O14578 (CTRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Citron Rho-interacting kinase
Short name=CRIK
EC=2.7.11.1

Alternative name(s):
Serine/threonine-protein kinase 21

Gene names

Name:	CIT
Synonyms:	CRIK, KIAA0949, STK21

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2027 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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. Ref.7 Ref.8 Ref.15
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Directly interacts with KIF14 depending on the activation state (stronger interaction with the kinase-dead form). Homodimer By similarity. Interacts with TTC3. Ref.7 Ref.9
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 CNH domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.
Sequence caution	The sequence BAA76793.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil SH3-binding Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle cytokinesis Inferred from mutant phenotype Ref.8. Source: UniProtKB dendrite development Inferred from electronic annotation. Source: Compara generation of neurons Inferred from sequence or structural similarity PubMed 11086988. Source: UniProtKB intracellular signal transduction Inferred from electronic annotation. Source: InterPro mitosis Inferred from sequence or structural similarity PubMed 11086988. Source: UniProtKB mitotic metaphase/anaphase transition Inferred from electronic annotation. Source: Compara mitotic sister chromatid segregation Inferred from electronic annotation. Source: Compara negative regulation of dendrite morphogenesis Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	actin cytoskeleton Inferred from electronic annotation. Source: Compara ruffle Inferred from electronic annotation. Source: Compara vacuole Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from sequence or structural similarity PubMed 9792683. Source: UniProtKB small GTPase regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14578-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O14578-2)

Also known as: Short; CRIK-SK;

The sequence of this isoform differs from the canonical sequence as follows:
     481-482: EV → GG
     483-2027: Missing.

Isoform 3 (identifier: O14578-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-467: Missing.
     1239-1253: Missing.
     1919-1919: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: O14578-4)

The sequence of this isoform differs from the canonical sequence as follows:
     694-694: E → EERRHSLENKVKRLETMERRENRLKDDIQTKSQQIQQMADKIL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2027	2027	Citron Rho-interacting kinase		PRO_0000085908
Regions
	Domain	97 – 360	264	Protein kinase
	Domain	361 – 431	71	AGC-kinase C-terminal
	Domain	1443 – 1563	121	PH
	Domain	1591 – 1881	291	CNH
	Nucleotide binding	103 – 111	9	ATP By similarity
	Zinc finger	1362 – 1411	50	Phorbol-ester/DAG-type
	Region	1091 – 1302	212	Interaction with Rho/Rac
	Coiled coil	453 – 1297	845	Potential
	Motif	1953 – 1958	6	SH3-binding Potential
Sites
	Active site	221	1	Proton acceptor By similarity
	Binding site	126	1	ATP By similarity
Amino acid modifications
	Modified residue	433	1	Phosphoserine Ref.11
	Modified residue	440	1	Phosphoserine Ref.10 Ref.11 Ref.13 Ref.16
	Modified residue	480	1	Phosphoserine By similarity
	Modified residue	1196	1	Phosphotyrosine By similarity
	Modified residue	1478	1	Phosphotyrosine By similarity
	Modified residue	1582	1	Phosphoserine By similarity
	Modified residue	1721	1	N6-acetyllysine Ref.12
Natural variations
	Alternative sequence	1 – 467	467	Missing in isoform 3.		VSP_014507
	Alternative sequence	481 – 482	2	EV → GG in isoform 2.		VSP_012434
	Alternative sequence	483 – 2027	1545	Missing in isoform 2.		VSP_012435
	Alternative sequence	694	1	E → EERRHSLENKVKRLETMERR ENRLKDDIQTKSQQIQQMAD KIL in isoform 4.		VSP_043301
	Alternative sequence	1239 – 1253	15	Missing in isoform 3.		VSP_014508
	Alternative sequence	1919	1	Missing in isoform 3.		VSP_014509
	Natural variant	7	1	G → E. Ref.17 Corresponds to variant rs36054900 [ dbSNP | Ensembl ].		VAR_040417
	Natural variant	9	1	R → Q. Ref.17 Corresponds to variant rs56193743 [ dbSNP | Ensembl ].		VAR_040418
	Natural variant	183	1	L → F. Ref.17		VAR_040419
Experimental info
	Sequence conflict	12	1	L → S in AAP43922. Ref.2
	Sequence conflict	56	1	F → L in AAP43922. Ref.2
	Sequence conflict	218	1	V → L in AAP43922. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 6B1D8C3F661F357B	FASTA	2,027	231,431
	10 20 30 40 50 60 MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE 70 80 90 100 110 120 ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG 130 140 150 160 170 180 DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG 190 200 210 220 230 240 DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF 250 260 270 280 290 300 GSAAKMNSNK MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 310 320 330 340 350 360 SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF 370 380 390 400 410 420 SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFS GEELPFVGFS 430 440 450 460 470 480 YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS 490 500 510 520 530 540 EVEAVLSQKE VELKASETQR SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH 550 560 570 580 590 600 DIREQSRKLQ EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK 610 620 630 640 650 660 RKATECQHKL LKAKDQGKPE VGEYAKLEKI NAEQQLKIQE LQEKLEKAVK ASTEATELLQ 670 680 690 700 710 720 NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEELEEKH REAQVSAQHL EVHLKQKEQH 730 740 750 760 770 780 YEEKIKVLDN QIKKDLADKE TLENMMQRHE EEAHEKGKIL SEQKAMINAM DSKIRSLEQR 790 800 810 820 830 840 IVELSEANKL AANSSLFTQR NMKAQEEMIS ELRQQKFYLE TQAGKLEAQN RKLEEQLEKI 850 860 870 880 890 900 SHQDHSDKNR LLELETRLRE VSLEHEEQKL ELKRQLTELQ LSLQERESQL TALQAARAAL 910 920 930 940 950 960 ESQLRQAKTE LEETTAEAEE EIQALTAHRD EIQRKFDALR NSCTVITDLE EQLNQLTEDN 970 980 990 1000 1010 1020 AELNNQNFYL SKQLDEASGA NDEIVQLRSE VDHLRREITE REMQLTSQKQ TMEALKTTCT 1030 1040 1050 1060 1070 1080 MLEEQVMDLE ALNDELLEKE RQWEAWRSVL GDEKSQFECR VRELQRMLDT EKQSRARADQ 1090 1100 1110 1120 1130 1140 RITESRQVVE LAVKEHKAEI LALQQALKEQ KLKAESLSDK LNDLEKKHAM LEMNARSLQQ 1150 1160 1170 1180 1190 1200 KLETERELKQ RLLEEQAKLQ QQMDLQKNHI FRLTQGLQEA LDRADLLKTE RSDLEYQLEN 1210 1220 1230 1240 1250 1260 IQVLYSHEKV KMEGTISQQT KLIDFLQAKM DQPAKKKKGL FSRRKEDPAL PTQVPLQYNE 1270 1280 1290 1300 1310 1320 LKLALEKEKA RCAELEEALQ KTRIELRSAR EEAAHRKATD HPHPSTPATA RQQIAMSAIV 1330 1340 1350 1360 1370 1380 RSPEHQPSAM SLLAPPSSRR KESSTPEEFS RRLKERMHHN IPHRFNVGLN MRATKCAVCL 1390 1400 1410 1420 1430 1440 DTVHFGRQAS KCLECQVMCH PKCSTCLPAT CGLPAEYATH FTEAFCRDKM NSPGLQTKEP 1450 1460 1470 1480 1490 1500 SSSLHLEGWM KVPRNNKRGQ QGWDRKYIVL EGSKVLIYDN EAREAGQRPV EEFELCLPDG 1510 1520 1530 1540 1550 1560 DVSIHGAVGA SELANTAKAD VPYILKMESH PHTTCWPGRT LYLLAPSFPD KQRWVTALES 1570 1580 1590 1600 1610 1620 VVAGGRVSRE KAEADAKLLG NSLLKLEGDD RLDMNCTLPF SDQVVLVGTE EGLYALNVLK 1630 1640 1650 1660 1670 1680 NSLTHVPGIG AVFQIYIIKD LEKLLMIAGE ERALCLVDVK KVKQSLAQSH LPAQPDISPN 1690 1700 1710 1720 1730 1740 IFEAVKGCHL FGAGKIENGL CICAAMPSKV VILRYNENLS KYCIRKEIET SEPCSCIHFT 1750 1760 1770 1780 1790 1800 NYSILIGTNK FYEIDMKQYT LEEFLDKNDH SLAPAVFAAS SNSFPVSIVQ VNSAGQREEY 1810 1820 1830 1840 1850 1860 LLCFHEFGVF VDSYGRRSRT DDLKWSRLPL AFAYREPYLF VTHFNSLEVI EIQARSSAGT 1870 1880 1890 1900 1910 1920 PARAYLDIPN PRYLGPAISS GAIYLASSYQ DKLRVICCKG NLVKESGTEH HRGPSTSRSS 1930 1940 1950 1960 1970 1980 PNKRGPPTYN EHITKRVASS PAPPEGPSHP REPSTPHRYR EGRTELRRDK SPGRPLEREK 1990 2000 2010 2020 SPGRMLSTRR ERSPGRLFED SSRGRLPAGA VRTPLSQVNK VWDQSSV
	Isoform 2 (Short) (CRIK-SK) [UniParc]. Checksum: 7F23D62DD30DC0CE	FASTA	482	54,399
	10 20 30 40 50 60 MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE 70 80 90 100 110 120 ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG 130 140 150 160 170 180 DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG 190 200 210 220 230 240 DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF 250 260 270 280 290 300 GSAAKMNSNK MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 310 320 330 340 350 360 SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF 370 380 390 400 410 420 SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFS GEELPFVGFS 430 440 450 460 470 480 YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS GG
	Isoform 3 [UniParc]. Checksum: 309A4BA63CB1419D	FASTA	1,544	177,035
	10 20 30 40 50 60 MEQEMTRLHR RVSEVEAVLS QKEVELKASE TQRSLLEQDL ATYITECSSL KRSLEQARME 70 80 90 100 110 120 VSQEDDKALQ LLHDIREQSR KLQEIKEQEY QAQVEEMRLM MNQLEEDLVS ARRRSDLYES 130 140 150 160 170 180 ELRESRLAAE EFKRKATECQ HKLLKAKDQG KPEVGEYAKL EKINAEQQLK IQELQEKLEK 190 200 210 220 230 240 AVKASTEATE LLQNIRQAKE RAERELEKLQ NREDSSEGIR KKLVEAEELE EKHREAQVSA 250 260 270 280 290 300 QHLEVHLKQK EQHYEEKIKV LDNQIKKDLA DKETLENMMQ RHEEEAHEKG KILSEQKAMI 310 320 330 340 350 360 NAMDSKIRSL EQRIVELSEA NKLAANSSLF TQRNMKAQEE MISELRQQKF YLETQAGKLE 370 380 390 400 410 420 AQNRKLEEQL EKISHQDHSD KNRLLELETR LREVSLEHEE QKLELKRQLT ELQLSLQERE 430 440 450 460 470 480 SQLTALQAAR AALESQLRQA KTELEETTAE AEEEIQALTA HRDEIQRKFD ALRNSCTVIT 490 500 510 520 530 540 DLEEQLNQLT EDNAELNNQN FYLSKQLDEA SGANDEIVQL RSEVDHLRRE ITEREMQLTS 550 560 570 580 590 600 QKQTMEALKT TCTMLEEQVM DLEALNDELL EKERQWEAWR SVLGDEKSQF ECRVRELQRM 610 620 630 640 650 660 LDTEKQSRAR ADQRITESRQ VVELAVKEHK AEILALQQAL KEQKLKAESL SDKLNDLEKK 670 680 690 700 710 720 HAMLEMNARS LQQKLETERE LKQRLLEEQA KLQQQMDLQK NHIFRLTQGL QEALDRADLL 730 740 750 760 770 780 KTERSDLEYQ LENIQVLYSH EKVKMEGTIS QQTKLIDFLQ AKMDQPAKKK KVPLQYNELK 790 800 810 820 830 840 LALEKEKARC AELEEALQKT RIELRSAREE AAHRKATDHP HPSTPATARQ QIAMSAIVRS 850 860 870 880 890 900 PEHQPSAMSL LAPPSSRRKE SSTPEEFSRR LKERMHHNIP HRFNVGLNMR ATKCAVCLDT 910 920 930 940 950 960 VHFGRQASKC LECQVMCHPK CSTCLPATCG LPAEYATHFT EAFCRDKMNS PGLQTKEPSS 970 980 990 1000 1010 1020 SLHLEGWMKV PRNNKRGQQG WDRKYIVLEG SKVLIYDNEA REAGQRPVEE FELCLPDGDV 1030 1040 1050 1060 1070 1080 SIHGAVGASE LANTAKADVP YILKMESHPH TTCWPGRTLY LLAPSFPDKQ RWVTALESVV 1090 1100 1110 1120 1130 1140 AGGRVSREKA EADAKLLGNS LLKLEGDDRL DMNCTLPFSD QVVLVGTEEG LYALNVLKNS 1150 1160 1170 1180 1190 1200 LTHVPGIGAV FQIYIIKDLE KLLMIAGEER ALCLVDVKKV KQSLAQSHLP AQPDISPNIF 1210 1220 1230 1240 1250 1260 EAVKGCHLFG AGKIENGLCI CAAMPSKVVI LRYNENLSKY CIRKEIETSE PCSCIHFTNY 1270 1280 1290 1300 1310 1320 SILIGTNKFY EIDMKQYTLE EFLDKNDHSL APAVFAASSN SFPVSIVQVN SAGQREEYLL 1330 1340 1350 1360 1370 1380 CFHEFGVFVD SYGRRSRTDD LKWSRLPLAF AYREPYLFVT HFNSLEVIEI QARSSAGTPA 1390 1400 1410 1420 1430 1440 RAYLDIPNPR YLGPAISSGA IYLASSYQDK LRVICCKGNL VKESGTEHHR GPSTSRSPNK 1450 1460 1470 1480 1490 1500 RGPPTYNEHI TKRVASSPAP PEGPSHPREP STPHRYREGR TELRRDKSPG RPLEREKSPG 1510 1520 1530 1540 RMLSTRRERS PGRLFEDSSR GRLPAGAVRT PLSQVNKVWD QSSV
	Isoform 4 [UniParc]. Checksum: A491E1437044643D	FASTA	2,069	236,607
	10 20 30 40 50 60 MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE 70 80 90 100 110 120 ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG 130 140 150 160 170 180 DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG 190 200 210 220 230 240 DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF 250 260 270 280 290 300 GSAAKMNSNK MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 310 320 330 340 350 360 SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF 370 380 390 400 410 420 SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFS GEELPFVGFS 430 440 450 460 470 480 YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS 490 500 510 520 530 540 EVEAVLSQKE VELKASETQR SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH 550 560 570 580 590 600 DIREQSRKLQ EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK 610 620 630 640 650 660 RKATECQHKL LKAKDQGKPE VGEYAKLEKI NAEQQLKIQE LQEKLEKAVK ASTEATELLQ 670 680 690 700 710 720 NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEERRHSL ENKVKRLETM ERRENRLKDD 730 740 750 760 770 780 IQTKSQQIQQ MADKILELEE KHREAQVSAQ HLEVHLKQKE QHYEEKIKVL DNQIKKDLAD 790 800 810 820 830 840 KETLENMMQR HEEEAHEKGK ILSEQKAMIN AMDSKIRSLE QRIVELSEAN KLAANSSLFT 850 860 870 880 890 900 QRNMKAQEEM ISELRQQKFY LETQAGKLEA QNRKLEEQLE KISHQDHSDK NRLLELETRL 910 920 930 940 950 960 REVSLEHEEQ KLELKRQLTE LQLSLQERES QLTALQAARA ALESQLRQAK TELEETTAEA 970 980 990 1000 1010 1020 EEEIQALTAH RDEIQRKFDA LRNSCTVITD LEEQLNQLTE DNAELNNQNF YLSKQLDEAS 1030 1040 1050 1060 1070 1080 GANDEIVQLR SEVDHLRREI TEREMQLTSQ KQTMEALKTT CTMLEEQVMD LEALNDELLE 1090 1100 1110 1120 1130 1140 KERQWEAWRS VLGDEKSQFE CRVRELQRML DTEKQSRARA DQRITESRQV VELAVKEHKA 1150 1160 1170 1180 1190 1200 EILALQQALK EQKLKAESLS DKLNDLEKKH AMLEMNARSL QQKLETEREL KQRLLEEQAK 1210 1220 1230 1240 1250 1260 LQQQMDLQKN HIFRLTQGLQ EALDRADLLK TERSDLEYQL ENIQVLYSHE KVKMEGTISQ 1270 1280 1290 1300 1310 1320 QTKLIDFLQA KMDQPAKKKK GLFSRRKEDP ALPTQVPLQY NELKLALEKE KARCAELEEA 1330 1340 1350 1360 1370 1380 LQKTRIELRS AREEAAHRKA TDHPHPSTPA TARQQIAMSA IVRSPEHQPS AMSLLAPPSS 1390 1400 1410 1420 1430 1440 RRKESSTPEE FSRRLKERMH HNIPHRFNVG LNMRATKCAV CLDTVHFGRQ ASKCLECQVM 1450 1460 1470 1480 1490 1500 CHPKCSTCLP ATCGLPAEYA THFTEAFCRD KMNSPGLQTK EPSSSLHLEG WMKVPRNNKR 1510 1520 1530 1540 1550 1560 GQQGWDRKYI VLEGSKVLIY DNEAREAGQR PVEEFELCLP DGDVSIHGAV GASELANTAK 1570 1580 1590 1600 1610 1620 ADVPYILKME SHPHTTCWPG RTLYLLAPSF PDKQRWVTAL ESVVAGGRVS REKAEADAKL 1630 1640 1650 1660 1670 1680 LGNSLLKLEG DDRLDMNCTL PFSDQVVLVG TEEGLYALNV LKNSLTHVPG IGAVFQIYII 1690 1700 1710 1720 1730 1740 KDLEKLLMIA GEERALCLVD VKKVKQSLAQ SHLPAQPDIS PNIFEAVKGC HLFGAGKIEN 1750 1760 1770 1780 1790 1800 GLCICAAMPS KVVILRYNEN LSKYCIRKEI ETSEPCSCIH FTNYSILIGT NKFYEIDMKQ 1810 1820 1830 1840 1850 1860 YTLEEFLDKN DHSLAPAVFA ASSNSFPVSI VQVNSAGQRE EYLLCFHEFG VFVDSYGRRS 1870 1880 1890 1900 1910 1920 RTDDLKWSRL PLAFAYREPY LFVTHFNSLE VIEIQARSSA GTPARAYLDI PNPRYLGPAI 1930 1940 1950 1960 1970 1980 SSGAIYLASS YQDKLRVICC KGNLVKESGT EHHRGPSTSR SSPNKRGPPT YNEHITKRVA 1990 2000 2010 2020 2030 2040 SSPAPPEGPS HPREPSTPHR YREGRTELRR DKSPGRPLER EKSPGRMLST RRERSPGRLF 2050 2060 EDSSRGRLPA GAVRTPLSQV NKVWDQSSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Huang C.Q., Wu S.L., Shan Y.X., Liu S., Xiao P.J. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and characterizing a novel human CRIK-SK gene." Mao Y., Xie Y., Wu Q. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Evidence of association between bipolar disorder and Citron on chromosome 12q24." Lyons-Warren A., Chang J.J., Balkissoon R., Kamiya A., Garant M., Nurnberger J., Scheftner W., Reich T., McMahon F., Kelsoe J., Gershon E., Coryell W., Byerley W., Berrettini W., Depaulo R., McInnis M., Sawa A. Mol. Psychiatry 10:807-809(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[4]	"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[5]	Ohara O., Nagase T., Kikuno R. Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"KIF14 and citron kinase act together to promote efficient cytokinesis." Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A., Barr F.A. J. Cell Biol. 172:363-372(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KIF14.
[8]	"Dissecting the role of Rho-mediated signaling in contractile ring formation." Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T. Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"The Down syndrome critical region protein TTC3 inhibits neuronal differentiation via RhoA and Citron kinase." Berto G., Camera P., Fusco C., Imarisio S., Ambrogio C., Chiarle R., Silengo L., Di Cunto F. J. Cell Sci. 120:1859-1867(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TTC3.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-440, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1721, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase." Tan I., Lai J., Yong J., Li S.F., Leung T. FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MYL9/MLC2.
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, MASS SPECTROMETRY.
[17]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-7; GLN-9 AND PHE-183.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY257469 mRNA. Translation: AAP13528.1. AY209000 mRNA. Translation: AAP43922.1. AY681966 mRNA. Translation: AAV87216.1. AB023166 mRNA. Translation: BAA76793.2. Different initiation. AC002563 Genomic DNA. Translation: AAB71327.1. AC079317 Genomic DNA. No translation available. AC004813 Genomic DNA. No translation available.
IPI	IPI00022465. IPI00607850. IPI00719285. IPI00884041.
RefSeq	NP_001193928.1. NM_001206999.1. NP_009105.1. NM_007174.2.
UniGene	Hs.119594.
3D structure databases
ProteinModelPortal	O14578.
SMR	O14578. Positions 41-424, 1363-1411, 1445-1566.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000261833.
PTM databases
PhosphoSite	O14578.
Proteomic databases
PaxDb	O14578.
PRIDE	O14578.
Protocols and materials databases
DNASU	11113.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261833; ENSP00000261833; ENSG00000122966. ENST00000392521; ENSP00000376306; ENSG00000122966.
GeneID	11113.
KEGG	hsa:11113.
UCSC	uc001txh.2. human. uc001txi.2. human.
Organism-specific databases
CTD	11113.
GeneCards	GC12M120123.
HGNC	HGNC:1985. CIT.
HPA	HPA019082.
MIM	605629. gene.
neXtProt	NX_O14578.
PharmGKB	PA26522.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000015347.
HOVERGEN	HBG071093.
KO	K16308.
OMA	MKAKDQG.
OrthoDB	EOG402WR8.
PhylomeDB	O14578.
Gene expression databases
ArrayExpress	O14578.
Bgee	O14578.
CleanEx	HS_CIT.
Genevestigator	O14578.
GermOnline	ENSG00000122966. Homo sapiens.
Family and domain databases
Gene3D	2.30.29.30. 1 hit.
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. [Graphical view]
PANTHER	PTHR22988:SF1. PTHR22988:SF1. 1 hit.
Pfam	PF00780. CNH. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF038145. Citron_Rho-interacting_kinase. 1 hit.
SMART	SM00109. C1. 1 hit. SM00036. CNH. 1 hit. SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50219. CNH. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O14578.
ChEMBL	CHEMBL5579.
ChiTaRS	CIT. human.
GenomeRNAi	11113.
NextBio	42242.
SOURCE	Search...

Entry information

Entry name

CTRO_HUMAN

Accession

Primary (citable) accession number: O14578
Secondary accession number(s): Q2M5E1 , Q6XUH8, Q86UQ9, Q9UPZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 4, 2005
Last modified:	April 3, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.