CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000246
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Citron Rho-interacting kinase 
Protein Synonyms/Alias
 CRIK; Serine/threonine-protein kinase 21 
Gene Name
 CIT 
Gene Synonyms/Alias
 CRIK; KIAA0949; STK21 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71QPALMKIKHVSNFVRubiquitination[1]
95QELQPSAKDFEVRSLubiquitination[2]
236VDRTGHIKLVDFGSAubiquitination[1]
245VDFGSAAKMNSNKMVubiquitination[1]
323MNFQRFLKFPDDPKVubiquitination[1]
350CGQKERLKFEGLCCHubiquitination[1]
380PPFVPTLKSDDDTSNubiquitination[2]
1108LALQQALKEQKLKAEubiquitination[3]
1721RYNENLSKYCIRKEIacetylation[4]
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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] 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
 Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. 
Sequence Annotation
 DOMAIN 97 360 Protein kinase.
 DOMAIN 361 431 AGC-kinase C-terminal.
 DOMAIN 1443 1563 PH.
 DOMAIN 1591 1881 CNH.
 NP_BIND 103 111 ATP (By similarity).
 ZN_FING 1362 1411 Phorbol-ester/DAG-type.
 REGION 1091 1302 Interaction with Rho/Rac.
 MOTIF 1953 1958 SH3-binding (Potential).
 ACT_SITE 221 221 Proton acceptor (By similarity).
 BINDING 126 126 ATP (By similarity).
 MOD_RES 433 433 Phosphoserine.
 MOD_RES 440 440 Phosphoserine.
 MOD_RES 480 480 Phosphoserine (By similarity).
 MOD_RES 1196 1196 Phosphotyrosine (By similarity).
 MOD_RES 1478 1478 Phosphotyrosine (By similarity).
 MOD_RES 1582 1582 Phosphoserine (By similarity).
 MOD_RES 1721 1721 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Kinase; Metal-binding; Mitosis; Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; SH3-binding; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2027 AA 
Protein Sequence
MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE 60
ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG 120
DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG 180
DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF 240
GSAAKMNSNK MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 300
SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF 360
SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFS GEELPFVGFS 420
YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS 480
EVEAVLSQKE VELKASETQR SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH 540
DIREQSRKLQ EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK 600
RKATECQHKL LKAKDQGKPE VGEYAKLEKI NAEQQLKIQE LQEKLEKAVK ASTEATELLQ 660
NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEELEEKH REAQVSAQHL EVHLKQKEQH 720
YEEKIKVLDN QIKKDLADKE TLENMMQRHE EEAHEKGKIL SEQKAMINAM DSKIRSLEQR 780
IVELSEANKL AANSSLFTQR NMKAQEEMIS ELRQQKFYLE TQAGKLEAQN RKLEEQLEKI 840
SHQDHSDKNR LLELETRLRE VSLEHEEQKL ELKRQLTELQ LSLQERESQL TALQAARAAL 900
ESQLRQAKTE LEETTAEAEE EIQALTAHRD EIQRKFDALR NSCTVITDLE EQLNQLTEDN 960
AELNNQNFYL SKQLDEASGA NDEIVQLRSE VDHLRREITE REMQLTSQKQ TMEALKTTCT 1020
MLEEQVMDLE ALNDELLEKE RQWEAWRSVL GDEKSQFECR VRELQRMLDT EKQSRARADQ 1080
RITESRQVVE LAVKEHKAEI LALQQALKEQ KLKAESLSDK LNDLEKKHAM LEMNARSLQQ 1140
KLETERELKQ RLLEEQAKLQ QQMDLQKNHI FRLTQGLQEA LDRADLLKTE RSDLEYQLEN 1200
IQVLYSHEKV KMEGTISQQT KLIDFLQAKM DQPAKKKKGL FSRRKEDPAL PTQVPLQYNE 1260
LKLALEKEKA RCAELEEALQ KTRIELRSAR EEAAHRKATD HPHPSTPATA RQQIAMSAIV 1320
RSPEHQPSAM SLLAPPSSRR KESSTPEEFS RRLKERMHHN IPHRFNVGLN MRATKCAVCL 1380
DTVHFGRQAS KCLECQVMCH PKCSTCLPAT CGLPAEYATH FTEAFCRDKM NSPGLQTKEP 1440
SSSLHLEGWM KVPRNNKRGQ QGWDRKYIVL EGSKVLIYDN EAREAGQRPV EEFELCLPDG 1500
DVSIHGAVGA SELANTAKAD VPYILKMESH PHTTCWPGRT LYLLAPSFPD KQRWVTALES 1560
VVAGGRVSRE KAEADAKLLG NSLLKLEGDD RLDMNCTLPF SDQVVLVGTE EGLYALNVLK 1620
NSLTHVPGIG AVFQIYIIKD LEKLLMIAGE ERALCLVDVK KVKQSLAQSH LPAQPDISPN 1680
IFEAVKGCHL FGAGKIENGL CICAAMPSKV VILRYNENLS KYCIRKEIET SEPCSCIHFT 1740
NYSILIGTNK FYEIDMKQYT LEEFLDKNDH SLAPAVFAAS SNSFPVSIVQ VNSAGQREEY 1800
LLCFHEFGVF VDSYGRRSRT DDLKWSRLPL AFAYREPYLF VTHFNSLEVI EIQARSSAGT 1860
PARAYLDIPN PRYLGPAISS GAIYLASSYQ DKLRVICCKG NLVKESGTEH HRGPSTSRSS 1920
PNKRGPPTYN EHITKRVASS PAPPEGPSHP REPSTPHRYR EGRTELRRDK SPGRPLEREK 1980
SPGRMLSTRR ERSPGRLFED SSRGRLPAGA VRTPLSQVNK VWDQSSV 2027 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0001726; C:ruffle; IEA:Compara.
 GO:0005773; C:vacuole; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
 GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0016358; P:dendrite development; IEA:Compara.
 GO:0048699; P:generation of neurons; ISS:UniProtKB.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IEA:Compara.
 GO:0007067; P:mitosis; ISS:UniProtKB.
 GO:0000070; P:mitotic sister chromatid segregation; IEA:Compara.
 GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR001180; Citron.
 IPR017405; Citron_Rho-interacting_kinase.
 IPR011009; Kinase-like_dom.
 IPR011993; PH_like_dom.
 IPR017892; Pkinase_C.
 IPR001849; Pleckstrin_homology.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00780; CNH
 PF00069; Pkinase
 PF00433; Pkinase_C 
SMART
 SM00109; C1
 SM00036; CNH
 SM00233; PH
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS50219; CNH
 PS50003; PH_DOMAIN
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS