CAMP2_MOUSE - dbPTM
CAMP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAMP2_MOUSE
UniProt AC Q8C1B1
Protein Name Calmodulin-regulated spectrin-associated protein 2 {ECO:0000305}
Gene Name Camsap2 {ECO:0000312|MGI:MGI:1922434}
Organism Mus musculus (Mouse).
Sequence Length 1461
Subcellular Localization Cytoplasm, cytoskeleton . Golgi apparatus . Associated with the minus-end of microtubules and also detected at the centrosomes. Decorates the minus-end of microtubules by decreasing the rate of tubulin incorporation and remaining bound. The length of
Protein Description Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. [PubMed: 23169647 Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (By similarity Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity In addition, it also reduces the velocity of microtubule polymerization (By similarity Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (By similarity Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (By similarity Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (By similarity Through the microtubule cytoskeleton, regulates the autophagosome transport (By similarity]
Protein Sequence MGDAADPREMRRTFIVPAIKPFDHYDFSRAKIACNLAWLVAKAFGTENVPEELGDPFYTDQYDQEHIKPPVVNLLLSAELYCRAGSLILKSDAAKPLLGHDAVIQALAQKGLYVTDQEKLVTERDLHKKPIQMSAHLAMIDTLMMAYTVEMISIEKVIACAQQYSAFFQATDLPYDIEDAVMYWMNKVNEHLKDIMEQEQKSKEHHPAEAPGGQKARYRKEQTLLKQLPCIPLVENLLKDGTDGCALAALIHFYCPAVVRLEDICLKETMSLADSLYNLQLIQEFCQEYLNHCCHFSLEDMLYAASSIKSNYLVFMAELFWWFEVVKPSFVQPRVVRPQGAEPAKDVPSVPVLNAAKRNIRDSSSSSDFSSRYTRPQTHSSASGGIRRSSSMSYVDGFIGTWPKEKRTSVHGVSFDISFDKEDSAQSSTPNRGIIRSVSNEGLTLNNSRASKHIRKNLSFKPVNGEEEESIEEELHVDPHGDLQSPMPLNTNELNSNESTHYKLPNGALQNRVLLDEFGNQIETPSIEEALQIIHDTERPPHTPRPDQIANGFFLHGQDLSILNSNIKLNQSSPDNLTDTKGALSPITDTTEVDTGIHVPSEDIPETMDEDSSLRDYTVSLDSDMDDASKLLQDYDLRASNPREALSPCPSTISTKSQPGSSASSSSGVKMTSFAEQKFRKLNHTDGKSSGSSSQKTTPEGSELNIPHVVSWAQIPEEAGVAPGRDTTQLLASEMVHLRMRLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKKKGEGISPLREEAAGAEDEKVYTDRAKERESQKMDGQRSKSLADIKESMETPPGRWLKSPTTPVDPERQWNLTSPSEETLNEGEILEYTKSIEKLNSSLHFLQQEMQRLSLQQEMLMQMREQQAWVISPPQPSPQKQIRDFKPRQAGLSSAAAPFSSDSPRPTHPSPQSSTRKSASFSVKNQRTPRPNELKITPLNRTLTPPRSVDSLPRLRRFSPSQVPIQTRSFVCFGDDGEPQKEPKQKEEIKKEPSECKGTLGPCDHNPGEKEIKPVESTVSEVLSQPITETVCVTPNEDQLSQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVSVEKLDGESDKEQFDDDQKVCCGFFFKDDQKAENDMAMKRAALLEKRLRREKETQLRKQQLEAEMEHKKEETRRKTEEERQKKEDERARREFIRQEYMRRKQLKLMEDMDTVIKPRPQAAKQKKQRPKSIHRDHIESPKTPIKGPPVSSLSLASLNTGDSESVHSGKRTPRSESVEGFLSPSRCGSRNGEKDWENASTTSSVASGTEYTGPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIGPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKRPVTPKKLLPTKA
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
20UbiquitinationTFIVPAIKPFDHYDF
HEEECCCCCCCCCCH
41.56-
242PhosphorylationENLLKDGTDGCALAA
HHHHCCCCCHHHHHH
39.0822817900
361MethylationNAAKRNIRDSSSSSD
HHHHHCCCCCCCCCC
41.11-
363PhosphorylationAKRNIRDSSSSSDFS
HHHCCCCCCCCCCCH
23.4425521595
365PhosphorylationRNIRDSSSSSDFSSR
HCCCCCCCCCCCHHC
37.5030352176
389PhosphorylationASGGIRRSSSMSYVD
CCCCCCCCCCCCEEC
19.5424925903
390PhosphorylationSGGIRRSSSMSYVDG
CCCCCCCCCCCEECC
28.4024925903
391PhosphorylationGGIRRSSSMSYVDGF
CCCCCCCCCCEECCC
17.0025521595
393PhosphorylationIRRSSSMSYVDGFIG
CCCCCCCCEECCCCC
24.7724925903
394PhosphorylationRRSSSMSYVDGFIGT
CCCCCCCEECCCCCC
8.2324925903
401PhosphorylationYVDGFIGTWPKEKRT
EECCCCCCCCCHHCE
33.5024925903
408PhosphorylationTWPKEKRTSVHGVSF
CCCCHHCEEEEEEEE
46.2829899451
409PhosphorylationWPKEKRTSVHGVSFD
CCCHHCEEEEEEEEE
19.0222324799
414PhosphorylationRTSVHGVSFDISFDK
CEEEEEEEEEEEECC
23.0723375375
418PhosphorylationHGVSFDISFDKEDSA
EEEEEEEEECCCCCC
29.2722817900
429PhosphorylationEDSAQSSTPNRGIIR
CCCCCCCCCCCCCCE
29.8127841257
437PhosphorylationPNRGIIRSVSNEGLT
CCCCCCEEECCCCCE
21.3525521595
439PhosphorylationRGIIRSVSNEGLTLN
CCCCEEECCCCCEEC
30.3425521595
444PhosphorylationSVSNEGLTLNNSRAS
EECCCCCEECCCHHH
37.9925619855
448PhosphorylationEGLTLNNSRASKHIR
CCCEECCCHHHHHHH
28.3125619855
451PhosphorylationTLNNSRASKHIRKNL
EECCCHHHHHHHHCC
24.5329899451
572PhosphorylationSNIKLNQSSPDNLTD
CCCCCCCCCCCCCCC
42.6425521595
573PhosphorylationNIKLNQSSPDNLTDT
CCCCCCCCCCCCCCC
26.8925521595
578PhosphorylationQSSPDNLTDTKGALS
CCCCCCCCCCCCCCC
48.1222324799
580PhosphorylationSPDNLTDTKGALSPI
CCCCCCCCCCCCCCC
26.5820415495
585PhosphorylationTDTKGALSPITDTTE
CCCCCCCCCCCCCCC
17.4525619855
588PhosphorylationKGALSPITDTTEVDT
CCCCCCCCCCCCCCC
30.5825619855
590PhosphorylationALSPITDTTEVDTGI
CCCCCCCCCCCCCCC
19.0625619855
620PhosphorylationSLRDYTVSLDSDMDD
CCCCEEEECCCCCHH
20.7522817900
623PhosphorylationDYTVSLDSDMDDASK
CEEEECCCCCHHHHH
39.8825521595
647PhosphorylationSNPREALSPCPSTIS
CCHHHHHCCCCCCCC
31.3525521595
651PhosphorylationEALSPCPSTISTKSQ
HHHCCCCCCCCCCCC
45.1229899451
652PhosphorylationALSPCPSTISTKSQP
HHCCCCCCCCCCCCC
12.2322817900
654PhosphorylationSPCPSTISTKSQPGS
CCCCCCCCCCCCCCC
29.8522817900
655PhosphorylationPCPSTISTKSQPGSS
CCCCCCCCCCCCCCC
30.7521082442
657PhosphorylationPSTISTKSQPGSSAS
CCCCCCCCCCCCCCC
41.52-
697PhosphorylationSGSSSQKTTPEGSEL
CCCCCCCCCCCCCCC
39.6919060867
711PhosphorylationLNIPHVVSWAQIPEE
CCCCCEEEHHHCCHH
18.6621183079
784PhosphorylationKKKGEGISPLREEAA
ECCCCCCCHHHHHHC
28.8326824392
816PhosphorylationQKMDGQRSKSLADIK
HHCCCCCCCCHHHHH
20.7828066266
818PhosphorylationMDGQRSKSLADIKES
CCCCCCCCHHHHHHH
30.0022324799
825PhosphorylationSLADIKESMETPPGR
CHHHHHHHHCCCCCC
19.5429176673
836PhosphorylationPPGRWLKSPTTPVDP
CCCCCCCCCCCCCCH
25.8825521595
838PhosphorylationGRWLKSPTTPVDPER
CCCCCCCCCCCCHHH
51.3123684622
839PhosphorylationRWLKSPTTPVDPERQ
CCCCCCCCCCCHHHC
25.3821082442
850PhosphorylationPERQWNLTSPSEETL
HHHCCCCCCCCHHHC
35.0623984901
851PhosphorylationERQWNLTSPSEETLN
HHCCCCCCCCHHHCC
29.6020415495
853PhosphorylationQWNLTSPSEETLNEG
CCCCCCCCHHHCCCC
48.0820415495
856PhosphorylationLTSPSEETLNEGEIL
CCCCCHHHCCCCCHH
30.7223984901
905PhosphorylationEQQAWVISPPQPSPQ
HHHCEEECCCCCCHH
22.4025521595
910PhosphorylationVISPPQPSPQKQIRD
EECCCCCCHHHHHCC
34.4125521595
926PhosphorylationKPRQAGLSSAAAPFS
CHHHCCCCCCCCCCC
19.6029472430
927PhosphorylationPRQAGLSSAAAPFSS
HHHCCCCCCCCCCCC
27.2829472430
933PhosphorylationSSAAAPFSSDSPRPT
CCCCCCCCCCCCCCC
31.9828066266
934PhosphorylationSAAAPFSSDSPRPTH
CCCCCCCCCCCCCCC
42.3528066266
936PhosphorylationAAPFSSDSPRPTHPS
CCCCCCCCCCCCCCC
25.4228066266
940PhosphorylationSSDSPRPTHPSPQSS
CCCCCCCCCCCCCCC
47.9328066266
943PhosphorylationSPRPTHPSPQSSTRK
CCCCCCCCCCCCCCC
28.1519060867
946PhosphorylationPTHPSPQSSTRKSAS
CCCCCCCCCCCCCCE
36.7428066266
947PhosphorylationTHPSPQSSTRKSASF
CCCCCCCCCCCCCEE
27.3028066266
948PhosphorylationHPSPQSSTRKSASFS
CCCCCCCCCCCCEEE
47.5728066266
953PhosphorylationSSTRKSASFSVKNQR
CCCCCCCEEEECCCC
25.7529176673
955PhosphorylationTRKSASFSVKNQRTP
CCCCCEEEECCCCCC
29.6829899451
970PhosphorylationRPNELKITPLNRTLT
CCCCCEEECCCCCCC
21.8222871156
975PhosphorylationKITPLNRTLTPPRSV
EEECCCCCCCCCCCC
33.6324759943
977PhosphorylationTPLNRTLTPPRSVDS
ECCCCCCCCCCCCCC
30.5426643407
981PhosphorylationRTLTPPRSVDSLPRL
CCCCCCCCCCCCCCH
35.73-
984PhosphorylationTPPRSVDSLPRLRRF
CCCCCCCCCCCHHCC
37.8125777480
992PhosphorylationLPRLRRFSPSQVPIQ
CCCHHCCCCCCCCCC
23.1025521595
994PhosphorylationRLRRFSPSQVPIQTR
CHHCCCCCCCCCCCC
42.4823684622
1000PhosphorylationPSQVPIQTRSFVCFG
CCCCCCCCCEEEEEC
29.0622705319
1104UbiquitinationEVSLSDLKPPEKADV
EEEHHHCCCCCCCCC
64.61-
1112PhosphorylationPPEKADVSVEKLDGE
CCCCCCCCEEECCCC
25.7125619855
1120PhosphorylationVEKLDGESDKEQFDD
EEECCCCCCHHHCCC
60.5625521595
1208PhosphorylationREFIRQEYMRRKQLK
HHHHHHHHHHHHHHH
6.3829514104
1222PhosphorylationKLMEDMDTVIKPRPQ
HHHHCCHHHHCCCHH
19.9326643407
1240PhosphorylationQKKQRPKSIHRDHIE
HHHCCCCCCCHHHCC
26.7225266776
1248PhosphorylationIHRDHIESPKTPIKG
CCHHHCCCCCCCCCC
30.9725521595
1251PhosphorylationDHIESPKTPIKGPPV
HHCCCCCCCCCCCCC
33.3625521595
1273PhosphorylationLNTGDSESVHSGKRT
CCCCCCCCCCCCCCC
29.1426060331
1276PhosphorylationGDSESVHSGKRTPRS
CCCCCCCCCCCCCCC
43.8029899451
1280PhosphorylationSVHSGKRTPRSESVE
CCCCCCCCCCCCCCC
26.9223984901
1283PhosphorylationSGKRTPRSESVEGFL
CCCCCCCCCCCCCCC
35.1124925903
1285PhosphorylationKRTPRSESVEGFLSP
CCCCCCCCCCCCCCC
27.0724925903
1291PhosphorylationESVEGFLSPSRCGSR
CCCCCCCCCCCCCCC
20.6825521595
1293PhosphorylationVEGFLSPSRCGSRNG
CCCCCCCCCCCCCCC
36.5125521595
1308PhosphorylationEKDWENASTTSSVAS
CCCHHHCCCCCCCCC
43.7423375375
1309PhosphorylationKDWENASTTSSVASG
CCHHHCCCCCCCCCC
28.4323375375
1310PhosphorylationDWENASTTSSVASGT
CHHHCCCCCCCCCCC
19.2623375375
1311PhosphorylationWENASTTSSVASGTE
HHHCCCCCCCCCCCC
23.9323375375
1312PhosphorylationENASTTSSVASGTEY
HHCCCCCCCCCCCCC
21.4323375375
1315PhosphorylationSTTSSVASGTEYTGP
CCCCCCCCCCCCCCC
44.0625521595
1317PhosphorylationTSSVASGTEYTGPKL
CCCCCCCCCCCCCCC
24.2723375375
1407AcetylationIGPKSITKKMIEGLY
CCCHHHHHHHHHHHH
38.3819854219
1408AcetylationGPKSITKKMIEGLYK
CCHHHHHHHHHHHHH
36.1415609651
1452PhosphorylationWQTKRPVTPKKLLPT
HCCCCCCCHHHHCCC
31.8827149854

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

Oops, there are no upstream regulatory protein records of CAMP2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAMP2_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 CAMP2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAMP2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAMP2_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-1291, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1222, AND MASSSPECTROMETRY.

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