DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structure (London, England : 1993) 2013 imex curation Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. DIP original experiment: DIP-255868X Structure (London, England : 1993) 2013 IMEx Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structure (London, England : 1993) 2013 imex curation Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. DIP original experiment: DIP-255870X Structure (London, England : 1993) 2013 IMEx Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structure (London, England : 1993) 2013 imex curation Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. DIP original experiment: DIP-255869X Structure (London, England : 1993) 2013 IMEx Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structure (London, England : 1993) 2013 imex curation Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Raiola L., Lussier-Price M., Gagnon D., Lafrance-Vanasse J., Mascle X., Arseneault G., Legault P., Archambault J., Omichinski JG. DIP original experiment: DIP-255871X Structure (London, England : 1993) 2013 IMEx Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. klf1_human Krueppel-like factor 1 KLF1 EKLF Erythroid krueppel-like transcription factor protein protein human Homo sapiens Human MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRFARSDELTRHYRKHTGQRPFRCQLCPRAFSRSDHLALHMKRHL DIP protein Q13351 original sequence version: 107 DIP protein Q13351 original sequence version: 117 mint Binds to the CACCC box in the beta-globin gene promoter and activates transcription. Probably serves as a general switch factor for erythroid development 6E9A48A2B6A37C76 p36956-1 Sterol regulatory element-binding protein 1 SREBF1 BHLHD1 SREBP1 Class D basic helix-loop-helix protein 1 Sterol regulatory element-binding transcription factor 1 protein protein human Homo sapiens Human MDEPPFSEAALEQALGEPCDLDAALLTDIEDMLQLINNQDSDFPGLFDPPYAGSGAGGTDPASPDTSSPGSLSPPPATLSSSLEAFLSGPQAAPSPLSPPQPAPTPLKMYPSMPAFSPGPGIKEESVPLSILQTPTPQPLPGALLPQSFPAPAPPQFSSTPVLGYPSPPGGFSTGSPPGNTQQPLPGLPLASPPGVPPVSLHTQVQSVVPQQLLTVTAAPTAAPVTTTVTSQIQQVPVLLQPHFIKADSLLLTAMKTDGATVKAAGLSPLVSGTTVQTGPLPTLVSGGTILATVPLVVDAEKLPINRLAAGSKAPASAQSRGEKRTAHNAIEKRYRSSINDKIIELKDLVVGTEAKLNKSAVLRKAIDYIRFLQHSNQKLKQENLSLRTAVHKSKSLKDLVSACGSGGNTDVLMEGVKTEVEDTLTPPPSDAGSPFQSSPLSLGSRGSGSGGSGSDSEPDSPVFEDSKAKPEQRPSLHSRGMLDRSRLALCTLVFLCLSCNPLASLLGARGLPSPSDTTSVYHSPGRNVLGTESRDGPGWAQWLLPPVVWLLNGLLVLVSLVLLFVYGEPVTRPHSGPAVYFWRHRKQADLDLARGDFAQAAQQLWLALRALGRPLPTSHLDLACSLLWNLIRHLLQRLWVGRWLAGRAGGLQQDCALRVDASASARDAALVYHKLHQLHTMGKHTGGHLTATNLALSALNLAECAGDAVSVATLAEIYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGSVPPAMQWLCHPVGHRFFVDGDWSVLSTPWESLYSLAGNPVDPLAQVTQLFREHLLERALNCVTQPNPSPGSADGDKEFSDALGYLQLLNSCSDAAGAPAYSFSISSSMATTTGVDPVAKWWASLTAVVIHWLRRDEEAAERLCPLVEHLPRVLQESERPLPRAALHSFKAARALLGCAKAESGPASLTICEKASGYLQDSLATTPASSSIDKAVQLFLCDLLLVVRTSLWRQQQPPAPAPAAQGTSSRPQASALELRGFQRDLSSLRRLAQSFRPAMRRVFLHEATARLMAGASPTRTHQLLDRSLRRRAGPGGKGGAVAELEPRPTRREHAEALLLASCYLPPGFLSAPGQRVGMLAEAARTLEKLGDRRLLHDCQQMLMRLGGGTTVTSS DIP protein P36956-1 original sequence version: 150 DIP protein P36956-1 original sequence version: 91 DIP protein P36956 original sequence version: 151 58F28870739FF259 ubiq_human UBIQ_HUMAN protein protein human Homo sapiens Human MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG klf1-ub-1 1 5 unspecified role unspecified role unspecified role unspecified role Region 1-40 Region 1-40 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction srebf1-ub-1 3 6 unspecified role unspecified role unspecified role unspecified role Region 1-50 Region 1-50 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction klf1-ub-2 4 5 unspecified role unspecified role unspecified role unspecified role Region 1-40 Region 1-40 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 50-90 Region 50-90 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ile44ala I44A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I44A'. ecolx Escherichia coli direct interaction direct interaction klf1-ub-3 2 5 unspecified role unspecified role unspecified role unspecified role Region 1-40 Region 1-40 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 50-90 Region 50-90 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q13351:p.Phe27Ser F27S mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F S This feature has been corrected as a result of our quality control procedures. The original label was 'F27S'. Wed May 02 20:12:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe27ser' Tue Jun 30 19:31:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe27Ser' Q13351:p.Leu28Ser L28S mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L S This feature has been corrected as a result of our quality control procedures. The original label was 'L28S'. Wed May 02 18:27:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu28ser' Tue Jun 30 19:19:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu28Ser' Q13351:p.Trp31Ser W31S mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain W S This feature has been corrected as a result of our quality control procedures. The original label was 'W31S'. Wed May 02 14:36:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp31ser' Tue Jun 30 17:15:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp31Ser' ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction