Search Results

Overview

Uniprot ID	O14578
Protein Name	Citron Rho-interacting kinase
Gene Name	CIT
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
1935	TYNEHITKRVASSPA
443	SGLDSPAKTSSMEKK
689	SSEGIRKKLVEAEEL

Function

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. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2

Protein Sequence

10 MLKFKYGARN 20 PLDAGAAEPI 30 ASRASRLNLF 40 FQGKPPFMTQ 50 QQMSPLSREG 60 ILDALFVLFE 70 ECSQPALMKI 80 KHVSNFVRKY 90 SDTIAELQEL 100 QPSAKDFEVR 110 SLVGCGHFAE 120 VQVVREKATG 130 DIYAMKVMKK 140 KALLAQEQVS 150 FFEEERNILS 160 RSTSPWIPQL 170 QYAFQDKNHL 180 YLVMEYQPGG 190 DLLSLLNRYE 200 DQLDENLIQF 210 YLAELILAVH 220 SVHLMGYVHR 230 DIKPENILVD 240 RTGHIKLVDF 250 GSAAKMNSNK 260 MVNAKLPIGT 270 PDYMAPEVLT 280 VMNGDGKGTY 290 GLDCDWWSVG 300 VIAYEMIYGR 310 SPFAEGTSAR 320 TFNNIMNFQR 330 FLKFPDDPKV 340 SSDFLDLIQS 350 LLCGQKERLK 360 FEGLCCHPFF 370 SKIDWNNIRN 380 SPPPFVPTLK 390 SDDDTSNFDE 400 PEKNSWVSSS 410 PCQLSPSGFS 420 GEELPFVGFS 430 YSKALGILGR 440 SESVVSGLDS 450 PAKTSSMEKK 460 LLIKSKELQD 470 SQDKCHKMEQ 480 EMTRLHRRVS 490 EVEAVLSQKE 500 VELKASETQR 510 SLLEQDLATY 520 ITECSSLKRS 530 LEQARMEVSQ 540 EDDKALQLLH 550 DIREQSRKLQ 560 EIKEQEYQAQ 570 VEEMRLMMNQ 580 LEEDLVSARR 590 RSDLYESELR 600 ESRLAAEEFK 610 RKATECQHKL 620 LKAKDQGKPE 630 VGEYAKLEKI 640 NAEQQLKIQE 650 LQEKLEKAVK 660 ASTEATELLQ 670 NIRQAKERAE 680 RELEKLQNRE 690 DSSEGIRKKL 700 VEAEELEEKH 710 REAQVSAQHL 720 EVHLKQKEQH 730 YEEKIKVLDN 740 QIKKDLADKE 750 TLENMMQRHE 760 EEAHEKGKIL 770 SEQKAMINAM 780 DSKIRSLEQR 790 IVELSEANKL 800 AANSSLFTQR 810 NMKAQEEMIS 820 ELRQQKFYLE 830 TQAGKLEAQN 840 RKLEEQLEKI 850 SHQDHSDKNR 860 LLELETRLRE 870 VSLEHEEQKL 880 ELKRQLTELQ 890 LSLQERESQL 900 TALQAARAAL 910 ESQLRQAKTE 920 LEETTAEAEE 930 EIQALTAHRD 940 EIQRKFDALR 950 NSCTVITDLE 960 EQLNQLTEDN 970 AELNNQNFYL 980 SKQLDEASGA 990 NDEIVQLRSE 1000 VDHLRREITE 1010 REMQLTSQKQ 1020 TMEALKTTCT 1030 MLEEQVMDLE 1040 ALNDELLEKE 1050 RQWEAWRSVL 1060 GDEKSQFECR 1070 VRELQRMLDT 1080 EKQSRARADQ 1090 RITESRQVVE 1100 LAVKEHKAEI 1110 LALQQALKEQ 1120 KLKAESLSDK 1130 LNDLEKKHAM 1140 LEMNARSLQQ 1150 KLETERELKQ 1160 RLLEEQAKLQ 1170 QQMDLQKNHI 1180 FRLTQGLQEA 1190 LDRADLLKTE 1200 RSDLEYQLEN 1210 IQVLYSHEKV 1220 KMEGTISQQT 1230 KLIDFLQAKM 1240 DQPAKKKKGL 1250 FSRRKEDPAL 1260 PTQVPLQYNE 1270 LKLALEKEKA 1280 RCAELEEALQ 1290 KTRIELRSAR 1300 EEAAHRKATD 1310 HPHPSTPATA 1320 RQQIAMSAIV 1330 RSPEHQPSAM 1340 SLLAPPSSRR 1350 KESSTPEEFS 1360 RRLKERMHHN 1370 IPHRFNVGLN 1380 MRATKCAVCL 1390 DTVHFGRQAS 1400 KCLECQVMCH 1410 PKCSTCLPAT 1420 CGLPAEYATH 1430 FTEAFCRDKM 1440 NSPGLQTKEP 1450 SSSLHLEGWM 1460 KVPRNNKRGQ 1470 QGWDRKYIVL 1480 EGSKVLIYDN 1490 EAREAGQRPV 1500 EEFELCLPDG 1510 DVSIHGAVGA 1520 SELANTAKAD 1530 VPYILKMESH 1540 PHTTCWPGRT 1550 LYLLAPSFPD 1560 KQRWVTALES 1570 VVAGGRVSRE 1580 KAEADAKLLG 1590 NSLLKLEGDD 1600 RLDMNCTLPF 1610 SDQVVLVGTE 1620 EGLYALNVLK 1630 NSLTHVPGIG 1640 AVFQIYIIKD 1650 LEKLLMIAGE 1660 ERALCLVDVK 1670 KVKQSLAQSH 1680 LPAQPDISPN 1690 IFEAVKGCHL 1700 FGAGKIENGL 1710 CICAAMPSKV 1720 VILRYNENLS 1730 KYCIRKEIET 1740 SEPCSCIHFT 1750 NYSILIGTNK 1760 FYEIDMKQYT 1770 LEEFLDKNDH 1780 SLAPAVFAAS 1790 SNSFPVSIVQ 1800 VNSAGQREEY 1810 LLCFHEFGVF 1820 VDSYGRRSRT 1830 DDLKWSRLPL 1840 AFAYREPYLF 1850 VTHFNSLEVI 1860 EIQARSSAGT 1870 PARAYLDIPN 1880 PRYLGPAISS 1890 GAIYLASSYQ 1900 DKLRVICCKG 1910 NLVKESGTEH 1920 HRGPSTSRSS 1930 PNKRGPPTYN 1940 EHITKRVASS 1950 PAPPEGPSHP 1960 REPSTPHRYR 1970 EGRTELRRDK 1980 SPGRPLEREK 1990 SPGRMLSTRR 2000 ERSPGRLFED 2010 SSRGRLPAGA 2020 VRTPLSQVNK VWDQSSV

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0016020	membrane
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0030165	PDZ domain binding
Molecular Function	GO:0019901	protein kinase binding
Molecular Function	GO:0106310	protein serine kinase activity
Molecular Function	GO:0004674	protein serine/threonine kinase activity
Molecular Function	GO:0030291	protein serine/threonine kinase inhibitor activity
Molecular Function	GO:0097110	scaffold protein binding
Molecular Function	GO:0017124	SH3 domain binding
Molecular Function	GO:0001223	transcription coactivator binding
Molecular Function	GO:0008270	zinc ion binding
Biological Process	GO:0048699	generation of neurons
Biological Process	GO:0000278	mitotic cell cycle
Biological Process	GO:0000281	mitotic cytokinesis
Biological Process	GO:0035331	negative regulation of hippo signaling
Biological Process	GO:0051402	neuron apoptotic process
Biological Process	GO:0032467	positive regulation of cytokinesis
Biological Process	GO:0032956	regulation of actin cytoskeleton organization

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.