CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031989
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rho guanine nucleotide exchange factor 6 
Protein Synonyms/Alias
 cDNA FLJ50776, highly similar to Rho guanine nucleotide exchange factor 6 
Gene Name
 ARHGEF6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
103PLSPKAVKGFETAPLubiquitination[1]
255KPFMRLEKYVTLLQEubiquitination[1]
368SGFIYQGKIPIAGTVubiquitination[1]
431ASCSSLSKTSSSSCSubiquitination[1, 2, 3]
490ERMSYILKESSKSPKubiquitination[1]
511HKRKTERKPSEEEYVubiquitination[1]
534EEDAQILKVIEAYCTubiquitination[1]
555GHGSSTRKDSIPQVLubiquitination[1, 3]
568VLLPEEEKLIIEETRubiquitination[1, 3]
585GQTIMEEKSLVDTVYubiquitination[1]
595VDTVYALKDEVRELKubiquitination[1, 2, 3]
609KQENKRMKQCLEEELubiquitination[1, 3]
631KLVRRLLKQTDECIRubiquitination[1, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 649 AA 
Protein Sequence
MTENGSHQLI VKARFNFKQT NEDELSVCKG DIIYVTRVEE GGWWEGTLNG RTGWFPSNYV 60
REIKSSDGVS LLLPGLECNG AISAHHNLCL PGSKRPLSPK AVKGFETAPL TKNYYTVVLQ 120
NILDTEKEYA KELQSLLVTY LRPLQSNNNL STVEVTSLLG NFEEVCTFQQ TLCQALEECS 180
KFPENQHKVG GCLLSLMPHF KSMYLAYCAN HPSAVNVLTQ HSDELEQFME NQGASSPGIL 240
ILTTNLSKPF MRLEKYVTLL QELERHMEDT HPDHQDILKA IVAFKTLMGQ CQDLRKRKQL 300
ELQILSEPIQ AWEGEDIKNL GNVIFMSQVM VQYGACEEKE ERYLMLFSNV LIMLSASPRM 360
SGFIYQGKIP IAGTVVTRLD EIEGNDCTFE ITGNTVERIV VHCNNNQDFQ EWLEQLNRLI 420
RGPASCSSLS KTSSSSCSAH SSFSSTGQPR GPLEPPQIIK PWSLSCLRPA PPLRPSAALG 480
YKERMSYILK ESSKSPKTMK KFLHKRKTER KPSEEEYVIR KSTAALEEDA QILKVIEAYC 540
TSANFQQGHG SSTRKDSIPQ VLLPEEEKLI IEETRSNGQT IMEEKSLVDT VYALKDEVRE 600
LKQENKRMKQ CLEEELKSRR DLEKLVRRLL KQTDECIRGE SSSKTSILP 649 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
 GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. 
Interpro
 IPR000219; DH-domain.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR011511; SH3_2.
 IPR001452; SH3_domain. 
Pfam
 PF00169; PH
 PF00621; RhoGEF
 PF07653; SH3_2 
SMART
 SM00233; PH
 SM00325; RhoGEF
 SM00326; SH3 
PROSITE
 PS50010; DH_2
 PS50003; PH_DOMAIN
 PS50002; SH3 
PRINTS
 PR00452; SH3DOMAIN.