CTRO_MOUSE - dbPTM
CTRO_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTRO_MOUSE
UniProt AC P49025
Protein Name Citron Rho-interacting kinase
Gene Name Cit
Organism Mus musculus (Mouse).
Sequence Length 2055
Subcellular Localization Cytoplasm .
Protein Description 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. 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..
Protein Sequence MLKFKYGVRNPPEASASEPIASRASRLNLFFQGKPPLMTQQQMSALSREGMLDALFALFEECSQPALMKMKHVSSFVQKYSDTIAELRELQPSARDFEVRSLVGCGHFAEVQVVREKATGDVYAMKIMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNNLYLVMEYQPGGDFLSLLNRYEDQLDESMIQFYLAELILAVHSVHQMGYVHRDIKPENILIDRTGEIKLVDFGSAAKMNSNKVDAKLPIGTPDYMAPEVLTVMNEDRRGTYGLDCDWWSVGVVAYEMVYGKTPFTEGTSARTFNNIMNFQRFLKFPDDPKVSSELLDLLQSLLCVQKERLKFEGLCCHPFFARTDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSVCQLSPSGFSGEELPFVGFSYSKALGYLGRSESVVSSLDSPAKVSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQSKEPGSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHIPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDVSPNIFEAVKGCHLFAAGKIENSLCICAAMPSKVVILRYNDNLSKYCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLDEFLDKNDHSLAPAVFASSSNSFPVSIVQANSAGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSLGSPARAYLEIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEQHRVPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYRDREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MLKFKYGV
-------CCCCCCCC		40.73-
21 (in isoform 3)Phosphorylation-12.0429899451
28 (in isoform 3)Phosphorylation-33.4229899451
75PhosphorylationMKMKHVSSFVQKYSD
HHHHHHHHHHHHHHH		28.4829514104
126AcetylationTGDVYAMKIMKKKAL
CCCHHHHHHHHHHHH		31.3219852605
152PhosphorylationERNILSRSTSPWIPQ
HHCHHCCCCCCCHHH		29.8426745281
153PhosphorylationRNILSRSTSPWIPQL
HCHHCCCCCCCHHHH		37.3826745281
154PhosphorylationNILSRSTSPWIPQLQ
CHHCCCCCCCHHHHH		21.3426745281
242PhosphorylationIKLVDFGSAAKMNSN
EEEEECCCCCCCCCC		25.66-
248PhosphorylationGSAAKMNSNKVDAKL
CCCCCCCCCCCCCCC		34.23-
262PhosphorylationLPIGTPDYMAPEVLT
CCCCCCCCCCCEEEE		9.07-
330PhosphorylationFPDDPKVSSELLDLL
CCCCHHHCHHHHHHH		24.99-
331PhosphorylationPDDPKVSSELLDLLQ
CCCHHHCHHHHHHHH		34.94-
430PhosphorylationALGYLGRSESVVSSL
HHHCCCCCHHHHHCC		32.2125619855
432PhosphorylationGYLGRSESVVSSLDS
HCCCCCHHHHHCCCC		29.1225619855
435PhosphorylationGRSESVVSSLDSPAK
CCCHHHHHCCCCCCC		24.0325619855
436PhosphorylationRSESVVSSLDSPAKV
CCHHHHHCCCCCCCC		25.2825619855
439PhosphorylationSVVSSLDSPAKVSSM
HHHHCCCCCCCCCHH		31.8626824392
479PhosphorylationTRLHRRVSEVEAVLS
HHHHHHHHHHHHHHC		33.8325521595
515PhosphorylationTYITECSSLKRSLEQ
HHHHHHHHHHHHHHH		49.9529899451
528PhosphorylationEQARMEVSQEDDKAL
HHHHHHCCHHHHHHH		17.9729514104
581PhosphorylationLVSARRRSDLYESEL
HHHHHHHHHHHHHHH		30.1024899341
584PhosphorylationARRRSDLYESELRES
HHHHHHHHHHHHHHH		23.54-
681PhosphorylationKLHNREDSSEGIKKK
HHHCCCCCCHHHHHH		26.0729899451
698PhosphorylationEAEERRHSLENKVKR
HHHHHHHHHHHHHHH		35.2522324799
817PhosphorylationAMDSKIRSLEQRIVE
HHHHHHHHHHHHHHH		39.4726239621
836PhosphorylationNKLAANSSLFTQRNM
HHHHHCCCHHHHHHH		27.5829514104
890PhosphorylationHQDHSDKSRLLELET
CCCCCCHHHHHHHHH		32.9022807455
1030PhosphorylationDEIVQLRSEVDHLRR
HHHHHHHHHHHHHHH		51.0319854140
1126PhosphorylationADQRITESRQVVELA
HHHHHHHHHHHHHHH		21.2523684622
1149UbiquitinationLALQQALKEQKLKAE
HHHHHHHHHHCHHHH		62.20-
1230PhosphorylationDRADLLKTERSDLEY
HHHHHHHHHHHHHHH		36.2819060867
1233PhosphorylationDLLKTERSDLEYQLE
HHHHHHHHHHHHHHH		40.0729899451
1237PhosphorylationTERSDLEYQLENIQV
HHHHHHHHHHHHHEE		26.2020415495
1246PhosphorylationLENIQVLYSHEKVKM
HHHHEEEEECCCCCC		14.77-
1331PhosphorylationATDHPHPSTPATARQ
CCCCCCCCCCHHHHH		43.9429899451
1332PhosphorylationTDHPHPSTPATARQQ
CCCCCCCCCHHHHHH		22.7624899341
1343PhosphorylationARQQIAMSAIVRSPE
HHHHHHHHHHHCCCC		13.0626643407
1348PhosphorylationAMSAIVRSPEHQPSA
HHHHHHCCCCCCCCH		24.6022322096
1354PhosphorylationRSPEHQPSAMSLLAP
CCCCCCCCHHHHCCC		29.9922322096
1357PhosphorylationEHQPSAMSLLAPPSS
CCCCCHHHHCCCCCC		21.6822322096
1363PhosphorylationMSLLAPPSSRRKESS
HHHCCCCCCCCCCCC		35.1020415495
1364PhosphorylationSLLAPPSSRRKESST
HHCCCCCCCCCCCCC		41.7120415495
1369PhosphorylationPSSRRKESSTPEEFS
CCCCCCCCCCHHHHH		42.4125266776
1458PhosphorylationFCRDKMNSPGLQSKE
HHHHHCCCCCCCCCC		19.4925521595
1504PhosphorylationEGSKVLIYDNEAREA
ECCEEEEECHHHHHC		14.4618034455
1549PhosphorylationTAKADVPYILKMESH
HCCCCCCEEEECCCC		20.80-
1608PhosphorylationDAKLLGNSLLKLEGD
HHHHHCCCHHHCCCC		33.0326824392
1638 (in isoform 5)Phosphorylation-20.1129514104
1669UbiquitinationYIIKDLEKLLMIAGE
EEECCHHHHHHHHHC		54.97-
1747AcetylationRYNDNLSKYCIRKEI
EECCCHHHHHHHHHC		47.51-
1778PhosphorylationLIGTNKFYEIDMKQY
EEECCCCEEEECCCC		17.37-
1785PhosphorylationYEIDMKQYTLDEFLD
EEEECCCCCHHHHHC		12.07-
1886PhosphorylationQARSSLGSPARAYLE
EEHHCCCCCCCEEEE		22.2223737553
1891PhosphorylationLGSPARAYLEIPNPR
CCCCCCEEEECCCCC		10.18-
1910PhosphorylationAISSGAIYLASSYQD
CCCCCCEEEECCCCC		8.83-
1941PhosphorylationTEQHRVPSTSRSSPN
CCCCCCCCCCCCCCC		35.8423375375
1942PhosphorylationEQHRVPSTSRSSPNK
CCCCCCCCCCCCCCC		23.3029899451
1943PhosphorylationQHRVPSTSRSSPNKR
CCCCCCCCCCCCCCC		34.2123375375
1945PhosphorylationRVPSTSRSSPNKRGP
CCCCCCCCCCCCCCC		50.3329899451
1946PhosphorylationVPSTSRSSPNKRGPP
CCCCCCCCCCCCCCC		31.2323384938
1955PhosphorylationNKRGPPTYNEHITKR
CCCCCCCCCHHHHHH		25.07-
1965PhosphorylationHITKRVASSPAPPEG
HHHHHHHCCCCCCCC		33.7225619855
1966PhosphorylationITKRVASSPAPPEGP
HHHHHHCCCCCCCCC		18.4925619855
1974PhosphorylationPAPPEGPSHPREPST
CCCCCCCCCCCCCCC		57.9129899451
1980PhosphorylationPSHPREPSTPHRYRD
CCCCCCCCCCCCCCC		50.2229899451
1981PhosphorylationSHPREPSTPHRYRDR
CCCCCCCCCCCCCCC		33.5525266776
1992PhosphorylationYRDREGRTELRRDKS
CCCCCCCCCCCCCCC		50.67-
1999PhosphorylationTELRRDKSPGRPLER
CCCCCCCCCCCCCCC		36.5526824392
2021PhosphorylationLSTRRERSPGRLFED
CCCCCCCCCCCCCCC		27.2726824392
2029PhosphorylationPGRLFEDSSRGRLPA
CCCCCCCCCCCCCCC		18.1025266776
2030PhosphorylationGRLFEDSSRGRLPAG
CCCCCCCCCCCCCCC		51.5925266776
2041PhosphorylationLPAGAVRTPLSQVNK
CCCCCCCCCHHHHCC		23.22-
2054PhosphorylationNKVWDQSSV------
CCHHCCCCC------		26.6427149854
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1237YPhosphorylationKinaseSRCP12931
PSP
1246YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTRO_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CTRO_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTC3_HUMANTTC3physical
17488780
RHOA_MOUSERhoaphysical
10493740
RAC1_MOUSERac1physical
10493740
CDC42_MOUSECdc42physical
10493740
PCM1_HUMANPCM1physical
26496610
AAPK1_HUMANPRKAA1physical
26496610
GTPB1_HUMANGTPBP1physical
26496610
MOONR_HUMANKIAA0753physical
26496610
KIF14_HUMANKIF14physical
26496610
CP131_HUMANCEP131physical
26496610
CEP72_HUMANCEP72physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTRO_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1608, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1237 AND TYR-1504, ANDMASS SPECTROMETRY.

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