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O14578

- CTRO_HUMAN

UniProt

O14578 - CTRO_HUMAN

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Protein

Citron Rho-interacting kinase

Gene

CIT

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 – 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
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. 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
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 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

BgeeiO14578.
CleanExiHS_CIT.
ExpressionAtlasiO14578. baseline and differential.
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.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000015347.
HOVERGENiHBG071093.
InParanoidiO14578.
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.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

        10         20         30         40         50
MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG
60 70 80 90 100
ILDALFVLFE ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR
110 120 130 140 150
SLVGCGHFAE VQVVREKATG DIYAMKVMKK KALLAQEQVS FFEEERNILS
160 170 180 190 200
RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG DLLSLLNRYE DQLDENLIQF
210 220 230 240 250
YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF GSAAKMNSNK
260 270 280 290 300
MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR
310 320 330 340 350
SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK
360 370 380 390 400
FEGLCCHPFF SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS
410 420 430 440 450
PCQLSPSGFS GEELPFVGFS YSKALGILGR SESVVSGLDS PAKTSSMEKK
460 470 480 490 500
LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS EVEAVLSQKE VELKASETQR
510 520 530 540 550
SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH DIREQSRKLQ
560 570 580 590 600
EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK
610 620 630 640 650
RKATECQHKL LKAKDQGKPE VGEYAKLEKI NAEQQLKIQE LQEKLEKAVK
660 670 680 690 700
ASTEATELLQ NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEELEEKH
710 720 730 740 750
REAQVSAQHL EVHLKQKEQH YEEKIKVLDN QIKKDLADKE TLENMMQRHE
760 770 780 790 800
EEAHEKGKIL SEQKAMINAM DSKIRSLEQR IVELSEANKL AANSSLFTQR
810 820 830 840 850
NMKAQEEMIS ELRQQKFYLE TQAGKLEAQN RKLEEQLEKI SHQDHSDKNR
860 870 880 890 900
LLELETRLRE VSLEHEEQKL ELKRQLTELQ LSLQERESQL TALQAARAAL
910 920 930 940 950
ESQLRQAKTE LEETTAEAEE EIQALTAHRD EIQRKFDALR NSCTVITDLE
960 970 980 990 1000
EQLNQLTEDN AELNNQNFYL SKQLDEASGA NDEIVQLRSE VDHLRREITE
1010 1020 1030 1040 1050
REMQLTSQKQ TMEALKTTCT MLEEQVMDLE ALNDELLEKE RQWEAWRSVL
1060 1070 1080 1090 1100
GDEKSQFECR VRELQRMLDT EKQSRARADQ RITESRQVVE LAVKEHKAEI
1110 1120 1130 1140 1150
LALQQALKEQ KLKAESLSDK LNDLEKKHAM LEMNARSLQQ KLETERELKQ
1160 1170 1180 1190 1200
RLLEEQAKLQ QQMDLQKNHI FRLTQGLQEA LDRADLLKTE RSDLEYQLEN
1210 1220 1230 1240 1250
IQVLYSHEKV KMEGTISQQT KLIDFLQAKM DQPAKKKKGL FSRRKEDPAL
1260 1270 1280 1290 1300
PTQVPLQYNE LKLALEKEKA RCAELEEALQ KTRIELRSAR EEAAHRKATD
1310 1320 1330 1340 1350
HPHPSTPATA RQQIAMSAIV RSPEHQPSAM SLLAPPSSRR KESSTPEEFS
1360 1370 1380 1390 1400
RRLKERMHHN IPHRFNVGLN MRATKCAVCL DTVHFGRQAS KCLECQVMCH
1410 1420 1430 1440 1450
PKCSTCLPAT CGLPAEYATH FTEAFCRDKM NSPGLQTKEP SSSLHLEGWM
1460 1470 1480 1490 1500
KVPRNNKRGQ QGWDRKYIVL EGSKVLIYDN EAREAGQRPV EEFELCLPDG
1510 1520 1530 1540 1550
DVSIHGAVGA SELANTAKAD VPYILKMESH PHTTCWPGRT LYLLAPSFPD
1560 1570 1580 1590 1600
KQRWVTALES VVAGGRVSRE KAEADAKLLG NSLLKLEGDD RLDMNCTLPF
1610 1620 1630 1640 1650
SDQVVLVGTE EGLYALNVLK NSLTHVPGIG AVFQIYIIKD LEKLLMIAGE
1660 1670 1680 1690 1700
ERALCLVDVK KVKQSLAQSH LPAQPDISPN IFEAVKGCHL FGAGKIENGL
1710 1720 1730 1740 1750
CICAAMPSKV VILRYNENLS KYCIRKEIET SEPCSCIHFT NYSILIGTNK
1760 1770 1780 1790 1800
FYEIDMKQYT LEEFLDKNDH SLAPAVFAAS SNSFPVSIVQ VNSAGQREEY
1810 1820 1830 1840 1850
LLCFHEFGVF VDSYGRRSRT DDLKWSRLPL AFAYREPYLF VTHFNSLEVI
1860 1870 1880 1890 1900
EIQARSSAGT PARAYLDIPN PRYLGPAISS GAIYLASSYQ DKLRVICCKG
1910 1920 1930 1940 1950
NLVKESGTEH HRGPSTSRSS PNKRGPPTYN EHITKRVASS PAPPEGPSHP
1960 1970 1980 1990 2000
REPSTPHRYR EGRTELRRDK SPGRPLEREK SPGRMLSTRR ERSPGRLFED
2010 2020
SSRGRLPAGA VRTPLSQVNK VWDQSSV
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]
ENST00000612548; ENSP00000482318; ENSG00000122966. [O14578-2]
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 ]
ENST00000612548 ; ENSP00000482318 ; ENSG00000122966 . [O14578-2 ]
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.
GeneTreei ENSGT00760000118994.
HOGENOMi HOG000015347.
HOVERGENi HBG071093.
InParanoidi O14578.
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

Bgeei O14578.
CleanExi HS_CIT.
ExpressionAtlasi O14578. baseline and differential.
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.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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: October 29, 2014
This is version 136 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