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P49025 (CTRO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Rho-interacting, serine/threonine-protein kinase 21
Gene names
Name:Cit
Synonyms:Crik
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2055 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. Probable 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 By similarity. Ref.1 Ref.2 Ref.5 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.2

Subunit structure

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

Subcellular location

Cytoplasm Ref.2.

Tissue specificity

A major signal was observed in testis and brain, but it was also detected in thymus, spleen, kidney, heart and lung. Ref.2 Ref.7

Developmental stage

Detected at E10.5 with highest expression in the developing central nervous system. After E16.5 expression decreases and at two weeks after birth is restricted to the proliferating neuronal precursor cells in the external germinal layer of the cerebellum and subventricular migratory stream. Ref.7

Disruption phenotype

Death before reaching adulthood, probably due to lethal epilepsy. Mice display severe defects in the olfactory bulbs, the hippocampus, and the cerebellum. These defects appear to result from impaired cytokinesis followed by the induction of apoptosis in specific neuroblast populations. Ref.7

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 AAC72822.1 differs from that shown. Reason: Frameshift at positions 396 and 408.

The sequence AAC72823.1 differs from that shown. Reason: Frameshift at positions 396 and 408.

The sequence AAH23775.1 differs from that shown. Reason: Frameshift at position 1011.

The sequence AAH51165.1 differs from that shown. Reason: Frameshift at position 1011.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P49025-1)

Also known as: CRIK;

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: P49025-2)

Also known as: CRIK-SK;

The sequence of this isoform differs from the canonical sequence as follows:
     467-494: MEQEMTRLHRRVSEVEAVLSQKEVELKA → VSISTAGLRPCSRILQSIYAEGSAGGHC
     495-2055: Missing.
Isoform 3 (identifier: P49025-3)

Also known as: Citron;

The sequence of this isoform differs from the canonical sequence as follows:
     1-458: Missing.
     459-466: DSQDKCHK → MLLGEEAM
Isoform 4 (identifier: P49025-4)

The sequence of this isoform differs from the canonical sequence as follows:
     693-735: Missing.
Isoform 5 (identifier: P49025-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1279-1279: K → KGLFSRRKEDPALPTQ
     1602-1602: A → AARDHTSSEHQPVWVE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20552055Citron Rho-interacting kinase
PRO_0000085909

Regions

Domain97 – 359263Protein kinase
Domain360 – 43071AGC-kinase C-terminal
Domain1469 – 1589121PH
Domain1617 – 1907291CNH
Nucleotide binding103 – 1119ATP By similarity
Zinc finger1388 – 143750Phorbol-ester/DAG-type
Region1132 – 1328197Interaction with Rho/Rac
Coiled coil441 – 1086646 Potential
Coiled coil1091 – 1247157 Potential
Coiled coil1275 – 132551 Potential
Motif1979 – 19846SH3-binding Potential
Compositional bias550 – 962413Glu-rich
Compositional bias1276 – 12794Poly-Lys

Sites

Active site2211Proton acceptor By similarity
Binding site1261ATP By similarity

Amino acid modifications

Modified residue4321Phosphoserine By similarity
Modified residue4391Phosphoserine By similarity
Modified residue4791Phosphoserine Ref.8
Modified residue12371Phosphotyrosine Ref.9
Modified residue15041Phosphotyrosine Ref.9
Modified residue16081Phosphoserine Ref.10
Modified residue17471N6-acetyllysine By similarity
Modified residue19991Phosphoserine By similarity
Modified residue20211Phosphoserine By similarity

Natural variations

Alternative sequence1 – 458458Missing in isoform 3.
VSP_012436
Alternative sequence459 – 4668DSQDKCHK → MLLGEEAM in isoform 3.
VSP_012437
Alternative sequence467 – 49428MEQEM…VELKA → VSISTAGLRPCSRILQSIYA EGSAGGHC in isoform 2.
VSP_012438
Alternative sequence495 – 20551561Missing in isoform 2.
VSP_012439
Alternative sequence693 – 73543Missing in isoform 4.
VSP_016093
Alternative sequence12791K → KGLFSRRKEDPALPTQ in isoform 5.
VSP_016094
Alternative sequence16021A → AARDHTSSEHQPVWVE in isoform 5.
VSP_016095

Experimental info

Mutagenesis1261K → A: Loss of phosphorylation. Ref.2
Sequence conflict781Q → R in BAE26199. Ref.3
Sequence conflict1821F → L in BAE26199. Ref.3
Sequence conflict2341E → H in BAE26199. Ref.3
Sequence conflict19451Missing in AAH51165. Ref.6

Sequences

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

Last modified November 8, 2005. Version 3.
Checksum: BDA9A12C14E12DF8

FASTA2,055235,389
        10         20         30         40         50         60 
MLKFKYGVRN PPEASASEPI ASRASRLNLF FQGKPPLMTQ QQMSALSREG MLDALFALFE 

        70         80         90        100        110        120 
ECSQPALMKM KHVSSFVQKY SDTIAELREL QPSARDFEVR SLVGCGHFAE VQVVREKATG 

       130        140        150        160        170        180 
DVYAMKIMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNNL YLVMEYQPGG 

       190        200        210        220        230        240 
DFLSLLNRYE DQLDESMIQF YLAELILAVH SVHQMGYVHR DIKPENILID RTGEIKLVDF 

       250        260        270        280        290        300 
GSAAKMNSNK VDAKLPIGTP DYMAPEVLTV MNEDRRGTYG LDCDWWSVGV VAYEMVYGKT 

       310        320        330        340        350        360 
PFTEGTSART FNNIMNFQRF LKFPDDPKVS SELLDLLQSL LCVQKERLKF EGLCCHPFFA 

       370        380        390        400        410        420 
RTDWNNIRNS PPPFVPTLKS DDDTSNFDEP EKNSWVSSSV CQLSPSGFSG EELPFVGFSY 

       430        440        450        460        470        480 
SKALGYLGRS ESVVSSLDSP AKVSSMEKKL LIKSKELQDS QDKCHKMEQE MTRLHRRVSE 

       490        500        510        520        530        540 
VEAVLSQKEV ELKASETQRS LLEQDLATYI TECSSLKRSL EQARMEVSQE DDKALQLLHD 

       550        560        570        580        590        600 
IREQSRKLQE IKEQEYQAQV EEMRLMMNQL EEDLVSARRR SDLYESELRE SRLAAEEFKR 

       610        620        630        640        650        660 
KANECQHKLM KAKDQGKPEV GEYSKLEKIN AEQQLKIQEL QEKLEKAVKA STEATELLQN 

       670        680        690        700        710        720 
IRQAKERAER ELEKLHNRED SSEGIKKKLV EAEERRHSLE NKVKRLETME RRENRLKDDI 

       730        740        750        760        770        780 
QTKSEQIQQM ADKILELEEK HREAQVSAQH LEVHLKQKEQ HYEEKIKVLD NQIKKDLADK 

       790        800        810        820        830        840 
ESLENMMQRH EEEAHEKGKI LSEQKAMINA MDSKIRSLEQ RIVELSEANK LAANSSLFTQ 

       850        860        870        880        890        900 
RNMKAQEEMI SELRQQKFYL ETQAGKLEAQ NRKLEEQLEK ISHQDHSDKS RLLELETRLR 

       910        920        930        940        950        960 
EVSLEHEEQK LELKRQLTEL QLSLQERESQ LTALQAARAA LESQLRQAKT ELEETTAEAE 

       970        980        990       1000       1010       1020 
EEIQALTAHR DEIQRKFDAL RNSCTVITDL EEQLNQLTED NAELNNQNFY LSKQLDEASG 

      1030       1040       1050       1060       1070       1080 
ANDEIVQLRS EVDHLRREIT EREMQLTSQK QTMEALKTTC TMLEEQVLDL EALNDELLEK 

      1090       1100       1110       1120       1130       1140 
ERQWEAWRSV LGDEKSQFEC RVRELQRMLD TEKQSRARAD QRITESRQVV ELAVKEHKAE 

      1150       1160       1170       1180       1190       1200 
ILALQQALKE QKLKAESLSD KLNDLEKKHA MLEMNARSLQ QKLETERELK QRLLEEQAKL 

      1210       1220       1230       1240       1250       1260 
QQQMDLQKNH IFRLTQGLQE ALDRADLLKT ERSDLEYQLE NIQVLYSHEK VKMEGTISQQ 

      1270       1280       1290       1300       1310       1320 
TKLIDFLQAK MDQPAKKKKV PLQYNELKLA LEKEKARCAE LEEALQKTRI ELRSAREEAA 

      1330       1340       1350       1360       1370       1380 
HRKATDHPHP STPATARQQI AMSAIVRSPE HQPSAMSLLA PPSSRRKESS TPEEFSRRLK 

      1390       1400       1410       1420       1430       1440 
ERMHHNIPHR FNVGLNMRAT KCAVCLDTVH FGRQASKCLE CQVMCHPKCS TCLPATCGLP 

      1450       1460       1470       1480       1490       1500 
AEYATHFTEA FCRDKMNSPG LQSKEPGSSL HLEGWMKVPR NNKRGQQGWD RKYIVLEGSK 

      1510       1520       1530       1540       1550       1560 
VLIYDNEARE AGQRPVEEFE LCLPDGDVSI HGAVGASELA NTAKADVPYI LKMESHPHTT 

      1570       1580       1590       1600       1610       1620 
CWPGRTLYLL APSFPDKQRW VTALESVVAG GRVSREKAEA DAKLLGNSLL KLEGDDRLDM 

      1630       1640       1650       1660       1670       1680 
NCTLPFSDQV VLVGTEEGLY ALNVLKNSLT HIPGIGAVFQ IYIIKDLEKL LMIAGEERAL 

      1690       1700       1710       1720       1730       1740 
CLVDVKKVKQ SLAQSHLPAQ PDVSPNIFEA VKGCHLFAAG KIENSLCICA AMPSKVVILR 

      1750       1760       1770       1780       1790       1800 
YNDNLSKYCI RKEIETSEPC SCIHFTNYSI LIGTNKFYEI DMKQYTLDEF LDKNDHSLAP 

      1810       1820       1830       1840       1850       1860 
AVFASSSNSF PVSIVQANSA GQREEYLLCF HEFGVFVDSY GRRSRTDDLK WSRLPLAFAY 

      1870       1880       1890       1900       1910       1920 
REPYLFVTHF NSLEVIEIQA RSSLGSPARA YLEIPNPRYL GPAISSGAIY LASSYQDKLR 

      1930       1940       1950       1960       1970       1980 
VICCKGNLVK ESGTEQHRVP STSRSSPNKR GPPTYNEHIT KRVASSPAPP EGPSHPREPS 

      1990       2000       2010       2020       2030       2040 
TPHRYRDREG RTELRRDKSP GRPLEREKSP GRMLSTRRER SPGRLFEDSS RGRLPAGAVR 

      2050 
TPLSQVNKVW DQSSV 

« Hide

Isoform 2 (CRIK-SK) [UniParc].

Checksum: E4AEAEA4C22D0051
Show »

FASTA49455,650
Isoform 3 (Citron) [UniParc].

Checksum: 7B7286C2305676DA
Show »

FASTA1,597183,449
Isoform 4 [UniParc].

Checksum: 50944A35251224E9
Show »

FASTA2,012230,083
Isoform 5 [UniParc].

Checksum: 996B21DE7CBF45AD
Show »

FASTA2,085238,846

References

« Hide 'large scale' references
[1]"A novel partner for the GTP-bound forms of rho and rac."
Madaule P., Furuyashiki T., Reid T., Ishizaki T., Watanabe G., Morii N., Narumiya S.
FEBS Lett. 377:243-248(1995) [PubMed: 8543060] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION.
Tissue: Brain.
[2]"Citron Rho-interacting kinase, a novel tissue-specific Ser/Thr kinase encompassing the Rho-Rac-binding protein Citron."
Di Cunto F., Calautti E., Hsiao J., Ong L., Topley G., Turco E., Dotto G.P.
J. Biol. Chem. 273:29706-29711(1998) [PubMed: 9792683] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-126.
Tissue: Keratinocyte.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Mammary gland.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 246-254, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Role of citron kinase as a target of the small GTPase Rho in cytokinesis."
Madaule P., Eda M., Watanabe N., Fujisawa K., Matsuoka T., Bito H., Ishizaki T., Narumiya S.
Nature 394:491-494(1998) [PubMed: 9697773] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 373-2055 (ISOFORM 4), FUNCTION.
Tissue: Brain.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 992-2055 (ISOFORM 5).
Strain: FVB/N.
Tissue: Mammary tumor.
[7]"Defective neurogenesis in citron kinase knockout mice by altered cytokinesis and massive apoptosis."
Di Cunto F., Imarisio S., Hirsch E., Broccoli V., Bulfone A., Migheli A., Atzori C., Turco E., Triolo R., Dotto G.P., Silengo L., Altruda F.
Neuron 28:115-127(2000) [PubMed: 11086988] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[8]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, MASS SPECTROMETRY.
Tissue: Brain.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1237 AND TYR-1504, MASS SPECTROMETRY.
Tissue: Brain.
[10]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1608, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39904 mRNA. Translation: AAC52341.1.
AF086823 mRNA. Translation: AAC72822.1. Frameshift.
AF086824 mRNA. Translation: AAC72823.1. Frameshift.
AK145037 mRNA. Translation: BAE26199.1.
AF070066 mRNA. Translation: AAC27933.1.
BC023775 mRNA. Translation: AAH23775.1. Frameshift.
BC051165 mRNA. Translation: AAH51165.1. Frameshift.
IPIIPI00406762.
IPI00474730.
IPI00655040.
IPI00655108.
IPI00956788.
PIRS68420.
UniGeneMm.426282.
Mm.8321.

3D structure databases

ProteinModelPortalP49025.
SMRP49025. Positions 44-423, 1389-1437, 1471-1587.
ModBaseSearch...

Protein-protein interaction databases

IntActP49025. 5 interactions.
STRINGP49025.

PTM databases

PhosphoSiteP49025.

Proteomic databases

PRIDEP49025.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCuc008zep.1. mouse.
uc008zet.1. mouse.

Organism-specific databases

MGIMGI:105313. Cit.

Phylogenomic databases

eggNOGroNOG11544.
GeneTreeENSGT00600000084128.
HOVERGENHBG071093.
OrthoDBEOG402WR8.
PhylomeDBP49025.

Gene expression databases

ArrayExpressP49025.
BgeeP49025.
CleanExMM_CIT.
GenevestigatorP49025.
GermOnlineENSMUSG00000029516. Mus musculus.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR001180. Citron.
IPR017405. Citron_Rho-interacting_kinase.
IPR011009. Kinase-like_dom.
IPR011993. PH_type.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 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. Kinase_like. 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

SOURCESearch...

Entry information

Entry nameCTRO_MOUSE
AccessionPrimary (citable) accession number: P49025
Secondary accession number(s): O88528 expand/collapse secondary AC list , O88937, O88938, Q3UM99, Q8CIJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 8, 2005
Last modified: November 16, 2011
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families