAVSGRMAIPGASGMPGNSVLLVTNLNPDFITPHGLFILFGVYGDVHRVKIMFNKKENALVQMADASQAQLAMNHLSGQRLYGKVLRATLSKHQAVQLPREGQEDQGLTKDFSNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVTMDDLKNLFTEAGCSVKAFKFFQKDRKMALIQLGSVEEAIQALIELHNHDLGENHHLRVSFSKSTI
Protein: U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (Nudix hydrolase 16) (U8 snoRNA-binding protein H29K) (m7GpppN-mRNA hydrolase) (Q96DE0)
Organism: Homo sapiens (Human)
Function: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs. Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21337011}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011}. Note=Localized predominantly in the cytoplasm (PubMed:21070968). Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity). {ECO:0000250|UniProtKB:Q6TEC1, ECO:0000269|PubMed:21070968}.
Interaction partners:
- TP53-binding protein 1
- Inosine triphosphate pyrophosphatase
- 5'
- Adenylosuccinate synthetase isozyme 2
- Cytosolic 5'-nucleotidase 3A
- AMP deaminase 2
- AMP deaminase 3
- AMP deaminase 1
- Nucleoside diphosphate kinase B
- Cytosolic purine 5'-nucleotidase
Sequence:
MAGARRLELGEALALGSGWRHACHALLYAPDPGMLFGRIPLRYAILMQMRFDGRLGFPGGFVDTQDRSLEDGLNRELREELGEAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEELLAVEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDLGLLQSGSISGLKIPAHH
Protein: Polynucleotide kinase 3'-phosphatase (M0R3C8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLHPLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENLEKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIPRKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPFQVLVATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPANWAPGRKKKDFSCADRLFALNLGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSGPLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNRVRPVCPSRGRPLPLLPLHRHSGAGAPQQPVSRDDGLLSYPRVRHGHVWLQEAVRGPNAG
Protein: T-cell acute lymphocytic leukemia protein 1 homolog (TAL-1) (Stem cell protein) (zSCL) (O93507)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that plays a pivotal role in hemopoietic and endothelial development, acting synergistically with lmo2 and downstream of clo. Specifies mesodermal precursors to a hemangioblast cell fate. Hemangioblasts are bipotential precursors of blood and endothelium, and in the absence of hemopoietic induction cues such as gata1, tal1/scl-lmo2-induced hemangioblasts differentiate into endothelial cells. Isoform alpha and isoform beta are redundant for the initiation of primitive hemopoiesis but have distinct roles in the regulation of primitive erythroid differentiation and definitive hemopoietic stem cell specification, most likely due to differences in expression levels. Specification of definitive hemopoietic stem cells requires isoform beta. DNA binding is required for erythroid maturation, but not for its other hemopoietic functions. Endothelial roles include development of the dorsal aorta, the site of definitive hemopoiesis in the embryo. Required for angiogenesis but not angioblast specification. Has an additional role in endocardium formation during heart development. May play a role in central nervous system development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P22091, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- GATA-binding protein 1a.
- Rhombotin-2
- LIM domain-binding protein 1-A.
- Transcription factor 3a.
- Endothelial transcription factor GATA-2a
- Runt-related transcription factor
- LIM domain-binding protein 1-A
- Transcription factor GATA-3
- ETS variant transcription factor 2
- Rhombotin-1
Sequence:
MMEKLKSEQFPLSPSAEGCASPPRGDGDARGKQEGTTAETGEHRLPEELNGVAKETAHHATELKKEVAVIELSRRGGSADIKGRELKAELSHKVQTTELCRPPIPLPLPPRDPLSDTRMVQLSPPAFPLPARAMLYSNMTTPLATINSGFAGDAEQYGMYPSNRVKRRPAPYEVEINDGSQPKIVRRIFTNSRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYINFLAKLLNDQDDMVGGEAPARANRDSRDATLVRDDLLQEMLSPNSSCGSLLDGDASPESFTEDQDSSVESRPSARGLHHSSLPLDGNAQR
Protein: Ribose-5-phosphate isomerase (EC 5.3.1.6) (Phosphoriboisomerase) (P47968)
Organism: Mus musculus (Mouse)
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Transketolase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Transketolase-like protein 1
- Transketolase-like protein 2
- Ribokinase
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
- Phosphoglucomutase-1
- ribose-phosphate diphosphokinase
Sequence:
MQRPGPFSTLYGRVLAPLPGRAGGAASGGGGNNWGLSGSHVQLPGRAHSETRGDKGGSSAGGPAPSTMSKAEEAKKLASHTAVENHVKNNQVLGIGSGSTIVHAVQRIAERVKQENLDLICIPTSFQARQLILQYGLTLSDLDQHPEIDLAIDGADEVDAELNLIKGGGGCLTQEKIVAGYASRFIVIADFRKDSKNLGDRWHKGIPIEVIPMAYVPVSRAVAQKFGGEVELRMAVNKAGPVVTDNGNFILDWKFDRVHKWSEVNTAIKMTPGVVDTGLFINMAERVYFGMQDGSVNVREKPF