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O14578 (CTRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2027 AA.
Sequence statusComplete.
Protein existenceEvidence 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.16

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 processCell cycle
Cell division
Differentiation
Mitosis
Neurogenesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
SH3-binding
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

Golgi organization

Inferred from electronic annotation. Source: Ensembl

cytokinesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

dendrite development

Inferred from electronic annotation. Source: Ensembl

generation of neurons

Inferred from sequence or structural similarity PubMed 11086988. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

metaphase/anaphase transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

mitosis

Inferred from sequence or structural similarity PubMed 11086988. Source: UniProtKB

mitotic sister chromatid segregation

Inferred from electronic annotation. Source: Ensembl

negative regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of actin polymerization or depolymerization

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi cisterna

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: Ensembl

vacuole

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20272027Citron Rho-interacting kinase
PRO_0000085908

Regions

Domain97 – 360264Protein kinase
Domain361 – 43171AGC-kinase C-terminal
Domain1443 – 1563121PH
Domain1591 – 1881291CNH
Nucleotide binding103 – 1119ATP By similarity
Zinc finger1362 – 141150Phorbol-ester/DAG-type
Region1091 – 1302212Interaction with Rho/Rac
Coiled coil453 – 1297845 Potential
Motif1953 – 19586SH3-binding Potential

Sites

Active site2211Proton acceptor By similarity
Binding site1261ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.18
Modified residue4331Phosphoserine Ref.12
Modified residue4401Phosphoserine Ref.10 Ref.12 Ref.14 Ref.17
Modified residue4801Phosphoserine By similarity
Modified residue11961Phosphotyrosine By similarity
Modified residue17211N6-acetyllysine Ref.13

Natural variations

Alternative sequence1 – 467467Missing in isoform 3.
VSP_014507
Alternative sequence481 – 4822EV → GG in isoform 2.
VSP_012434
Alternative sequence483 – 20271545Missing in isoform 2.
VSP_012435
Alternative sequence6941E → EERRHSLENKVKRLETMERR ENRLKDDIQTKSQQIQQMAD KIL in isoform 4.
VSP_043301
Alternative sequence1239 – 125315Missing in isoform 3.
VSP_014508
Alternative sequence19191Missing in isoform 3.
VSP_014509
Natural variant71G → E. Ref.19
Corresponds to variant rs36054900 [ dbSNP | Ensembl ].
VAR_040417
Natural variant91R → Q. Ref.19
Corresponds to variant rs56193743 [ dbSNP | Ensembl ].
VAR_040418
Natural variant1831L → F. Ref.19
VAR_040419

Experimental info

Sequence conflict121L → S in AAP43922. Ref.2
Sequence conflict561F → L in AAP43922. Ref.2
Sequence conflict2181V → L in AAP43922. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 6B1D8C3F661F357B

FASTA2,027231,431
        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 

« Hide

Isoform 2 (Short) (CRIK-SK) [UniParc].

Checksum: 7F23D62DD30DC0CE
Show »

FASTA48254,399
Isoform 3 [UniParc].

Checksum: 309A4BA63CB1419D
Show »

FASTA1,544177,035
Isoform 4 [UniParc].

Checksum: A491E1437044643D
Show »

FASTA2,069236,607

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"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.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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. expand/collapse author list , 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.
RefSeqNP_001193928.1. NM_001206999.1.
NP_009105.1. NM_007174.2.
UniGeneHs.119594.

3D structure databases

ProteinModelPortalO14578.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116290. 13 interactions.
IntActO14578. 1 interaction.
MINTMINT-2795177.
STRING9606.ENSP00000261833.

Chemistry

BindingDBO14578.
ChEMBLCHEMBL5579.
GuidetoPHARMACOLOGY1509.

PTM databases

PhosphoSiteO14578.

Proteomic databases

PaxDbO14578.
PRIDEO14578.

Protocols and materials databases

DNASU11113.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261833; ENSP00000261833; ENSG00000122966. [O14578-1]
ENST00000392521; ENSP00000376306; ENSG00000122966. [O14578-4]
GeneID11113.
KEGGhsa:11113.
UCSCuc001txh.2. human. [O14578-3]
uc001txi.2. human. [O14578-1]
uc001txj.2. human. [O14578-4]

Organism-specific databases

CTD11113.
GeneCardsGC12M120123.
HGNCHGNC:1985. CIT.
HPAHPA019082.
MIM605629. gene.
neXtProtNX_O14578.
PharmGKBPA26522.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000015347.
HOVERGENHBG071093.
KOK16308.
OMAMKAKDQG.
OrthoDBEOG7P8P6X.
PhylomeDBO14578.
TreeFamTF101140.

Enzyme and pathway databases

SignaLinkO14578.

Gene expression databases

ArrayExpressO14578.
BgeeO14578.
CleanExHS_CIT.
GenevestigatorO14578.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR000961. 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020684. Rho-assoc_coiled-coil_kin.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR22988:SF3. PTHR22988:SF3. 1 hit.
PfamPF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF038145. Citron_Rho-interacting_kinase. 1 hit.
SMARTSM00109. C1. 1 hit.
SM00036. CNH. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSCIT. human.
GeneWikiCIT_(gene).
GenomeRNAi11113.
NextBio42242.
PROO14578.
SOURCESearch...

Entry information

Entry nameCTRO_HUMAN
AccessionPrimary (citable) accession number: O14578
Secondary accession number(s): Q2M5E1 expand/collapse secondary AC list , Q6XUH8, Q86UQ9, Q9UPZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM