CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012277
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dedicator of cytokinesis protein 1 
Protein Synonyms/Alias
 180 kDa protein downstream of CRK; DOCK180 
Gene Name
 DOCK1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
799RVKGAALKYLPTIVNubiquitination[1]
1054KRAKILNKYGDMRRQacetylation[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1. 
Sequence Annotation
 DOMAIN 9 70 SH3.
 DOMAIN 425 609 DHR-1.
 DOMAIN 1207 1617 DHR-2.
 REGION 1687 1695 Phosphoinositide-binding (Potential).
 REGION 1793 1819 Interaction with NCK2 second and third
 REGION 1820 1836 Interaction with NCK2 third SH3 domain
 REGION 1837 1852 Interaction with NCK2 (minor).
 MOTIF 1799 1805 SH3-binding; interaction with CRK
 MOTIF 1838 1843 SH3-binding; interaction with CRK
 MOD_RES 1751 1751 Phosphoserine.
 MOD_RES 1756 1756 Phosphoserine (By similarity).  
Keyword
 3D-structure; Apoptosis; Complete proteome; Cytoplasm; Guanine-nucleotide releasing factor; Membrane; Phagocytosis; Phosphoprotein; Polymorphism; Reference proteome; SH3 domain; SH3-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1865 AA 
Protein Sequence
MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT LRKKSKKGIF 60
PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWS TIWRQLYVQD NREMFRSVRH 120
MIYDLIEWRS QILSGTLPQD ELKELKKKVT AKIDYGNRIL DLDLVVRDED GNILDPELTS 180
TISLFRAHEI ASKQVEERLQ EEKSQKQNID INRQAKFAAT PSLALFVNLK NVVCKIGEDA 240
EVLMSLYDPV ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ 300
IVRVGRMELR DNNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQPVAGENDF 360
LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DIHQIRKEFP HLVDRTTAVA RKTGFPEIIM 420
PGDVRNDIYV TLVQGDFDKG SKTTAKNVEV TVSVYDEDGK RLEHVIFPGA GDEAISEYKS 480
VIYYQVKQPR WFETVKVAIP IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD 540
GTTLRDGEHD LIVYKAEAKK LEDAATYLSL PSTKAELEEK GHSATGKSMQ SLGSCTISKD 600
SFQISTLVCS TKLTQNVDLL GLLKWRSNTS LLQQNLRQLM KVDGGEVVKF LQDTLDALFN 660
IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET YIKKHFSATL AYTKLTKVLK 720
NYVDGAEKPG VNEQLYKAMK ALESIFKFIV RSRILFNQLY ENKGEADFVE SLLQLFRSIN 780
DMMSSMSDQT VRVKGAALKY LPTIVNDVKL VFDPKELSKM FTEFILNVPM GLLTIQKLYC 840
LIEIVHSDLF TQHDCREILL PMMTDQLKYH LERQEDLEAC CQLLSHILEV LYRKDVGPTQ 900
RHVQIIMEKL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL IKTFGKMRTD 960
VVDFLMETFI MFKNLIGKNV YPFDWVIMNM VQNKVFLRAI NQYADMLNKK FLDQANFELQ 1020
LWNNYFHLAV AFLTQESLQL ENFSSAKRAK ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF 1080
IPEMVGPILE MTLIPETELR KATIPIFFDM MQCEFHSTRS FQMFENEIIT KLDHEVEGGR 1140
GDEQYKVLFD KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMHD ENKENRMSCT 1200
VNVLNFYKEI EREEMYIRYL YKLCDLHKEC DNYTEAAYTL LLHAKLLKWS EDVCVAHLTQ 1260
RDGYQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL AEQYENEMFD YEQLSELLKK 1320
QAQFYENIVK VIRPKPDYFA VGYYGQGFPT FLRGKVFIYR GKEYERREDF EARLLTQFPN 1380
AEKMKTTSPP GDDIKNSPGQ YIQCFTVKPK LDLPPKFHRP VSEQIVSFYR VNEVQRFEYS 1440
RPIRKGEKNP DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT 1500
NDKINSMVQQ HLDDPSLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTDRY LQEHPEAHEK 1560
IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC FKQLKEKVEK EYGVRIMPSS 1620
LDDRRGSRPR SMVRSFTMPS SSRPLSVASV SSLSSDSTPS RPGSDGFALE PLLPKKMHSR 1680
SQDKLDKDDL EKEKKDKKKE KRNSKHQEIF EKEFKPTDIS LQQSEAVILS ETISPLRPQR 1740
PKSQVMNVIG SERRFSVSPS SPSSQQTPPP VTPRAKLSFS MQSSLELNGM TGADVADVPP 1800
PLPLKGSVAD YGNLMENQDL LGSPTPPPPP PHQRHLPPPL PSKTPPPPPP KTTRKQASVD 1860
SGIVQ 1865 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005096; F:GTPase activator activity; TAS:ProtInc.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; TAS:ProtInc.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0016477; P:cell migration; IEA:Compara.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc.
 GO:0006911; P:phagocytosis, engulfment; TAS:ProtInc.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc. 
Interpro
 IPR027007; DHR-1_domain.
 IPR027357; DHR-2.
 IPR026791; DOCK.
 IPR026799; DOCK_A.
 IPR010703; DOCK_C.
 IPR001452; SH3_domain. 
Pfam
 PF06920; Ded_cyto
 PF14429; DOCK-C2
 PF00018; SH3_1 
SMART
 SM00326; SH3 
PROSITE
 PS51650; DHR_1
 PS51651; DHR_2
 PS50002; SH3 
PRINTS