SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O14578

- CTRO_HUMAN

UniProt

O14578 - CTRO_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Citron Rho-interacting kinase
Gene
CIT, CRIK, KIAA0949, STK21
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1261ATP By similarity
Active sitei221 – 2211Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi103 – 1119ATP By similarity
Zinc fingeri1362 – 141150Phorbol-ester/DAG-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Ensembl
  2. Golgi organization Source: Ensembl
  3. cytokinesis Source: UniProtKB
  4. dendrite development Source: Ensembl
  5. generation of neurons Source: UniProtKB
  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
Complete GO annotation...

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. Golgi cisterna Source: Ensembl
  2. actin cytoskeleton Source: Ensembl
  3. neuronal cell body Source: Ensembl
  4. plasma membrane Source: Ensembl
  5. ruffle Source: Ensembl
  6. vacuole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20272027Citron Rho-interacting kinase
PRO_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 – 4801Phosphoserine By similarity
Modified residuei1196 – 11961Phosphotyrosine By 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 TTC3.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliO14578.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 360264Protein kinase
Add
BLAST
Domaini361 – 43171AGC-kinase C-terminal
Add
BLAST
Domaini1443 – 1563121PH
Add
BLAST
Domaini1591 – 1881291CNH
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili453 – 1297845 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1953 – 19586SH3-binding Reviewed prediction

Sequence similaritiesi

Contains 1 CNH domain.
Contains 1 PH domain.

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.

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.
VSP_014507Add
BLAST
Alternative sequencei481 – 4822EV → GG in isoform 2.
VSP_012434
Alternative sequencei483 – 20271545Missing in isoform 2.
VSP_012435Add
BLAST
Alternative sequencei694 – 6941E → EERRHSLENKVKRLETMERR ENRLKDDIQTKSQQIQQMAD KIL in isoform 4.
VSP_043301
Alternative sequencei1239 – 125315Missing in isoform 3.
VSP_014508Add
BLAST
Alternative sequencei1919 – 19191Missing in isoform 3.
VSP_014509

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 134 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

Similar proteinsi