CCM2_HUMAN - dbPTM
CCM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCM2_HUMAN
UniProt AC Q9BSQ5
Protein Name Cerebral cavernous malformations 2 protein
Gene Name CCM2
Organism Homo sapiens (Human).
Sequence Length 444
Subcellular Localization Cytoplasm.
Protein Description Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity)..
Protein Sequence MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA
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
6Acetylation--MEEEGKKGKKPGI
--CCCCCCCCCCCCC		62.7312436821
15PhosphorylationGKKPGIVSPFKRVFL
CCCCCCCCCCHHHEE		23.7723401153
27 (in isoform 2)Phosphorylation-41.22-
36 (in isoform 2)Phosphorylation-6.4728122231
65UbiquitinationLLSDYIEKEVKYLGQ
HHHHHHHHHHHHHHH		59.24-
69PhosphorylationYIEKEVKYLGQLTSI
HHHHHHHHHHHHCCC		22.65-
74PhosphorylationVKYLGQLTSIPGYLN
HHHHHHHCCCCCCCC		19.4029978859
75PhosphorylationKYLGQLTSIPGYLNP
HHHHHHCCCCCCCCC		35.0629978859
79PhosphorylationQLTSIPGYLNPSSRT
HHCCCCCCCCCCCCH		9.6529759185
83PhosphorylationIPGYLNPSSRTEILH
CCCCCCCCCCHHHHH		31.2329978859
84PhosphorylationPGYLNPSSRTEILHF
CCCCCCCCCHHHHHH		44.4729978859
96UbiquitinationLHFIDNAKRAHQLPG
HHHHHHHHHHHCCCC		57.27-
157PhosphorylationAHLVVLKTAQDPGIS
CEEEEEEECCCCCCC		25.9522199227
164PhosphorylationTAQDPGISPSQSLCA
ECCCCCCCHHHHHHH		25.1430266825
166PhosphorylationQDPGISPSQSLCAES
CCCCCCHHHHHHHHC		26.1330266825
168PhosphorylationPGISPSQSLCAESSR
CCCCHHHHHHHHCCC		29.7430266825
173PhosphorylationSQSLCAESSRGLSAG
HHHHHHHCCCCCCCC		13.5530108239
174PhosphorylationQSLCAESSRGLSAGS
HHHHHHCCCCCCCCC		23.1330108239
178PhosphorylationAESSRGLSAGSLSES
HHCCCCCCCCCCCCC		33.1528122231
181PhosphorylationSRGLSAGSLSESAVG
CCCCCCCCCCCCCCC		28.5628857561
183PhosphorylationGLSAGSLSESAVGPV
CCCCCCCCCCCCCHH		31.0728634120
185PhosphorylationSAGSLSESAVGPVEA
CCCCCCCCCCCHHHH		25.5228348404
185 (in isoform 2)Phosphorylation-25.5227251275
187 (in isoform 2)Phosphorylation-14.3427251275
206 (in isoform 2)Phosphorylation-17.4927251275
238PhosphorylationRAIFDGASTPTHHLS
HHHHCCCCCCCEECE		40.2129255136
239PhosphorylationAIFDGASTPTHHLSL
HHHCCCCCCCEECEE		31.5023401153
241PhosphorylationFDGASTPTHHLSLHS
HCCCCCCCEECEEEC		23.2429255136
245PhosphorylationSTPTHHLSLHSDDSS
CCCCEECEEECCCCC		21.4923927012
248PhosphorylationTHHLSLHSDDSSTKV
CEECEEECCCCCCCC		48.7023927012
251PhosphorylationLSLHSDDSSTKVDIK
CEEECCCCCCCCEEE		44.9223403867
252PhosphorylationSLHSDDSSTKVDIKE
EEECCCCCCCCEEEE		38.9623403867
253PhosphorylationLHSDDSSTKVDIKET
EECCCCCCCCEEEEE		38.7523403867
259 (in isoform 2)Phosphorylation-57.8827251275
260 (in isoform 2)Phosphorylation-21.7127251275
266 (in isoform 2)Phosphorylation-14.4427251275
273PhosphorylationSTFCFPESVDVGGAS
EEEEEECCCCCCCCC		24.6930108239
280PhosphorylationSVDVGGASPHSKTIS
CCCCCCCCCCCCCCC		26.8125849741
283PhosphorylationVGGASPHSKTISESE
CCCCCCCCCCCCHHH		34.5730108239
285PhosphorylationGASPHSKTISESELS
CCCCCCCCCCHHHHC		32.5226657352
287PhosphorylationSPHSKTISESELSAS
CCCCCCCCHHHHCHH		40.0627732954
289PhosphorylationHSKTISESELSASAT
CCCCCCHHHHCHHHH		36.7328387310
292PhosphorylationTISESELSASATELL
CCCHHHHCHHHHHHH		19.0027732954
294PhosphorylationSESELSASATELLQD
CHHHHCHHHHHHHHH		32.1427732954
296PhosphorylationSELSASATELLQDYM
HHHCHHHHHHHHHHH		25.3527732954
301 (in isoform 2)Phosphorylation-30.6727251275
306 (in isoform 2)Phosphorylation-6.0327251275
315 (in isoform 2)Phosphorylation-2.7827251275
382PhosphorylationKDGRGIITDSFGRHR
CCCCEEEECCCCCCC		24.5429255136
384PhosphorylationGRGIITDSFGRHRRA
CCEEEECCCCCCCCE		22.4319664994
393O-linked_GlycosylationGRHRRALSTTSSSTT
CCCCCEECCCCCCCC		28.7523301498
393PhosphorylationGRHRRALSTTSSSTT
CCCCCEECCCCCCCC		28.7529255136
394PhosphorylationRHRRALSTTSSSTTN
CCCCEECCCCCCCCC		31.3928450419
395PhosphorylationHRRALSTTSSSTTNG
CCCEECCCCCCCCCC		24.2029255136
396PhosphorylationRRALSTTSSSTTNGN
CCEECCCCCCCCCCC		23.5229255136
397PhosphorylationRALSTTSSSTTNGNR
CEECCCCCCCCCCCC		29.6129255136
398PhosphorylationALSTTSSSTTNGNRA
EECCCCCCCCCCCCC		38.7329255136
399PhosphorylationLSTTSSSTTNGNRAT
ECCCCCCCCCCCCCC		26.6529255136
400PhosphorylationSTTSSSTTNGNRATG
CCCCCCCCCCCCCCC		42.9729255136
405 (in isoform 2)Phosphorylation-21.9527251275
406PhosphorylationTTNGNRATGSSDDRS
CCCCCCCCCCCCCCC		34.0725332170
408PhosphorylationNGNRATGSSDDRSAP
CCCCCCCCCCCCCCC		26.6625332170
413PhosphorylationTGSSDDRSAPSEGDE
CCCCCCCCCCCCCCH		52.0728985074
414 (in isoform 2)Phosphorylation-16.7227251275
415 (in isoform 2)Phosphorylation-33.8727251275
416PhosphorylationSDDRSAPSEGDEWDR
CCCCCCCCCCCHHHH		54.6628985074
416 (in isoform 2)Phosphorylation-54.6627251275
429PhosphorylationDRMISDISSDIEALG
HHHHHHHHHHHHHHC		27.2729978859
430PhosphorylationRMISDISSDIEALGC
HHHHHHHHHHHHHCC		42.8329978859
437 (in isoform 2)Phosphorylation-2.9527251275
438PhosphorylationDIEALGCSMDQDSA-
HHHHHCCCCCCCCC-		24.4827732954
443PhosphorylationGCSMDQDSA------
CCCCCCCCC------		30.1930108239
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
384SPhosphorylationKinaseSTK25O00506
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCM2_HUMAN !!
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 CCM2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMUF1_HUMANSMURF1physical
19318350
TWST2_HUMANTWIST2physical
25814554
VTM2L_HUMANVSTM2Lphysical
25814554
KRIT1_HUMANKRIT1physical
25814554
DOK4_HUMANDOK4physical
25814554
KRIT1_HUMANKRIT1physical
28514442
ITBP1_HUMANITGB1BP1physical
28514442
RAD21_HUMANRAD21physical
28514442
UBE3D_HUMANUBE3Dphysical
28514442
DD19B_HUMANDDX19Bphysical
28514442
STK26_HUMANSTK26physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603284Cerebral cavernous malformations 2 (CCM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CCM2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASSSPECTROMETRY.

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