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O14578

- CTRO_HUMAN

UniProt

O14578 - CTRO_HUMAN

Protein

Citron Rho-interacting kinase

Gene

CIT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    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/MLC2.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261ATPPROSITE-ProRule annotation
    Active sitei221 – 2211Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi103 – 1119ATPPROSITE-ProRule annotation
    Zinc fingeri1362 – 141150Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. PDZ domain binding Source: UniProt
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. small GTPase regulator activity Source: InterPro

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. dendrite development Source: Ensembl
    3. G2/M transition of mitotic cell cycle Source: Ensembl
    4. generation of neurons Source: UniProtKB
    5. Golgi organization Source: Ensembl
    6. intracellular signal transduction Source: InterPro
    7. metaphase/anaphase transition of mitotic cell cycle Source: Ensembl
    8. mitotic nuclear division Source: UniProtKB
    9. mitotic sister chromatid segregation Source: Ensembl
    10. negative regulation of dendrite morphogenesis Source: Ensembl
    11. regulation of actin polymerization or depolymerization Source: Ensembl
    12. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO14578.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citron Rho-interacting kinase (EC:2.7.11.1)
    Short name:
    CRIK
    Alternative name(s):
    Serine/threonine-protein kinase 21
    Gene namesi
    Name:CIT
    Synonyms:CRIK, KIAA0949, STK21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1985. CIT.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. Golgi cisterna Source: Ensembl
    3. membrane Source: UniProtKB
    4. neuronal cell body Source: Ensembl
    5. plasma membrane Source: Ensembl
    6. ruffle Source: Ensembl
    7. vacuole Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26522.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20272027Citron Rho-interacting kinasePRO_0000085908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei433 – 4331Phosphoserine1 Publication
    Modified residuei440 – 4401Phosphoserine4 Publications
    Modified residuei480 – 4801PhosphoserineBy similarity
    Modified residuei1196 – 11961PhosphotyrosineBy similarity
    Modified residuei1721 – 17211N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14578.
    PaxDbiO14578.
    PRIDEiO14578.

    PTM databases

    PhosphoSiteiO14578.

    Expressioni

    Gene expression databases

    ArrayExpressiO14578.
    BgeeiO14578.
    CleanExiHS_CIT.
    GenevestigatoriO14578.

    Organism-specific databases

    HPAiHPA019082.

    Interactioni

    Subunit structurei

    Directly interacts with KIF14 depending on the activation state (stronger interaction with the kinase-dead form). Homodimer By similarity. Interacts with TTC3.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi116290. 14 interactions.
    IntActiO14578. 1 interaction.
    MINTiMINT-2795177.
    STRINGi9606.ENSP00000261833.

    Structurei

    3D structure databases

    ProteinModelPortaliO14578.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 360264Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini361 – 43171AGC-kinase C-terminalAdd
    BLAST
    Domaini1443 – 1563121PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini1591 – 1881291CNHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1091 – 1302212Interaction with Rho/RacAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili453 – 1297845Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1953 – 19586SH3-bindingSequence Analysis

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 CNH domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1362 – 141150Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, SH3-binding, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000015347.
    HOVERGENiHBG071093.
    KOiK16308.
    OMAiMKAKDQG.
    OrthoDBiEOG7P8P6X.
    PhylomeDBiO14578.
    TreeFamiTF101140.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR001180. Citron.
    IPR017405. Citron_Rho-interacting_kinase.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00780. CNH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038145. Citron_Rho-interacting_kinase. 1 hit.
    SMARTiSM00109. C1. 1 hit.
    SM00036. CNH. 1 hit.
    SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14578-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG     50
    ILDALFVLFE ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR 100
    SLVGCGHFAE VQVVREKATG DIYAMKVMKK KALLAQEQVS FFEEERNILS 150
    RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG DLLSLLNRYE DQLDENLIQF 200
    YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF GSAAKMNSNK 250
    MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 300
    SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK 350
    FEGLCCHPFF SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS 400
    PCQLSPSGFS GEELPFVGFS YSKALGILGR SESVVSGLDS PAKTSSMEKK 450
    LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS EVEAVLSQKE VELKASETQR 500
    SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH DIREQSRKLQ 550
    EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK 600
    RKATECQHKL LKAKDQGKPE VGEYAKLEKI NAEQQLKIQE LQEKLEKAVK 650
    ASTEATELLQ NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEELEEKH 700
    REAQVSAQHL EVHLKQKEQH YEEKIKVLDN QIKKDLADKE TLENMMQRHE 750
    EEAHEKGKIL SEQKAMINAM DSKIRSLEQR IVELSEANKL AANSSLFTQR 800
    NMKAQEEMIS ELRQQKFYLE TQAGKLEAQN RKLEEQLEKI SHQDHSDKNR 850
    LLELETRLRE VSLEHEEQKL ELKRQLTELQ LSLQERESQL TALQAARAAL 900
    ESQLRQAKTE LEETTAEAEE EIQALTAHRD EIQRKFDALR NSCTVITDLE 950
    EQLNQLTEDN AELNNQNFYL SKQLDEASGA NDEIVQLRSE VDHLRREITE 1000
    REMQLTSQKQ TMEALKTTCT MLEEQVMDLE ALNDELLEKE RQWEAWRSVL 1050
    GDEKSQFECR VRELQRMLDT EKQSRARADQ RITESRQVVE LAVKEHKAEI 1100
    LALQQALKEQ KLKAESLSDK LNDLEKKHAM LEMNARSLQQ KLETERELKQ 1150
    RLLEEQAKLQ QQMDLQKNHI FRLTQGLQEA LDRADLLKTE RSDLEYQLEN 1200
    IQVLYSHEKV KMEGTISQQT KLIDFLQAKM DQPAKKKKGL FSRRKEDPAL 1250
    PTQVPLQYNE LKLALEKEKA RCAELEEALQ KTRIELRSAR EEAAHRKATD 1300
    HPHPSTPATA RQQIAMSAIV RSPEHQPSAM SLLAPPSSRR KESSTPEEFS 1350
    RRLKERMHHN IPHRFNVGLN MRATKCAVCL DTVHFGRQAS KCLECQVMCH 1400
    PKCSTCLPAT CGLPAEYATH FTEAFCRDKM NSPGLQTKEP SSSLHLEGWM 1450
    KVPRNNKRGQ QGWDRKYIVL EGSKVLIYDN EAREAGQRPV EEFELCLPDG 1500
    DVSIHGAVGA SELANTAKAD VPYILKMESH PHTTCWPGRT LYLLAPSFPD 1550
    KQRWVTALES VVAGGRVSRE KAEADAKLLG NSLLKLEGDD RLDMNCTLPF 1600
    SDQVVLVGTE EGLYALNVLK NSLTHVPGIG AVFQIYIIKD LEKLLMIAGE 1650
    ERALCLVDVK KVKQSLAQSH LPAQPDISPN IFEAVKGCHL FGAGKIENGL 1700
    CICAAMPSKV VILRYNENLS KYCIRKEIET SEPCSCIHFT NYSILIGTNK 1750
    FYEIDMKQYT LEEFLDKNDH SLAPAVFAAS SNSFPVSIVQ VNSAGQREEY 1800
    LLCFHEFGVF VDSYGRRSRT DDLKWSRLPL AFAYREPYLF VTHFNSLEVI 1850
    EIQARSSAGT PARAYLDIPN PRYLGPAISS GAIYLASSYQ DKLRVICCKG 1900
    NLVKESGTEH HRGPSTSRSS PNKRGPPTYN EHITKRVASS PAPPEGPSHP 1950
    REPSTPHRYR EGRTELRRDK SPGRPLEREK SPGRMLSTRR ERSPGRLFED 2000
    SSRGRLPAGA VRTPLSQVNK VWDQSSV 2027
    Length:2,027
    Mass (Da):231,431
    Last modified:January 4, 2005 - v2
    Checksum:i6B1D8C3F661F357B
    GO
    Isoform 2 (identifier: O14578-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:482
    Mass (Da):54,399
    Checksum:i7F23D62DD30DC0CE
    GO
    Isoform 3 (identifier: O14578-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,544
    Mass (Da):177,035
    Checksum:i309A4BA63CB1419D
    GO
    Isoform 4 (identifier: O14578-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,069
    Mass (Da):236,607
    Checksum:iA491E1437044643D
    GO

    Sequence cautioni

    The sequence BAA76793.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121L → S in AAP43922. 1 PublicationCurated
    Sequence conflicti56 – 561F → L in AAP43922. 1 PublicationCurated
    Sequence conflicti218 – 2181V → L in AAP43922. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71G → E.1 Publication
    Corresponds to variant rs36054900 [ dbSNP | Ensembl ].
    VAR_040417
    Natural varianti9 – 91R → Q.1 Publication
    Corresponds to variant rs56193743 [ dbSNP | Ensembl ].
    VAR_040418
    Natural varianti183 – 1831L → F.1 Publication
    VAR_040419

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 467467Missing in isoform 3. 1 PublicationVSP_014507Add
    BLAST
    Alternative sequencei481 – 4822EV → GG in isoform 2. 1 PublicationVSP_012434
    Alternative sequencei483 – 20271545Missing in isoform 2. 1 PublicationVSP_012435Add
    BLAST
    Alternative sequencei694 – 6941E → EERRHSLENKVKRLETMERR ENRLKDDIQTKSQQIQQMAD KIL in isoform 4. 1 PublicationVSP_043301
    Alternative sequencei1239 – 125315Missing in isoform 3. 1 PublicationVSP_014508Add
    BLAST
    Alternative sequencei1919 – 19191Missing in isoform 3. 1 PublicationVSP_014509

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS55891.1. [O14578-4]
    CCDS9192.1. [O14578-1]
    RefSeqiNP_001193928.1. NM_001206999.1. [O14578-4]
    NP_009105.1. NM_007174.2. [O14578-1]
    UniGeneiHs.119594.

    Genome annotation databases

    EnsembliENST00000261833; ENSP00000261833; ENSG00000122966. [O14578-1]
    ENST00000392521; ENSP00000376306; ENSG00000122966. [O14578-4]
    GeneIDi11113.
    KEGGihsa:11113.
    UCSCiuc001txh.2. human. [O14578-3]
    uc001txi.2. human. [O14578-1]
    uc001txj.2. human. [O14578-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS55891.1. [O14578-4 ]
    CCDS9192.1. [O14578-1 ]
    RefSeqi NP_001193928.1. NM_001206999.1. [O14578-4 ]
    NP_009105.1. NM_007174.2. [O14578-1 ]
    UniGenei Hs.119594.

    3D structure databases

    ProteinModelPortali O14578.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116290. 14 interactions.
    IntActi O14578. 1 interaction.
    MINTi MINT-2795177.
    STRINGi 9606.ENSP00000261833.

    Chemistry

    BindingDBi O14578.
    ChEMBLi CHEMBL5579.
    GuidetoPHARMACOLOGYi 1509.

    PTM databases

    PhosphoSitei O14578.

    Proteomic databases

    MaxQBi O14578.
    PaxDbi O14578.
    PRIDEi O14578.

    Protocols and materials databases

    DNASUi 11113.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261833 ; ENSP00000261833 ; ENSG00000122966 . [O14578-1 ]
    ENST00000392521 ; ENSP00000376306 ; ENSG00000122966 . [O14578-4 ]
    GeneIDi 11113.
    KEGGi hsa:11113.
    UCSCi uc001txh.2. human. [O14578-3 ]
    uc001txi.2. human. [O14578-1 ]
    uc001txj.2. human. [O14578-4 ]

    Organism-specific databases

    CTDi 11113.
    GeneCardsi GC12M120123.
    HGNCi HGNC:1985. CIT.
    HPAi HPA019082.
    MIMi 605629. gene.
    neXtProti NX_O14578.
    PharmGKBi PA26522.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000015347.
    HOVERGENi HBG071093.
    KOi K16308.
    OMAi MKAKDQG.
    OrthoDBi EOG7P8P6X.
    PhylomeDBi O14578.
    TreeFami TF101140.

    Enzyme and pathway databases

    SignaLinki O14578.

    Miscellaneous databases

    ChiTaRSi CIT. human.
    GeneWikii CIT_(gene).
    GenomeRNAii 11113.
    NextBioi 42242.
    PROi O14578.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14578.
    Bgeei O14578.
    CleanExi HS_CIT.
    Genevestigatori O14578.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR001180. Citron.
    IPR017405. Citron_Rho-interacting_kinase.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00780. CNH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038145. Citron_Rho-interacting_kinase. 1 hit.
    SMARTi 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 ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiCTRO_HUMAN
    AccessioniPrimary (citable) accession number: O14578
    Secondary accession number(s): Q2M5E1
    , Q6XUH8, Q86UQ9, Q9UPZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3